SLC22A5 (OCTN2) is a plasma-membrane, sodium-dependent, high-affinity L-carnitine transporter of the SLC22 organic cation/carnitine transporter family (major facilitator superfamily). It couples the inward movement of one sodium ion to the uptake of one molecule of (R)-carnitine (Km in the low micromolar range), mediating cellular import of carnitine from blood and diet. This uptake is the essential first step that makes carnitine available for the mitochondrial carnitine shuttle (CPT1/CACT/CPT2) and hence for long-chain fatty-acid beta-oxidation, and OCTN2 also drives renal tubular reabsorption of filtered carnitine. Beyond carnitine it is polyspecific, transporting acyl-carnitines, glycine betaine, and diverse organic cations and cationic drugs (e.g. tetraethylammonium), the latter in a lower-affinity, sodium-independent manner. It is an integral multipass membrane protein expressed at the plasma membrane, apical/brush-border in absorptive and reabsorptive epithelia (kidney proximal tubule, intestine, placenta) and at the basal membrane of Sertoli cells. Loss-of-function variants cause systemic primary carnitine deficiency, an autosomal-recessive fatty-acid oxidation disorder presenting with hypoketotic hypoglycemia, cardiomyopathy and skeletal myopathy that is treatable with oral L-carnitine.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetically-inferred plasma-membrane localization. OCTN2 is a well-established integral plasma-membrane transporter, directly demonstrated in multiple systems, so this IBA is correct and represents the site of action. Reason: OCTN2 is an integral plasma-membrane, multipass transporter; extensive experimental evidence (below) confirms plasma-membrane localization and function. Supporting Evidence: PMID:33334877 The carnitine/organic cation transporter novel 2 (OCTN2) is responsible for the cellular uptake of carnitine in most tissues. |
| GO:0015697 quaternary ammonium group transport | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic inference that OCTN2 is involved in quaternary ammonium group transport. Carnitine and many OCTN2 organic-cation substrates are quaternary ammonium compounds, so this is a correct family-level process term, though broader than the specific carnitine transport that is the core function. Reason: Correct but general; OCTN2 does transport quaternary ammonium compounds (carnitine, TEA), but the informative core process is carnitine transmembrane transport. Retained as a valid broader process. Supporting Evidence: PMID:10454528 OCTN2 transports organic cations without involving Na(+), but it transports carnitine only in the presence of Na(+). |
| GO:0015651 quaternary ammonium group transmembrane transporter activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetically-inferred quaternary ammonium group transmembrane transporter activity. OCTN2 transports quaternary ammonium substrates (carnitine, TEA), so the activity is real, but it is broader than the specific carnitine transporter activity that defines the gene. Reason: A valid but general molecular-function term for the family; the specific core MF is carnitine transmembrane transporter activity (GO:0015226). Supporting Evidence: PMID:10454528 novel organic cation transporter (OCTN) 2 is a transporter for organic cations as well as carnitine. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | REMOVE | Summary: Electronic InterPro2GO mapping (IPR045915) assigning ATP binding. OCTN2 is a secondary active transporter that couples carnitine uptake to the sodium electrochemical gradient (Na+ symport); it is not an ATP-driven pump and there is no evidence it binds or hydrolyses ATP. This is a spurious domain-based inference. Reason: OCTN2 is an MFS-family Na+-coupled symporter, not an ATP-binding/ATP-driven transporter. The InterPro-to-GO ATP-binding mapping is biologically incorrect for this protein; no experimental support exists. Supporting Evidence: PMID:10966938 hOCTN2 mediates electrogenic Na(+)-dependent stereoselective high-affinity transport of L-carnitine and Na(+). |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Electronic subcellular-location mapping to endoplasmic reticulum. ER localization applies only to the non-functional splice variant OCTN2VT (isoform 3), which is retained in the ER; the functional transporter is at the plasma membrane. Reason: ER localization is real but pertains to the ER-retained, transport-dead isoform 3 (OCTN2VT); it is not the location of the functional carnitine transporter. Retained as a non-core, isoform-restricted annotation. Supporting Evidence: PMID:17509700 OCTN2VT was retained in the endoplasmic reticulum (ER) with poor N-glycosylation. In addition, the retention in the ER caused no carnitine uptake into the cells. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Electronic subcellular-location mapping to plasma membrane, consistent with the well-established localization of the functional transporter. Reason: Correctly captures the plasma-membrane localization of OCTN2, confirmed experimentally. Supporting Evidence: PMID:33334877 OCTN2 must interact with the surrounding lipid microenvironment to function. |
| GO:0009925 basal plasma membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Electronic annotation of basal plasma membrane localization. OCTN2 is predominantly apical/brush-border in most epithelia but is localized to the basal membrane of Sertoli cells, so a basal-membrane annotation is supportable in specific cell types. Reason: Cell-type-specific basal localization (Sertoli cells) is documented; not the predominant (apical) localization, so kept as non-core. Supporting Evidence: PMID:35307651 OCTN2, multidrug resistance protein (MRP) 3, MRP6, and MRP7 localized to SC basal membranes and peritubular myoid cells (PMCs) |
| GO:0015199 amino-acid betaine transmembrane transporter activity | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Electronic (ARBA) annotation of amino-acid betaine transmembrane transporter activity. OCTN2 does transport glycine betaine, so this is correct; it is a secondary substrate rather than the core carnitine activity. Reason: OCTN2-mediated betaine transport is experimentally documented; a genuine but non-core polyspecific activity. Supporting Evidence: PMID:10966938 hOCTN2 mediated transport of betaine. |
| GO:0015837 amine transport | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Electronic (ARBA) annotation to the broad process amine transport. OCTN2 transports amine-containing organic cations and carnitine, so this is correct but very general. Reason: A correct but broad parent process; the specific process is carnitine transmembrane transport. Supporting Evidence: PMID:10454528 OCTN2 transports organic cations without involving Na(+) |
| GO:0015879 carnitine transport | IEA GO_REF:0000002 | ACCEPT | Summary: Electronic InterPro2GO annotation to carnitine transport, matching the defining physiological role of OCTN2. Reason: Carnitine transport is the core biological process of OCTN2, extensively documented experimentally. Supporting Evidence: PMID:9685390 OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans. |
| GO:0016020 membrane | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Electronic InterPro annotation to the generic term membrane. Correct (OCTN2 is a multipass membrane protein) but uninformative relative to the specific plasma-membrane annotations. Reason: Trivially correct generic location; superseded by the more specific plasma-membrane annotations. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation of apical plasma membrane localization, consistent with the polarized apical/brush-border localization of OCTN2 in epithelia. Reason: Apical localization is directly documented in kidney, intestine, placenta and ocular epithelia; correct. Supporting Evidence: PMID:17274673 an apical membrane expression pattern of OCTN2 in Caki-1 cells was discovered. |
| GO:0022857 transmembrane transporter activity | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Electronic InterPro annotation to the root transmembrane transporter activity term. Correct but maximally general. Reason: Trivially correct high-level MF; the informative MF is carnitine transmembrane transporter activity. Supporting Evidence: PMID:9685390 OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans. |
| GO:0030165 PDZ domain binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Electronic (ARBA) annotation of PDZ domain binding. OCTN2 has a C-terminal PDZ-binding motif that binds the PDZ protein PDZK1, which regulates its transport activity; this is experimentally confirmed (see PMID:15523054 IPI annotation below). Reason: PDZ-domain binding (via the C-terminal motif, to PDZK1) is real and functionally relevant to OCTN2 regulation, but is an accessory regulatory interaction rather than the transporter's core function. Supporting Evidence: PMID:15523054 a requirement of the last four amino acids in OCTN1 and OCTN2 for the interaction |
| GO:0055085 transmembrane transport | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Electronic InterPro annotation to the broad process transmembrane transport. Correct but general. Reason: Correct high-level process; superseded by carnitine transmembrane transport. Supporting Evidence: PMID:9685390 uptake of L-[3H]carnitine was strongly enhanced in a sodium-dependent manner |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MARK AS OVER ANNOTATED | Summary: High-throughput interactome (HuRI/CCSB) interaction, here with HMGCS1. Bare protein binding is uninformative about molecular function and this HT-derived binary interaction has no independent functional validation for OCTN2. Reason: Generic protein binding from a proteome-scale interactome screen; provides no functional insight and the specific interaction (HMGCS1) is not biologically characterized for OCTN2. Per curation guidelines, bare protein binding is not retained as informative. Supporting Evidence: PMID:28514442 Architecture of the human interactome defines protein communities and disease networks |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MARK AS OVER ANNOTATED | Summary: High-throughput binary interactome (HuRI) interactions (with keratins KRT34, KRTAP6-3, MTUS2, NOTCH2NLC and others). Bare protein binding from a large-scale Y2H map, uninformative about OCTN2 molecular function. Reason: Generic protein binding from a proteome-scale interactome map; keratin/keratin- associated-protein partners are common Y2H artifacts and are not biologically validated for OCTN2. Not informative of function. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: High-throughput proteome-scale interactome (BioPlex) interaction, here with HMGCS1. Bare protein binding, uninformative about molecular function. Reason: Generic protein binding from a proteome-scale affinity-purification map; no functional characterization for OCTN2. Not retained as informative. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome |
| GO:0015837 amine transport | TAS Reactome:R-HSA-549127 | KEEP AS NON CORE | Summary: Reactome-asserted involvement in the broad process amine transport (SLC-mediated transport of organic cations). Correct but general; the specific OCTN2 process is carnitine transmembrane transport. Reason: Reactome pathway assertion for a general amine/organic-cation transport process; correct but broader than the specific carnitine function. Supporting Evidence: PMID:10454528 OCTN2 transports organic cations without involving Na(+) |
| GO:1902603 carnitine transmembrane transport | TAS Reactome:R-HSA-165026 | ACCEPT | Summary: Reactome-asserted involvement in carnitine transmembrane transport (OCTN2 transports carnitine from extracellular space to cytosol). This is the core biological process of OCTN2. Reason: Directly captures the defining process; supported by Reactome and by extensive experimental evidence. Supporting Evidence: PMID:9685390 uptake of L-[3H]carnitine was strongly enhanced in a sodium-dependent manner |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:15238359 L-Carnitine transport in human placental brush-border membra... | ACCEPT | Summary: Direct assay of OCTN2-mediated Na+-dependent, high-affinity L-carnitine transport in human placental brush-border membranes. This is the core molecular function of OCTN2. Reason: Experimentally demonstrated carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:15238359 OCTN2, a high-affinity, Na(+)-dependent carnitine transporter, was present in placental BBM |
| GO:1902603 carnitine transmembrane transport | IDA PMID:15238359 L-Carnitine transport in human placental brush-border membra... | ACCEPT | Summary: Direct evidence that OCTN2 mediates L-carnitine transport across the placental brush-border membrane. Core biological process. Reason: Experimentally demonstrated carnitine transmembrane transport; core process. Supporting Evidence: PMID:15238359 l-carnitine uptake was sodium and temperature dependent, showed high affinity for carnitine |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:15523054 PDZK1 directly regulates the function of organic cation/carn... | ACCEPT | Summary: OCTN2-mediated carnitine uptake measured directly (and shown to be stimulated ~6-fold by PDZK1 co-expression). Confirms carnitine transporter activity. Reason: Direct assay of OCTN2 carnitine transport activity; core molecular function. Supporting Evidence: PMID:15523054 double transfection of OCTN2 with PDZK1 stimulated the uptake by OCTN2 of its endogenous substrate carnitine |
| GO:1902603 carnitine transmembrane transport | IDA PMID:15523054 PDZK1 directly regulates the function of organic cation/carn... | ACCEPT | Summary: Direct evidence of OCTN2-mediated carnitine transport (endogenous substrate carnitine), core biological process. Reason: Experimentally demonstrated carnitine transmembrane transport; core process. Supporting Evidence: PMID:15523054 the uptake by OCTN2 of its endogenous substrate carnitine |
| GO:0005783 endoplasmic reticulum | EXP PMID:17509700 OCTN2VT, a splice variant of OCTN2, does not transport carni... | KEEP AS NON CORE | Summary: Experimental demonstration of ER localization for the OCTN2VT splice variant (isoform 3), which is ER-retained and unable to transport carnitine. This is an isoform-specific, non-functional location. Reason: ER localization is genuine but restricted to the transport-dead isoform 3 (OCTN2VT); it does not describe the functional transporter's location. Kept as isoform-specific non-core. Supporting Evidence: PMID:17509700 OCTN2VT was retained in the endoplasmic reticulum (ER) with poor N-glycosylation. |
| GO:0005886 plasma membrane | EXP PMID:33334877 Cholesterol stimulates the cellular uptake of L-carnitine by... | ACCEPT | Summary: Experimental plasma-membrane localization of functional OCTN2 (HEK293 cells overexpressing OCTN2; cholesterol modulation studies). Core localization. Reason: Directly documented plasma-membrane localization of the active transporter. Supporting Evidence: PMID:33334877 how plasma membrane cholesterol modulates OCTN2 transport of L-carnitine |
| GO:0016324 apical plasma membrane | EXP PMID:10966938 Functional and pharmacological characterization of human Na(... | ACCEPT | Summary: Functional/pharmacological characterization of hOCTN2 as an electrogenic Na+-carnitine cotransporter; UniProt records apical cell-membrane localization from this work. Apical localization is well-supported across epithelia. Reason: Apical plasma-membrane localization of OCTN2 is documented here and in multiple epithelial systems; correct. Supporting Evidence: PMID:10966938 hOCTN2 mediates electrogenic Na(+)-dependent stereoselective high-affinity transport of L-carnitine and Na(+). |
| GO:0015199 amino-acid betaine transmembrane transporter activity | IDA PMID:33124720 Deorphaning a solute carrier 22 family member, SLC22A15, thr... | KEEP AS NON CORE | Summary: OCTN2 is used here as a reference zwitterion transporter and its betaine/dimethylglycine transport is noted; UniProt records betaine and N,N-dimethylglycine as OCTN2 substrates. Betaine transport by OCTN2 was demonstrated experimentally in PMID:10966938. Reason: OCTN2-mediated betaine (and dimethylglycine) transport is a genuine but secondary polyspecific activity; not the core carnitine function. Supporting Evidence: PMID:33124720 Dimethylglycine, known to interact with SLC22A5 PMID:10966938 hOCTN2 mediated transport of betaine. |
| GO:0034341 response to type II interferon | IDA PMID:20722056 Cytokine regulation of OCTN2 expression and activity in smal... | KEEP AS NON CORE | Summary: Intestinal OCTN2 expression and Na+-dependent carnitine uptake activity are increased by IFN-gamma. This is a regulatory response (OCTN2 is induced by the cytokine), not a core transporter function. Reason: OCTN2 responds to (is induced by) IFN-gamma in intestine; a genuine but peripheral/regulatory biological process rather than the transporter's core function. Supporting Evidence: PMID:20722056 IFN-Ξ³ increased both total and apical membrane expression of Caco2BBE OCTN2 |
| GO:0034612 response to tumor necrosis factor | IDA PMID:20722056 Cytokine regulation of OCTN2 expression and activity in smal... | KEEP AS NON CORE | Summary: Intestinal OCTN2 apical membrane expression and carnitine uptake are increased by TNF-alpha. A regulatory/response process, not core transport function. Reason: OCTN2 responds to (is regulated by) TNF; peripheral regulatory process. Supporting Evidence: PMID:20722056 TNF-Ξ± stimulated apical expression |
| GO:1900749 (R)-carnitine transport | IDA PMID:20722056 Cytokine regulation of OCTN2 expression and activity in smal... | ACCEPT | Summary: Na+-dependent 3H-carnitine uptake by OCTN2 measured directly in intestinal epithelial cells (siRNA-confirmed as OCTN2-dependent). Core carnitine transport process. Reason: Directly demonstrated OCTN2-mediated (R)-carnitine transport; core process. Supporting Evidence: PMID:20722056 more than 80% of Na+-dependent carnitine uptake is due to OCTN2 in Caco2BBE cells |
| GO:1901235 (R)-carnitine transmembrane transporter activity | IDA PMID:20722056 Cytokine regulation of OCTN2 expression and activity in smal... | ACCEPT | Summary: OCTN2-mediated Na+-dependent (R)-carnitine transporter activity demonstrated directly (siRNA knockdown abolishes >80% of Na+-dependent uptake). Core molecular function at the specific substrate level. Reason: Direct evidence of (R)-carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:20722056 The Na+-dependent 3H-carnitine uptake in cells treated with OCTN2 siRNA was reduced from 0.88 Β± 0.10 to 0.16 Β± 0.06 |
| GO:0009925 basal plasma membrane | IDA PMID:35307651 Localization of Xenobiotic Transporters Expressed at the Hum... | KEEP AS NON CORE | Summary: Immunohistological localization of OCTN2 to Sertoli-cell basal membranes and peritubular myoid cells at the human blood-testis barrier. Cell-type-specific basal localization. Reason: Documented basal-membrane localization in specific testicular cell types; not the predominant apical localization, so non-core. Supporting Evidence: PMID:35307651 OCTN2, multidrug resistance protein (MRP) 3, MRP6, and MRP7 localized to SC basal membranes and peritubular myoid cells (PMCs) |
| GO:0005886 plasma membrane | IDA PMID:17509700 OCTN2VT, a splice variant of OCTN2, does not transport carni... | ACCEPT | Summary: Functional OCTN2 shown at the plasma membrane (with robust N-glycosylation), contrasted with the ER-retained OCTN2VT variant. Core localization. Reason: Direct plasma-membrane localization of the functional transporter. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:0016324 apical plasma membrane | IDA PMID:18005709 The Bacillus subtilis quorum-sensing molecule CSF contribute... | ACCEPT | Summary: OCTN2 identified as an apical membrane organic cation transporter in intestinal epithelial cells, mediating uptake of the bacterial CSF pentapeptide. Apical localization is the site of action in absorptive epithelia. Reason: Apical plasma-membrane site of action directly demonstrated in intestinal epithelia. Supporting Evidence: PMID:18005709 These effects of CSF depend on its uptake by an apical membrane organic cation transporter-2 (OCTN2). |
| GO:0016324 apical plasma membrane | IDA PMID:20722056 Cytokine regulation of OCTN2 expression and activity in smal... | ACCEPT | Summary: OCTN2 localized to the apical (brush-border) membrane of intestinal epithelial cells by immunohistochemistry and surface biotinylation. Core polarized localization. Reason: Directly documented apical plasma-membrane localization in intestine. Supporting Evidence: PMID:20722056 OCTN2 was highly expressed in the brush border (apical membrane) and subapical region of epithelial cells |
| GO:0022857 transmembrane transporter activity | IDA PMID:18005709 The Bacillus subtilis quorum-sensing molecule CSF contribute... | KEEP AS NON CORE | Summary: OCTN2 demonstrated to transport the bacterial CSF pentapeptide across the apical membrane. This supports transmembrane transporter activity, though the annotation uses the maximally general MF term. Reason: Correct but general MF; the specific informative MF is carnitine transmembrane transporter activity. Retained as a valid broader term. Supporting Evidence: PMID:18005709 OCTN2-mediated CSF transport serves as an example of a host-bacterial interaction |
| GO:0070715 sodium-dependent organic cation transport | IDA PMID:18005709 The Bacillus subtilis quorum-sensing molecule CSF contribute... | KEEP AS NON CORE | Summary: OCTN2-mediated apical uptake of the cationic bacterial pentapeptide CSF; UniProt records this as a Na+-coupled transport reaction. Supports Na+-dependent organic cation (peptide) transport. Reason: A genuine polyspecific Na+-dependent organic-cation transport activity (CSF peptide), distinct from the core carnitine function; retained as non-core. Supporting Evidence: PMID:18005709 These effects of CSF depend on its uptake by an apical membrane organic cation transporter-2 (OCTN2). |
| GO:1900749 (R)-carnitine transport | IDA PMID:17509700 OCTN2VT, a splice variant of OCTN2, does not transport carni... | ACCEPT | Summary: OCTN2 shown to be indispensable for carnitine transport across the plasma membrane (the functional variant transports carnitine, the ER-retained variant does not). Core carnitine transport process. Reason: Direct evidence for OCTN2-mediated (R)-carnitine transport; core process. Supporting Evidence: PMID:17509700 A novel organic cation transporter OCTN2 is indispensable for carnitine transport across plasma membrane |
| GO:1900749 (R)-carnitine transport | IDA PMID:33334877 Cholesterol stimulates the cellular uptake of L-carnitine by... | ACCEPT | Summary: OCTN2 responsible for cellular uptake of carnitine; carnitine transport measured directly in OCTN2-overexpressing cells (and shown to be cholesterol- dependent). Core carnitine transport process. Reason: Direct evidence for OCTN2-mediated carnitine uptake; core process. Supporting Evidence: PMID:33334877 The carnitine/organic cation transporter novel 2 (OCTN2) is responsible for the cellular uptake of carnitine in most tissues. |
| GO:1901235 (R)-carnitine transmembrane transporter activity | IDA PMID:17509700 OCTN2VT, a splice variant of OCTN2, does not transport carni... | ACCEPT | Summary: OCTN2 (functional isoform) transports carnitine across the plasma membrane; the ER-retained OCTN2VT does not, confirming that plasma-membrane OCTN2 is the carnitine transporter. Core molecular function. Reason: Direct evidence for (R)-carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:17509700 the retention in the ER caused no carnitine uptake into the cells |
| GO:1901235 (R)-carnitine transmembrane transporter activity | IDA PMID:33334877 Cholesterol stimulates the cellular uptake of L-carnitine by... | ACCEPT | Summary: Direct carnitine transport assays in OCTN2-overexpressing HEK293 cells establish OCTN2 (R)-carnitine transporter activity (modulated by membrane cholesterol). Core molecular function. Reason: Direct evidence for (R)-carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:33334877 how plasma membrane cholesterol modulates OCTN2 transport of L-carnitine |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:10454528 Functional characteristics and tissue distribution pattern o... | ACCEPT | Summary: Functional characterization establishing OCTN2 as a Na+-dependent carnitine transporter (and Na+-independent organic cation transporter). Core molecular function. Reason: Direct experimental demonstration of carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:10454528 it transports carnitine only in the presence of Na(+) |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:10966938 Functional and pharmacological characterization of human Na(... | ACCEPT | Summary: Electrophysiological and flux characterization of hOCTN2 as an electrogenic Na+-carnitine cotransporter (Km ~4.8 uM). Core molecular function. Reason: Direct evidence for high-affinity carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:10966938 hOCTN2 mediates electrogenic Na(+)-dependent stereoselective high-affinity transport of L-carnitine and Na(+). |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:17855766 Transport of butyryl-L-carnitine, a potential prodrug, via t... | ACCEPT | Summary: OCTN2 transports L-carnitine and its butyryl ester (butyryl-L-carnitine) as a high-affinity transporter. Confirms carnitine transporter activity. Reason: Direct evidence of OCTN2 carnitine (and acyl-carnitine) transport activity; core molecular function. Supporting Evidence: PMID:17855766 OCTN2 is a high-affinity/low-capacity transporter |
| GO:0015651 quaternary ammonium group transmembrane transporter activity | IMP PMID:10454528 Functional characteristics and tissue distribution pattern o... | KEEP AS NON CORE | Summary: OCTN2 transports quaternary ammonium substrates (carnitine, organic cations); loss-of-function mutants (M352R, P478L) abolish transport. Correct family-level MF, broader than the specific carnitine activity. Reason: A correct but general quaternary ammonium transporter activity; the specific core MF is carnitine transmembrane transporter activity. Supporting Evidence: PMID:10454528 Two mutations, M352R and P478L, in human OCTN2 are associated with loss of transport function |
| GO:0015651 quaternary ammonium group transmembrane transporter activity | IMP PMID:10966938 Functional and pharmacological characterization of human Na(... | KEEP AS NON CORE | Summary: hOCTN2 transports carnitine and betaine (quaternary ammonium compounds); shows only small currents with classic OCT substrates. Correct but general MF. Reason: Correct family-level quaternary-ammonium MF; superseded by the specific carnitine transporter activity as the core function. Supporting Evidence: PMID:10966938 hOCTN2 mediated transport of betaine. |
| GO:0015697 quaternary ammonium group transport | IMP PMID:10454528 Functional characteristics and tissue distribution pattern o... | KEEP AS NON CORE | Summary: OCTN2 mediates transport of quaternary ammonium compounds (carnitine and organic cations); mutation studies confirm transport function. Correct but broad process. Reason: Correct but general process; the specific process is carnitine transmembrane transport. Supporting Evidence: PMID:10454528 OCTN2 transports organic cations without involving Na(+) |
| GO:0015697 quaternary ammonium group transport | IMP PMID:10966938 Functional and pharmacological characterization of human Na(... | KEEP AS NON CORE | Summary: hOCTN2 transports the quaternary ammonium compounds carnitine and betaine. Correct but broad process term. Reason: Correct general process; superseded by carnitine transmembrane transport. Supporting Evidence: PMID:10966938 hOCTN2 mediated transport of betaine. |
| GO:1902270 (R)-carnitine transmembrane transport | IDA PMID:10454528 Functional characteristics and tissue distribution pattern o... | ACCEPT | Summary: Direct demonstration that OCTN2 transports carnitine (Na+-dependently) across the membrane. Core carnitine transport process at the specific substrate level. Reason: Direct evidence for (R)-carnitine transmembrane transport; core process. Supporting Evidence: PMID:10454528 it transports carnitine only in the presence of Na(+) |
| GO:1902270 (R)-carnitine transmembrane transport | IDA PMID:10966938 Functional and pharmacological characterization of human Na(... | ACCEPT | Summary: Electrogenic Na+-dependent L-carnitine transport by hOCTN2 characterized by voltage clamp/flux. Core carnitine transport process. Reason: Direct evidence for (R)-carnitine transmembrane transport; core process. Supporting Evidence: PMID:10966938 L-carnitine transport was electrogenic. |
| GO:1902270 (R)-carnitine transmembrane transport | IDA PMID:17855766 Transport of butyryl-L-carnitine, a potential prodrug, via t... | ACCEPT | Summary: OCTN2 transports L-carnitine (and butyryl-L-carnitine) in an electrogenic, Na+-dependent manner. Core carnitine transport process. Reason: Direct evidence for (R)-carnitine transmembrane transport; core process. Supporting Evidence: PMID:17855766 Transport of BC via OCTN2 is electrogenic |
| GO:1901235 (R)-carnitine transmembrane transporter activity | IMP PMID:23877104 Functional expression of organic cation/carnitine transporte... | ACCEPT | Summary: OCTN2 gene silencing dramatically suppresses Na+-dependent L-carnitine uptake in human brain capillary endothelial cells, demonstrating OCTN2 (R)-carnitine transporter activity. Core molecular function. Reason: siRNA knockdown directly implicates OCTN2 in (R)-carnitine transporter activity; core molecular function. Supporting Evidence: PMID:23877104 [(3)H]L-Carnitine uptake was dramatically suppressed by silencing of the OCTN2 gene. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | REMOVE | Summary: Sequence-similarity transfer (from mouse Octn2, O70594) of a cytoplasm annotation. OCTN2 is an integral multipass plasma-membrane transporter; a bulk cytoplasm localization does not describe its functional location and is a likely mislocalization/over-annotation. Reason: OCTN2 is an integral membrane protein resident in the plasma membrane (and ER for the non-functional isoform); a generic cytoplasm location is not supported and is misleading. This ISS is an over-annotation. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:1901235 (R)-carnitine transmembrane transporter activity | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer (from mouse Octn2) of (R)-carnitine transporter activity. Consistent with the directly demonstrated human OCTN2 function. Reason: ISS from mouse ortholog matches the extensive direct human evidence for (R)-carnitine transmembrane transporter activity; core molecular function. Supporting Evidence: PMID:10966938 high-affinity transport of L-carnitine and Na(+). |
| GO:1902270 (R)-carnitine transmembrane transport | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer (from mouse Octn2) of (R)-carnitine transmembrane transport. Consistent with the directly demonstrated human process. Reason: ISS matches abundant direct human evidence for (R)-carnitine transmembrane transport; core process. Supporting Evidence: PMID:10454528 it transports carnitine only in the presence of Na(+) |
| GO:0015226 carnitine transmembrane transporter activity | EXP PMID:9685390 Molecular and functional identification of sodium ion-depend... | ACCEPT | Summary: Original molecular/functional identification of OCTN2 as a high-affinity, Na+-dependent carnitine transporter (Km 4.34 uM). Foundational evidence for the core molecular function. Reason: Direct experimental identification of OCTN2 carnitine transporter activity; core molecular function. Supporting Evidence: PMID:9685390 uptake of L-[3H]carnitine was strongly enhanced in a sodium-dependent manner with Km value of 4.34 microM |
| GO:0015226 carnitine transmembrane transporter activity | TAS Reactome:R-HSA-549297 | ACCEPT | Summary: Reactome assertion that SLC22A5 (with SLC22A4/15/16) cotransports carnitine and Na+ from extracellular region to cytosol. Core molecular function. Reason: Reactome pathway assertion matching the well-established core carnitine transporter activity. Supporting Evidence: PMID:9685390 OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans. |
| GO:0015226 carnitine transmembrane transporter activity | TAS Reactome:R-HSA-5625674 | ACCEPT | Summary: Reactome assertion (defective SLC22A5 does not cotransport carnitine/Na+) referencing the normal carnitine transporter activity of OCTN2. Core molecular function. Reason: Reactome pathway assertion consistent with the established core carnitine transporter activity (and its loss in disease). Supporting Evidence: PMID:9916797 loss of OCTN2 function causes SCD |
| GO:0005829 cytosol | ISS GO_REF:0000024 | REMOVE | Summary: Sequence-similarity transfer (from mouse Octn2) of a cytosol annotation. As with the cytoplasm annotation, OCTN2 is an integral plasma-membrane protein; a cytosol localization is not supported. Reason: OCTN2 is an integral membrane transporter, not a cytosolic/soluble protein; the ISS cytosol annotation is a mislocalization/over-annotation. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:0005886 plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer (from mouse Octn2) of plasma-membrane localization, consistent with the direct human evidence. Core localization. Reason: ISS matches abundant direct evidence for plasma-membrane localization of OCTN2. Supporting Evidence: PMID:33334877 OCTN2 must interact with the surrounding lipid microenvironment to function. |
| GO:0150104 transport across blood-brain barrier | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Sequence-similarity transfer (from rat Octn2, Q9Z0E8) of a role in transport across the blood-brain barrier. OCTN2 is functionally expressed at the human BBB and mediates L-carnitine uptake there (confirmed by siRNA in PMID:23877104). Reason: OCTN2 contributes to carnitine transport at the blood-brain barrier, a tissue-specific manifestation of its core carnitine transport function rather than a distinct core process. Supporting Evidence: PMID:23877104 OCTN2 is involved in L-carnitine transport at the human BBB. |
| GO:1902270 (R)-carnitine transmembrane transport | IMP PMID:23877104 Functional expression of organic cation/carnitine transporte... | ACCEPT | Summary: OCTN2 gene silencing suppresses Na+-dependent L-carnitine uptake in human brain endothelial cells, implicating OCTN2 in (R)-carnitine transmembrane transport. Core carnitine transport process. Reason: siRNA knockdown directly implicates OCTN2 in (R)-carnitine transmembrane transport; core process. Supporting Evidence: PMID:23877104 [(3)H]L-Carnitine uptake was dramatically suppressed by silencing of the OCTN2 gene. |
| GO:0015651 quaternary ammonium group transmembrane transporter activity | IDA PMID:23567998 Transport of gabapentin by LAT1 (SLC7A5). | UNDECIDED | Summary: This paper concerns gabapentin transport by LAT1 (SLC7A5) at the blood-brain barrier; its abstract characterizes LAT1 and reports that gabapentin was negative for OCT-like transport. The cached abstract does not document an OCTN2/quaternary-ammonium transport assay, and the full text is unavailable, so the basis of the ARUK-UCL IDA annotation to OCTN2 cannot be verified from the cache. Reason: Cannot verify the OCTN2-specific supporting evidence from the abstract-only cache (the paper foregrounds LAT1); per curation policy, an experimental annotation whose full text I cannot read is left UNDECIDED rather than removed. Supporting Evidence: PMID:23567998 Gabapentin was negative for OCT like transport and LAT2 activity |
| GO:0015697 quaternary ammonium group transport | IDA PMID:23567998 Transport of gabapentin by LAT1 (SLC7A5). | UNDECIDED | Summary: As above (PMID:23567998, gabapentin/LAT1). The cached abstract does not document an OCTN2 quaternary-ammonium transport assay; full text unavailable. Reason: The OCTN2-specific evidence cannot be verified from the abstract-only cache; left UNDECIDED rather than removed per policy on experimental annotations. Supporting Evidence: PMID:23567998 Gabapentin was negative for OCT like transport and LAT2 activity |
| GO:0150104 transport across blood-brain barrier | NAS PMID:30280653 Blood-Brain Barrier: From Physiology to Disease and Back. | KEEP AS NON CORE | Summary: Non-traceable author-statement annotation citing a general blood-brain- barrier review. The specific functional evidence for OCTN2 at the BBB comes from the experimental PMID:23877104; this NAS from a review is weak support. Reason: A weak (NAS, from a review) restatement of OCTN2's tissue-specific BBB carnitine-transport role; kept as non-core, with the experimental evidence provided by PMID:23877104. Supporting Evidence: PMID:23877104 OCTN2 is involved in L-carnitine transport at the human BBB. |
| GO:0150104 transport across blood-brain barrier | NAS PMID:26590417 Establishment and Dysfunction of the Blood-Brain Barrier. | KEEP AS NON CORE | Summary: Non-traceable author-statement annotation citing a general blood-brain- barrier review. Weak support; the functional OCTN2 BBB evidence is experimental (PMID:23877104). Reason: Weak (NAS, review-based) restatement of the tissue-specific BBB carnitine- transport role; non-core. Supporting Evidence: PMID:23877104 OCTN2 is involved in L-carnitine transport at the human BBB. |
| GO:0009609 response to symbiotic bacterium | IMP PMID:18005709 The Bacillus subtilis quorum-sensing molecule CSF contribute... | KEEP AS NON CORE | Summary: OCTN2-dependent uptake of the Bacillus subtilis quorum-sensing peptide CSF in intestinal epithelia links the transporter to host responses to commensal bacteria. A downstream, tissue-specific biology of OCTN2's cationic- peptide transport, not a core transporter function. Reason: Genuine but peripheral role (mediating uptake of a bacterial signaling peptide) downstream of OCTN2's transport activity; non-core. Supporting Evidence: PMID:18005709 OCTN2-mediated CSF transport serves as an example of a host-bacterial interaction that allows the host to monitor and respond to changes in the behavior or composition of colonic flora. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5625674 | ACCEPT | Summary: Reactome-asserted plasma-membrane localization of SLC22A5. Consistent with the established core localization. Reason: Reactome pathway assertion matching well-established plasma-membrane localization. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | MARK AS OVER ANNOTATED | Summary: High-throughput proteomic detection of OCTN2 among proteins in human urinary exosomes. Incidental proteomic co-purification (renal epithelial membrane proteins are commonly recovered in urinary exosomes); not a functional subcellular location. Reason: Exosome detection is a mass-spectrometry co-occurrence consistent with shedding of apical renal membrane proteins; it does not indicate a functional exosomal role and over-annotates the localization. Supporting Evidence: PMID:19056867 Normal human urine contains large numbers of exosomes |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-165026 | ACCEPT | Summary: Reactome-asserted plasma-membrane localization of SLC22A5 (in the carnitine transport reaction). Consistent with core localization. Reason: Reactome assertion matching established plasma-membrane localization. Supporting Evidence: PMID:33334877 OCTN2 must interact with the surrounding lipid microenvironment to function. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-549297 | ACCEPT | Summary: Reactome-asserted plasma-membrane localization of SLC22A5 (in the carnitine/Na+ cotransport reaction). Consistent with core localization. Reason: Reactome assertion matching established plasma-membrane localization. Supporting Evidence: PMID:17509700 OCTN2 was expressed on the plasma membrane with robust N-glycosylation |
| GO:0060731 positive regulation of intestinal epithelial structure maintenance | IMP PMID:18005709 The Bacillus subtilis quorum-sensing molecule CSF contribute... | KEEP AS NON CORE | Summary: OCTN2-mediated uptake of the bacterial CSF peptide induces cytoprotective heat shock proteins that prevent oxidant-induced intestinal epithelial injury and loss of barrier function, linking OCTN2 to intestinal homeostasis. A downstream, tissue-specific process rather than a core transporter function. Reason: Genuine but peripheral physiological consequence of OCTN2 cationic-peptide transport in the intestine; non-core. Supporting Evidence: PMID:18005709 CSF also induces cytoprotective heat shock proteins (Hsps), which prevent oxidant-induced intestinal epithelial cell injury and loss of barrier function. |
| GO:0070715 sodium-dependent organic cation transport | IDA PMID:15238359 L-Carnitine transport in human placental brush-border membra... | ACCEPT | Summary: OCTN2-mediated Na+-dependent, high-affinity L-carnitine uptake in placental brush-border membranes. Carnitine is a zwitterionic organic cation; this Na+-dependent organic-cation transport is essentially the core carnitine uptake function. Reason: Directly demonstrated Na+-dependent organic-cation (carnitine) transport by OCTN2; reflects the core function. Supporting Evidence: PMID:15238359 l-carnitine uptake was sodium and temperature dependent |
| GO:0070715 sodium-dependent organic cation transport | IDA PMID:9685390 Molecular and functional identification of sodium ion-depend... | ACCEPT | Summary: OCTN2 characterized as a sodium-dependent high-affinity carnitine (zwitterionic organic cation) transporter. Reflects the core Na+-coupled transport mechanism. Reason: Directly demonstrated Na+-dependent organic-cation (carnitine) transport; reflects the core function/mechanism. Supporting Evidence: PMID:9685390 OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans. |
| GO:0005515 protein binding | IPI PMID:15523054 PDZK1 directly regulates the function of organic cation/carn... | MARK AS OVER ANNOTATED | Summary: OCTN2 binds the PDZ scaffolding protein PDZK1 (interaction data). While recorded as generic protein binding, this specific interaction is functionally important (PDZK1 stimulates OCTN2 carnitine transport). The informative capture is the PDZ-domain-binding annotation (GO:0030165) from the same study. Reason: Bare protein binding is uninformative per curation guidelines; the biologically meaningful content (binding PDZK1 via a PDZ motif) is better captured by the PDZ domain binding annotation from the same reference. Supporting Evidence: PMID:15523054 The present findings are the first to identify PDZK1 as a functional regulator of OCTN2 through direct interaction with the C terminus. |
| GO:0005886 plasma membrane | IC PMID:9618255 cDNA sequence, transport function, and genomic organization ... | ACCEPT | Summary: Plasma-membrane localization inferred by the curator from the demonstrated transport function (OCTN2 mediates TEA transport when expressed in HeLa cells). Consistent with the established core localization. Reason: Plasma-membrane localization inferred from surface transport function and confirmed by later direct evidence; correct. Supporting Evidence: PMID:9618255 OCTN2 mediates the transport of tetraethylammonium, a prototypical organic cation, in a pH-dependent manner. |
| GO:0015226 carnitine transmembrane transporter activity | IDA PMID:9685390 Molecular and functional identification of sodium ion-depend... | ACCEPT | Summary: Original identification of OCTN2 as a high-affinity Na+-dependent carnitine transporter. Core molecular function. Reason: Direct experimental demonstration of carnitine transporter activity; core molecular function. Supporting Evidence: PMID:9685390 uptake of L-[3H]carnitine was strongly enhanced in a sodium-dependent manner with Km value of 4.34 microM |
| GO:0015226 carnitine transmembrane transporter activity | IMP PMID:9916797 Primary systemic carnitine deficiency is caused by mutations... | ACCEPT | Summary: Mutational evidence that loss of OCTN2 function causes systemic carnitine deficiency (jvs mouse mutation abrogates carnitine transport; human SLC22A5 mutations in SCD pedigrees). Confirms OCTN2 carnitine transporter activity via loss-of-function. Core molecular function. Reason: Loss-of-function (disease/mutation) evidence directly supports carnitine transporter activity; core molecular function. Supporting Evidence: PMID:9916797 this mutation abrogates carnitine transport. |
| GO:0015651 quaternary ammonium group transmembrane transporter activity | IDA PMID:9618255 cDNA sequence, transport function, and genomic organization ... | KEEP AS NON CORE | Summary: OCTN2 mediates transport of the quaternary ammonium compound tetraethylammonium (TEA) in a pH-dependent manner when expressed in HeLa cells. Correct family-level MF, broader than the specific carnitine activity. Reason: Genuine quaternary-ammonium (organic cation) transporter activity, but the informative core MF is carnitine transmembrane transporter activity. Supporting Evidence: PMID:9618255 OCTN2 mediates the transport of tetraethylammonium, a prototypical organic cation, in a pH-dependent manner. |
| GO:0015697 quaternary ammonium group transport | IDA PMID:9618255 cDNA sequence, transport function, and genomic organization ... | KEEP AS NON CORE | Summary: OCTN2 transports the quaternary ammonium organic cation TEA (and competing organic cations MPP+, MPTP, methamphetamine). Correct but broad process. Reason: Correct but general organic-cation transport process; the specific process is carnitine transmembrane transport. Supporting Evidence: PMID:9618255 Several organic cations, including the neurotoxins 1-methyl-4-phenylpyridinium |
| GO:0015879 carnitine transport | IDA PMID:9685390 Molecular and functional identification of sodium ion-depend... | ACCEPT | Summary: OCTN2 identified as the physiologically important high-affinity Na+-carnitine cotransporter. Core carnitine transport process. Reason: Direct evidence of OCTN2-mediated carnitine transport; core process. Supporting Evidence: PMID:9685390 OCTN2 is a physiologically important, high affinity sodium-carnitine cotransporter in humans. |
| GO:0015879 carnitine transport | IMP PMID:9916797 Primary systemic carnitine deficiency is caused by mutations... | ACCEPT | Summary: Loss-of-function OCTN2 mutations abrogate carnitine transport and cause systemic carnitine deficiency, confirming OCTN2's role in carnitine transport. Core process. Reason: Mutation/disease evidence directly supports OCTN2 involvement in carnitine transport; core process. Supporting Evidence: PMID:9916797 this mutation abrogates carnitine transport. |
| GO:0016324 apical plasma membrane | IDA PMID:17274673 OCTN2-mediated carnitine uptake in a newly discovered human ... | ACCEPT | Summary: OCTN2 localized to the apical membrane of the human proximal tubule cell line Caki-1, where it mediates carnitine reabsorption. Core polarized localization in kidney. Reason: Directly documented apical plasma-membrane localization in proximal tubule cells; correct. Supporting Evidence: PMID:17274673 an apical membrane expression pattern of OCTN2 in Caki-1 cells was discovered. |
| GO:0016324 apical plasma membrane | IDA PMID:18641280 Expression and localization of carnitine/organic cation tran... | ACCEPT | Summary: OCTN2 predominantly localized to the apical membranes of human corneal and conjunctival epithelial cells, with apical L-carnitine uptake. Apical localization consistent across epithelia. Reason: Directly documented apical plasma-membrane localization in ocular epithelia; correct. Supporting Evidence: PMID:18641280 OCTN1 and OCTN2 were predominately localized in the apical membranes of the cells. |
| GO:0030165 PDZ domain binding | IPI PMID:15523054 PDZK1 directly regulates the function of organic cation/carn... | KEEP AS NON CORE | Summary: The OCTN2 C-terminal PDZ-binding motif (last four residues) binds the PDZ protein PDZK1 (and NHERF2), and PDZK1 co-expression stimulates OCTN2 carnitine transport capacity ~6-fold. An informative, functionally relevant molecular function (accessory regulatory interaction). Reason: A specific, biologically meaningful protein-domain interaction that regulates OCTN2 transport; retained as an informative non-core molecular function (the core MF remains carnitine transport). Supporting Evidence: PMID:15523054 a specific interaction of apical transporters OCTN1 and OCTN2, but not basolateral transporters OCT1 and OCT2, with PDZK1 |
| GO:0031526 brush border membrane | IDA PMID:15238359 L-Carnitine transport in human placental brush-border membra... | ACCEPT | Summary: OCTN2 detected by Western blot in placental brush-border (but not basal) membrane vesicles. Brush-border (apical) localization consistent with the transporter's polarized reabsorptive/absorptive role. Reason: Directly documented brush-border membrane localization; correct and informative (specific apical sub-localization). Supporting Evidence: PMID:15238359 OCTN2, a high-affinity, Na(+)-dependent carnitine transporter, was present in placental BBM but not in isolated basal plasma membrane vesicles. |
| GO:0031526 brush border membrane | ISS PMID:15523054 PDZK1 directly regulates the function of organic cation/carn... | ACCEPT | Summary: Brush-border membrane localization supported by sequence-similarity transfer (rat Octn2, Q9Z0E8) alongside the demonstrated colocalization of OCTN2 and PDZK1 in kidney brush-border membranes. Consistent with the direct human evidence. Reason: Brush-border localization is corroborated directly (placenta, OCTN2/PDZK1 colocalization in kidney BBM) and by ISS from the rat ortholog; correct. Supporting Evidence: PMID:15523054 both PDZK1 and OCTN2 are colocalized in brush-border membranes of the kidney. |
| GO:0005886 plasma membrane | TAS PMID:9916797 Primary systemic carnitine deficiency is caused by mutations... | ACCEPT | Summary: Author-asserted plasma-membrane localization of the carnitine transporter (membrane-physiological studies indicated a plasma-membrane carnitine transport defect in SCD). Consistent with the established core localization. Reason: Traceable author statement of plasma-membrane carnitine transporter localization, corroborated by extensive direct evidence. Supporting Evidence: PMID:9916797 a defect of the carnitine transport system in the plasma membrane in SCD patients |
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