ID SPNS1_HUMAN Reviewed; 528 AA. AC Q9H2V7; B5MDM9; Q6P182; Q71RB5; Q7L541; Q86VU7; Q8N953; Q8TCS5; Q9BRN5; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 28-JAN-2026, entry version 176. DE RecName: Full=Protein spinster homolog 1; DE AltName: Full=HSpin1 {ECO:0000303|PubMed:12815463}; DE AltName: Full=SPNS1 {ECO:0000303|PubMed:36161949, ECO:0000303|PubMed:37075117}; DE AltName: Full=Spinster-like protein 1; GN Name=SPNS1; Synonyms=SPIN1; ORFNames=PP20300; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11340170; DOI=10.1128/mcb.21.11.3775-3788.2001; RA Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L., RA Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W., RA Kaneda M., Umeda M., Yamamoto D.; RT "Mutations in the novel membrane protein spinster interfere with programmed RT cell death and cause neural degeneration in Drosophila melanogaster."; RL Mol. Cell. Biol. 21:3775-3788(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Mammary cancer; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP PRO-230. RC TISSUE=Blood, Brain, Pancreas, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=12408844; DOI=10.1016/s0896-6273(02)01014-0; RA Sweeney S.T., Davis G.W.; RT "Unrestricted synaptic growth in spinster-a late endosomal protein RT implicated in TGF-beta-mediated synaptic growth regulation."; RL Neuron 36:403-416(2002). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2 AND BCL2L1. RX PubMed=12815463; DOI=10.1038/sj.cdd.4401246; RA Yanagisawa H., Miyashita T., Nakano Y., Yamamoto D.; RT "HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a RT caspase-independent autophagic cell death."; RL Cell Death Differ. 10:798-807(2003). RN [10] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=36161949; DOI=10.1073/pnas.2210353119; RA He M., Kuk A.C.Y., Ding M., Chin C.F., Galam D.L.A., Nah J.M., Tan B.C., RA Yeo H.L., Chua G.L., Benke P.I., Wenk M.R., Ho L., Torta F., Silver D.L.; RT "Spns1 is a lysophospholipid transporter mediating lysosomal phospholipid RT salvage."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2210353119-e2210353119(2022). RN [11] RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=37075117; DOI=10.1126/sciadv.adf8966; RA Scharenberg S.G., Dong W., Ghoochani A., Nyame K., Levin-Konigsberg R., RA Krishnan A.R., Rawat E.S., Spees K., Bassik M.C., Abu-Remaileh M.; RT "An SPNS1-dependent lysosomal lipid transport pathway that enables cell RT survival under choline limitation."; RL Sci. Adv. 9:eadf8966-eadf8966(2023). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Plays a critical role in the phospholipid salvage pathway CC from lysosomes to the cytosol (PubMed:36161949, PubMed:37075117). CC Mediates the rate-limiting, proton-dependent, lysosomal efflux of CC lysophospholipids, which can then be reacylated by acyltransferases in CC the endoplasmic reticulum to form phospholipids (PubMed:36161949, CC PubMed:37075117). Selective for zwitterionic headgroups such as CC lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), CC can also transport lysophosphatidylglycerol (LPG), but not other CC anionic lysophospholipids, sphingosine, nor sphingomyelin CC (PubMed:36161949). Transports lysophospholipids with saturated, CC monounsaturated, and polyunsaturated fatty acids, such as 1- CC hexadecanoyl-sn-glycero-3-phosphocholine, 1-(9Z-octadecenoyl)-sn- CC glycero-3-phosphocholine and 1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)- CC sn-glycero-3-phosphocholine, respectively (PubMed:36161949, CC PubMed:37075117). Can also transport lysoplasmalogen (LPC with a fatty CC alcohol) such as 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine CC (PubMed:36161949). Lysosomal LPC could function as intracellular CC signaling messenger (PubMed:37075117). Essential player in lysosomal CC homeostasis (PubMed:36161949). Crucial for cell survival under CC conditions of nutrient limitation (PubMed:37075117). May be involved in CC necrotic or autophagic cell death (PubMed:12815463). CC {ECO:0000269|PubMed:12815463, ECO:0000269|PubMed:36161949, CC ECO:0000269|PubMed:37075117, ECO:0000303|PubMed:37075117}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine(out) + H(+)(out) = a 1- CC acyl-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74435, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000269|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + H(+)(out) = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74427, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000305|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) + CC H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) + CC H(+)(in); Xref=Rhea:RHEA:74411, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000269|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3- CC phosphocholine(out) + H(+)(out) = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)- CC sn-glycero-3-phosphocholine(in) + H(+)(in); Xref=Rhea:RHEA:74451, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74344; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000305|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3- CC phosphocholine(out) + H(+)(out) = 1-(4Z,7Z,10Z,13Z,16Z,19Z- CC docosahexaenoyl)-sn-glycero-3-phosphocholine(in) + H(+)(in); CC Xref=Rhea:RHEA:74423, ChEBI:CHEBI:15378, ChEBI:CHEBI:73873; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000305|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(out) + H(+)(out) = a CC 1-acyl-sn-glycero-3-phosphoethanolamine(in) + H(+)(in); CC Xref=Rhea:RHEA:74439, ChEBI:CHEBI:15378, ChEBI:CHEBI:64381; CC Evidence={ECO:0000269|PubMed:36161949, ECO:0000305|PubMed:37075117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine(in) CC + H(+)(in); Xref=Rhea:RHEA:74415, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:74971; Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + H(+)(out) CC = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + H(+)(in); CC Xref=Rhea:RHEA:74443, ChEBI:CHEBI:15378, ChEBI:CHEBI:64840; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol)(out) CC + H(+)(out) = 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn- CC glycerol)(in) + H(+)(in); Xref=Rhea:RHEA:74419, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72828; Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(out) + CC H(+)(out) = a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine(in) + CC H(+)(in); Xref=Rhea:RHEA:74447, ChEBI:CHEBI:15378, ChEBI:CHEBI:77287; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine(out) + CC H(+)(out) = 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine(in) + CC H(+)(in); Xref=Rhea:RHEA:74431, ChEBI:CHEBI:15378, ChEBI:CHEBI:73850; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = a 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine(in) + CC H(+)(in); Xref=Rhea:RHEA:74455, ChEBI:CHEBI:15378, ChEBI:CHEBI:77288; CC Evidence={ECO:0000269|PubMed:36161949}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-(1Z-hexadecenyl)-sn-glycero-3-phosphoethanolamine(out) + CC H(+)(out) = 1-O-(1Z-hexadecenyl)-sn-glycero-3-phosphoethanolamine(in) CC + H(+)(in); Xref=Rhea:RHEA:74459, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:133139; Evidence={ECO:0000269|PubMed:36161949}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.0-6.0. {ECO:0000269|PubMed:36161949, CC ECO:0000269|PubMed:37075117}; CC -!- SUBUNIT: Interacts with BCL2 and BCL2L1. {ECO:0000269|PubMed:12815463}. CC -!- INTERACTION: CC Q9H2V7; Q07817: BCL2L1; NbExp=3; IntAct=EBI-1386527, EBI-78035; CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:12408844}; CC Multi-pass membrane protein {ECO:0000269|PubMed:12408844}. CC Mitochondrion inner membrane {ECO:0000269|PubMed:12815463}; Multi-pass CC membrane protein {ECO:0000269|PubMed:12815463}. Note=Ocassionally CC localizes to mitochondria. {ECO:0000269|PubMed:12815463}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9H2V7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H2V7-2; Sequence=VSP_028196; CC Name=3; Synonyms=CRA_d; CC IsoId=Q9H2V7-3; Sequence=VSP_028195, VSP_028196; CC Name=4; CC IsoId=Q9H2V7-4; Sequence=VSP_028194; CC Name=5; CC IsoId=Q9H2V7-5; Sequence=VSP_036389; CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster CC (TC 2.A.1.49) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ15259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAQ15259.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF212371; AAG43830.1; -; mRNA. DR EMBL; AK095677; BAC04603.1; -; mRNA. DR EMBL; AK289787; BAF82476.1; -; mRNA. DR EMBL; AF370423; AAQ15259.1; ALT_SEQ; mRNA. DR EMBL; AL390215; CAB99229.1; -; mRNA. DR EMBL; AC109460; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471267; EAW52018.1; -; Genomic_DNA. DR EMBL; CH471267; EAW52019.1; -; Genomic_DNA. DR EMBL; BC006156; AAH06156.1; -; mRNA. DR EMBL; BC008325; AAH08325.1; -; mRNA. DR EMBL; BC038961; AAH38961.1; -; mRNA. DR EMBL; BC047741; AAH47741.1; -; mRNA. DR EMBL; BC065235; AAH65235.1; -; mRNA. DR CCDS; CCDS10646.1; -. [Q9H2V7-1] DR CCDS; CCDS45452.1; -. [Q9H2V7-2] DR CCDS; CCDS45453.1; -. [Q9H2V7-3] DR CCDS; CCDS45454.1; -. [Q9H2V7-4] DR RefSeq; NP_001135920.1; NM_001142448.2. [Q9H2V7-1] DR RefSeq; NP_001135921.1; NM_001142449.2. [Q9H2V7-3] DR RefSeq; NP_001135922.1; NM_001142450.2. [Q9H2V7-4] DR RefSeq; NP_001135923.1; NM_001142451.2. [Q9H2V7-2] DR RefSeq; NP_114427.1; NM_032038.3. [Q9H2V7-1] DR PDB; 9BOI; EM; 3.22 A; A=56-528. DR PDBsum; 9BOI; -. DR AlphaFoldDB; Q9H2V7; -. DR EMDB; EMD-44741; -. DR EMDB; EMD-44742; -. DR SMR; Q9H2V7; -. DR BioGRID; 123836; 146. DR FunCoup; Q9H2V7; 1135. DR IntAct; Q9H2V7; 83. DR MINT; Q9H2V7; -. DR STRING; 9606.ENSP00000309945; -. DR BindingDB; Q9H2V7; -. DR TCDB; 2.A.1.49.2; the major facilitator superfamily (mfs). DR GlyGen; Q9H2V7; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9H2V7; -. DR PhosphoSitePlus; Q9H2V7; -. DR SwissPalm; Q9H2V7; -. DR BioMuta; SPNS1; -. DR DMDM; 74733566; -. DR jPOST; Q9H2V7; -. DR MassIVE; Q9H2V7; -. DR PaxDb; 9606-ENSP00000309945; -. DR PeptideAtlas; Q9H2V7; -. DR ProteomicsDB; 80600; -. [Q9H2V7-1] DR ProteomicsDB; 80601; -. [Q9H2V7-2] DR ProteomicsDB; 80602; -. [Q9H2V7-3] DR ProteomicsDB; 80604; -. [Q9H2V7-5] DR Pumba; Q9H2V7; -. DR Antibodypedia; 26665; 78 antibodies from 19 providers. DR DNASU; 83985; -. DR Ensembl; ENST00000311008.16; ENSP00000309945.11; ENSG00000169682.18. [Q9H2V7-1] DR Ensembl; ENST00000323081.12; ENSP00000318228.8; ENSG00000169682.18. [Q9H2V7-4] DR Ensembl; ENST00000334536.12; ENSP00000335494.8; ENSG00000169682.18. [Q9H2V7-2] DR Ensembl; ENST00000352260.11; ENSP00000306050.10; ENSG00000169682.18. [Q9H2V7-3] DR GeneID; 83985; -. DR KEGG; hsa:83985; -. DR MANE-Select; ENST00000311008.16; ENSP00000309945.11; NM_032038.3; NP_114427.1. DR UCSC; uc002drx.3; human. [Q9H2V7-1] DR AGR; HGNC:30621; -. DR ClinPGx; PA162404561; -. DR CTD; 83985; -. DR DisGeNET; 83985; -. DR GeneCards; SPNS1; -. DR HGNC; HGNC:30621; SPNS1. DR HPA; ENSG00000169682; Low tissue specificity. DR MIM; 612583; gene. DR OpenTargets; ENSG00000169682; -. DR VEuPathDB; HostDB:ENSG00000169682; -. DR eggNOG; KOG1330; Eukaryota. DR GeneTree; ENSGT00390000005976; -. DR HOGENOM; CLU_001265_5_12_1; -. DR InParanoid; Q9H2V7; -. DR OMA; YICAAGL; -. DR OrthoDB; 6770063at2759; -. DR PAN-GO; Q9H2V7; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9H2V7; -. DR PathwayCommons; Q9H2V7; -. DR SignaLink; Q9H2V7; -. DR Agora; ENSG00000169682; -. DR BioGRID-ORCS; 83985; 85 hits in 1177 CRISPR screens. DR ChiTaRS; SPNS1; human. DR GenomeRNAi; 83985; -. DR Pharos; Q9H2V7; Tbio. DR PRO; PR:Q9H2V7; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H2V7; protein. DR Bgee; ENSG00000169682; Expressed in granulocyte and 98 other cell types or tissues. DR ExpressionAtlas; Q9H2V7; baseline and differential. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IDA:MGI. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0051977; P:lysophospholipid transport; IDA:MGI. DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central. DR GO; GO:0035751; P:regulation of lysosomal lumen pH; IEA:Ensembl. DR CDD; cd17328; MFS_spinster_like; 1. DR FunFam; 1.20.1250.20:FF:000097; protein spinster homolog 1; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR044770; MFS_spinster-like. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR23505:SF13; PROTEIN SPINSTER HOMOLOG 1; 1. DR PANTHER; PTHR23505; SPINSTER; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Lipid transport; Lysosome; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..528 FT /note="Protein spinster homolog 1" FT /id="PRO_0000305039" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 127..147 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 160..180 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 187..207 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 278..298 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 323..343 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 357..377 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 381..401 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 421..441 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 465..485 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..73 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15498874" FT /id="VSP_028194" FT VAR_SEQ 81..102 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_028195" FT VAR_SEQ 223..528 FT /note="TPGLGVVAVLLLFLVVREPPRGAVERHSDLPPLNPTSWWADLRALARNPSFV FT LSSLGFTAVAFVTGSLALWAPAFLLRSRVVLGETPPCLPGDSCSSSDSLIFGLITCLTG FT VLGVGLGVEISRRLRHSNPRADPLVCATGLLGSAPFLFLSLACARGSIVATYIFIFIGE FT TLLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAGSPYLIGLISDRLRRNWPP FT SFLSEFRALQFSLMLCAFVGALGGAAFLGTAIFIEADRRRAQLHVQGLLHEAGSTDDRI FT VVPQRGRSTRVPVASVLI -> SLVLAWG (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_036389" FT VAR_SEQ 271..322 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_028196" FT VARIANT 230 FT /note="A -> P (in dbSNP:rs17855956)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035157" FT HELIX 57..77 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 83..89 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 95..119 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 124..142 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 151..178 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 181..213 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 216..220 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 225..236 FT /evidence="ECO:0007829|PDB:9BOI" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 271..305 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 320..348 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 354..376 FT /evidence="ECO:0007829|PDB:9BOI" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 382..396 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 398..409 FT /evidence="ECO:0007829|PDB:9BOI" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 415..431 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 434..442 FT /evidence="ECO:0007829|PDB:9BOI" FT HELIX 461..496 FT /evidence="ECO:0007829|PDB:9BOI" SQ SEQUENCE 528 AA; 56630 MW; F1B9D2EB3F9F1B48 CRC64; MAGSDTAPFL SQADDPDDGP VPGTPGLPGS TGNPKSEEPE VPDQEGLQRI TGLSPGRSAL IVAVLCYINL LNYMDRFTVA GVLPDIEQFF NIGDSSSGLI QTVFISSYMV LAPVFGYLGD RYNRKYLMCG GIAFWSLVTL GSSFIPGEHF WLLLLTRGLV GVGEASYSTI APTLIADLFV ADQRSRMLSI FYFAIPVGSG LGYIAGSKVK DMAGDWHWAL RVTPGLGVVA VLLLFLVVRE PPRGAVERHS DLPPLNPTSW WADLRALARN PSFVLSSLGF TAVAFVTGSL ALWAPAFLLR SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRHS NPRADPLVCA TGLLGSAPFL FLSLACARGS IVATYIFIFI GETLLSMNWA IVADILLYVV IPTRRSTAEA FQIVLSHLLG DAGSPYLIGL ISDRLRRNWP PSFLSEFRAL QFSLMLCAFV GALGGAAFLG TAIFIEADRR RAQLHVQGLL HEAGSTDDRI VVPQRGRSTR VPVASVLI //