ID EMC10_HUMAN Reviewed; 262 AA. AC Q5UCC4; Q5UCC6; Q69YT5; Q6UWP3; Q86YL4; Q8N541; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 10-JUN-2026, entry version 144. DE RecName: Full=ER membrane protein complex subunit 10; DE AltName: Full=Hematopoietic signal peptide-containing membrane domain-containing protein 1; DE Flags: Precursor; GN Name=EMC10; Synonyms=C19orf63, INM02; ORFNames=UNQ764/PRO1556; 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 2). RC TISSUE=Insulinoma; RX PubMed=15163304; DOI=10.1677/erc.0.0110295; RA Wang X.-C., Xu S.-Y., Wu X.-Y., Song H.-D., Mao Y.-F., Fan H.-Y., Yu F., RA Mou B., Gu Y.-Y., Xu L.-Q., Zhou X.-O., Chen Z., Chen J.-L., Hu R.-M.; RT "Gene expression profiling in human insulinoma tissue: genes involved in RT the insulin secretion pathway and cloning of novel full-length cDNAs."; RL Endocr. Relat. Cancer 11:295-303(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), GLYCOSYLATION, SUBCELLULAR RP LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=20680400; DOI=10.1007/s11060-010-0314-6; RA Junes-Gill K.S., Gallaher T.K., Gluzman-Poltorak Z., Miller J.D., RA Wheeler C.J., Fan X., Basile L.A.; RT "hHSS1: a novel secreted factor and suppressor of glioma growth located at RT chromosome 19q13.33."; RL J. Neurooncol. 102:197-211(2011). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-261 (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-262 (ISOFORM 2). RC TISSUE=Testis; 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 [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [8] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION (ISOFORM 2). RX PubMed=19570817; DOI=10.1677/joe-09-0086; RA Wang X., Gong W., Liu Y., Yang Z., Zhou W., Wang M., Yang Z., Wen J., RA Hu R.; RT "Molecular cloning of a novel secreted peptide, INM02, and regulation of RT its expression by glucose."; RL J. Endocrinol. 202:355-364(2009). RN [9] RP IDENTIFICATION IN THE EMC COMPLEX, AND SUBCELLULAR LOCATION (ISOFORM 1). RX PubMed=22119785; DOI=10.1038/ncb2383; RA Christianson J.C., Olzmann J.A., Shaler T.A., Sowa M.E., Bennett E.J., RA Richter C.M., Tyler R.E., Greenblatt E.J., Harper J.W., Kopito R.R.; RT "Defining human ERAD networks through an integrative mapping strategy."; RL Nat. Cell Biol. 14:93-105(2012). RN [10] 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). RN [11] RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=28931551; DOI=10.1161/circulationaha.117.029980; RA Reboll M.R., Korf-Klingebiel M., Klede S., Polten F., Brinkmann E., RA Reimann I., Schoenfeld H.J., Bobadilla M., Faix J., Kensah G., Gruh I., RA Klintschar M., Gaestel M., Niessen H.W., Pich A., Bauersachs J., RA Gogos J.A., Wang Y., Wollert K.C.; RT "EMC10 (endoplasmic reticulum membrane protein complex subunit 10) is a RT bone marrow-derived angiogenic growth factor promoting tissue repair after RT myocardial infarction."; RL Circulation 136:1809-1823(2017). RN [12] RP FUNCTION. RX PubMed=30415835; DOI=10.1016/j.cell.2018.10.009; RA Chitwood P.J., Juszkiewicz S., Guna A., Shao S., Hegde R.S.; RT "EMC Is Required to Initiate Accurate Membrane Protein Topogenesis."; RL Cell 175:1507-1519(2018). RN [13] RP FUNCTION. RX PubMed=29809151; DOI=10.7554/elife.37018; RA Shurtleff M.J., Itzhak D.N., Hussmann J.A., Schirle Oakdale N.T., RA Costa E.A., Jonikas M., Weibezahn J., Popova K.D., Jan C.H., Sinitcyn P., RA Vembar S.S., Hernandez H., Cox J., Burlingame A.L., Brodsky J.L., Frost A., RA Borner G.H., Weissman J.S.; RT "The ER membrane protein complex interacts cotranslationally to enable RT biogenesis of multipass membrane proteins."; RL Elife 7:0-0(2018). RN [14] RP FUNCTION, AND SUBUNIT. RX PubMed=29242231; DOI=10.1126/science.aao3099; RA Guna A., Volkmar N., Christianson J.C., Hegde R.S.; RT "The ER membrane protein complex is a transmembrane domain insertase."; RL Science 359:470-473(2018). RN [15] RP INVOLVEMENT IN NEDDFAS. RX PubMed=32869858; DOI=10.1111/cge.13842; RA Umair M., Ballow M., Asiri A., Alyafee Y., Al Tuwaijri A., Alhamoudi K.M., RA Aloraini T., Abdelhakim M., Althagafi A.T., Kafkas S., Alsubaie L., RA Alrifai M.T., Hoehndorf R., Alfares A., Alfadhel M.; RT "EMC10 homozygous variant identified in a family with global developmental RT delay, mild intellectual disability, and speech delay."; RL Clin. Genet. 98:555-561(2020). RN [16] RP INVOLVEMENT IN NEDDFAS, AND TISSUE SPECIFICITY. RX PubMed=33531666; DOI=10.1038/s41436-021-01097-x; RA Shao D.D., Straussberg R., Ahmed H., Khan A., Tian S., Hill R.S., RA Smith R.S., Majmundar A.J., Ameziane N., Neil J.E., Yang E., Al Tenaiji A., RA Jamuar S.S., Schlaeger T.M., Al-Saffar M., Hovel I., Al-Shamsi A., RA Basel-Salmon L., Amir A.Z., Rento L.M., Lim J.Y., Ganesan I., Shril S., RA Evrony G., Barkovich A.J., Bauer P., Hildebrandt F., Dong M., Borck G., RA Beetz C., Al-Gazali L., Eyaid W., Walsh C.A.; RT "A recurrent, homozygous EMC10 frameshift variant is associated with a RT syndrome of developmental delay with variable seizures and dysmorphic RT features."; RL Genet. Med. 23:1158-1162(2021). RN [17] {ECO:0007744|PDB:6Z3W} RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) OF THE EMC COMPLEX, RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32459176; DOI=10.7554/elife.57887; RA O'Donnell J.P., Phillips B.P., Yagita Y., Juszkiewicz S., Wagner A., RA Malinverni D., Keenan R.J., Miller E.A., Hegde R.S.; RT "The architecture of EMC reveals a path for membrane protein insertion."; RL Elife 9:0-0(2020). RN [18] {ECO:0007744|PDB:6WW7} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF THE EMC COMPLEX, RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SIGNAL PEPTIDE, AND GLYCOSYLATION RP AT ASN-182. RX PubMed=32439656; DOI=10.1126/science.abb5008; RA Pleiner T., Tomaleri G.P., Januszyk K., Inglis A.J., Hazu M., RA Voorhees R.M.; RT "Structural basis for membrane insertion by the human ER membrane protein RT complex."; RL Science 369:433-436(2020). CC -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex CC (EMC) that enables the energy-independent insertion into endoplasmic CC reticulum membranes of newly synthesized membrane proteins CC (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, CC PubMed:32459176). Preferentially accommodates proteins with CC transmembrane domains that are weakly hydrophobic or contain CC destabilizing features such as charged and aromatic residues CC (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the CC cotranslational insertion of multi-pass membrane proteins in which CC stop-transfer membrane-anchor sequences become ER membrane spanning CC helices (PubMed:29809151, PubMed:30415835). It is also required for the CC post-translational insertion of tail-anchored/TA proteins in CC endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By CC mediating the proper cotranslational insertion of N-terminal CC transmembrane domains in an N-exo topology, with translocated N- CC terminus in the lumen of the ER, controls the topology of multi-pass CC membrane proteins like the G protein-coupled receptors CC (PubMed:30415835). By regulating the insertion of various proteins in CC membranes, it is indirectly involved in many cellular processes CC (Probable). Promotes angiogenesis and tissue repair in the heart after CC myocardial infarction. Stimulates cardiac endothelial cell migration CC and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling CC pathways (PubMed:28931551). {ECO:0000269|PubMed:28931551, CC ECO:0000269|PubMed:29242231, ECO:0000269|PubMed:29809151, CC ECO:0000269|PubMed:30415835, ECO:0000269|PubMed:32439656, CC ECO:0000269|PubMed:32459176, ECO:0000305}. CC -!- SUBUNIT: Component of the ER membrane protein complex (EMC). CC {ECO:0000269|PubMed:22119785, ECO:0000269|PubMed:29242231, CC ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:22119785, ECO:0000305|PubMed:32439656, CC ECO:0000305|PubMed:32459176}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted CC {ECO:0000269|PubMed:19570817, ECO:0000269|PubMed:20680400, CC ECO:0000269|PubMed:28931551}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=HSM1 {ECO:0000303|PubMed:20680400}; CC IsoId=Q5UCC4-1; Sequence=Displayed; CC Name=2; Synonyms=Hematopoietic signal peptide-containing secreted CC protein 1 {ECO:0000303|PubMed:20680400}, HSS1 CC {ECO:0000303|PubMed:20680400}; CC IsoId=Q5UCC4-2; Sequence=VSP_030473; CC -!- TISSUE SPECIFICITY: Present in serum (at protein level). Increased CC expression seen in the left ventrice after myocardial infarction (at CC protein level). Expressed in the pituitary gland. Expressed in brain CC (PubMed:33531666). {ECO:0000269|PubMed:19570817, CC ECO:0000269|PubMed:20680400, ECO:0000269|PubMed:28931551, CC ECO:0000269|PubMed:33531666}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:20680400}. CC -!- DISEASE: Neurodevelopmental disorder with dysmorphic facies and CC variable seizures (NEDDFAS) [MIM:619264]: An autosomal recessive CC disorder characterized by global developmental delay apparent in early CC childhood, mildly impaired intellectual development, speech delay, CC behavioral abnormalities, and non-specific dysmorphic facial features. CC Some patients may have seizures, brain imaging abnormalities, mild CC skeletal defects, and renal abnormalities. CC {ECO:0000269|PubMed:32869858, ECO:0000269|PubMed:33531666}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the EMC10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ89073.1; Type=Miscellaneous discrepancy; Note=Intron retention at the C-terminus.; 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; AY194293; AAO23975.2; -; mRNA. DR EMBL; AY761095; AAV30543.1; -; mRNA. DR EMBL; AY761097; AAV30545.1; -; mRNA. DR EMBL; CH471135; EAW71871.1; -; Genomic_DNA. DR EMBL; BC032948; AAH32948.1; -; mRNA. DR EMBL; BC035001; AAH35001.1; -; mRNA. DR EMBL; AY358710; AAQ89073.1; ALT_SEQ; mRNA. DR EMBL; AL512761; CAH10658.1; -; mRNA. DR CCDS; CCDS12796.1; -. [Q5UCC4-1] DR CCDS; CCDS42594.1; -. [Q5UCC4-2] DR RefSeq; NP_778233.4; NM_175063.5. [Q5UCC4-2] DR RefSeq; NP_996261.1; NM_206538.4. [Q5UCC4-1] DR PDB; 6WW7; EM; 3.40 A; I=1-262. DR PDB; 6Z3W; EM; 6.40 A; I=1-262. DR PDB; 7ADO; EM; 3.39 A; I=2-262. DR PDB; 7ADP; EM; 3.60 A; I=2-262. DR PDB; 8EOI; EM; 3.40 A; I=50-206. DR PDB; 8J0N; EM; 3.47 A; J=1-207. DR PDB; 8J0O; EM; 3.32 A; J=1-207. DR PDB; 8S9S; EM; 3.60 A; 10=1-262. DR PDB; 9C7V; EM; 6.60 A; 10=1-262. DR PDBsum; 6WW7; -. DR PDBsum; 6Z3W; -. DR PDBsum; 7ADO; -. DR PDBsum; 7ADP; -. DR PDBsum; 8EOI; -. DR PDBsum; 8J0N; -. DR PDBsum; 8J0O; -. DR PDBsum; 8S9S; -. DR PDBsum; 9C7V; -. DR AlphaFoldDB; Q5UCC4; -. DR EMDB; EMD-11732; -. DR EMDB; EMD-11733; -. DR EMDB; EMD-21929; -. DR EMDB; EMD-28376; -. DR EMDB; EMD-35906; -. DR EMDB; EMD-35907; -. DR EMDB; EMD-40245; -. DR EMDB; EMD-40246; -. DR EMDB; EMD-45295; -. DR SMR; Q5UCC4; -. DR BioGRID; 129844; 61. DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant. DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant. DR CORUM; Q5UCC4; -. DR FunCoup; Q5UCC4; 974. DR IntAct; Q5UCC4; 33. DR MINT; Q5UCC4; -. DR NDEx; IQUERY-CP-EMC10; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000334037; -. DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family. DR GlyConnect; Q5UCC4; 4 N-Linked glycans (1 site). DR GlyCosmos; Q5UCC4; 3 sites, 5 glycans. DR GlyGen; Q5UCC4; 5 sites, 5 N-linked glycans (1 site), 3 O-linked glycans (4 sites). DR iPTMnet; Q5UCC4; -. DR PhosphoSitePlus; Q5UCC4; -. DR SwissPalm; Q5UCC4; -. DR BioMuta; EMC10; -. DR DMDM; 74708213; -. DR jPOST; Q5UCC4; -. DR MassIVE; Q5UCC4; -. DR PaxDb; 9606-ENSP00000334037; -. DR PeptideAtlas; Q5UCC4; -. DR ProteomicsDB; 65243; -. [Q5UCC4-1] DR ProteomicsDB; 65244; -. [Q5UCC4-2] DR Pumba; Q5UCC4; -. DR TopDownProteomics; Q5UCC4-1; -. [Q5UCC4-1] DR Antibodypedia; 53684; 74 antibodies from 17 providers. DR DNASU; 284361; -. DR Ensembl; ENST00000334976.11; ENSP00000334037.6; ENSG00000161671.17. [Q5UCC4-1] DR Ensembl; ENST00000376918.7; ENSP00000366117.2; ENSG00000161671.17. [Q5UCC4-2] DR GeneID; 284361; -. DR KEGG; hsa:284361; -. DR MANE-Select; ENST00000334976.11; ENSP00000334037.6; NM_206538.4; NP_996261.1. DR UCSC; uc002psk.5; human. [Q5UCC4-1] DR AGR; HGNC:27609; -. DR ClinPGx; PA162378790; -. DR CTD; 284361; -. DR DisGeNET; 284361; -. DR GeneCards; EMC10; -. DR GeneReviews; EMC10; -. DR HGNC; HGNC:27609; EMC10. DR HPA; ENSG00000161671; Tissue enhanced (skeletal). DR MalaCards; EMC10; -. DR MIM; 614545; gene. DR MIM; 619264; phenotype. DR OpenTargets; ENSG00000161671; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000161671; -. DR eggNOG; KOG4827; Eukaryota. DR GeneTree; ENSGT00390000004520; -. DR HOGENOM; CLU_065716_0_0_1; -. DR InParanoid; Q5UCC4; -. DR OMA; QFNDVLW; -. DR OrthoDB; 1894652at2759; -. DR PAN-GO; Q5UCC4; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q5UCC4; -. DR PathwayCommons; Q5UCC4; -. DR SignaLink; Q5UCC4; -. DR Agora; ENSG00000161671; -. DR BioGRID-ORCS; 284361; 12 hits in 1153 CRISPR screens. DR ChiTaRS; EMC10; human. DR GenomeRNAi; 284361; -. DR Pharos; Q5UCC4; Tbio. DR PRO; PR:Q5UCC4; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q5UCC4; protein. DR Bgee; ENSG00000161671; Expressed in adenohypophysis and 177 other cell types or tissues. DR ExpressionAtlas; Q5UCC4; baseline and differential. DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB. DR GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IDA:ComplexPortal. DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB. DR CDD; cd22209; EMC10; 1. DR PANTHER; PTHR21397; CHROMATIN COMPLEXES SUBUNIT BAP18-RELATED; 1. DR PANTHER; PTHR21397:SF4; ER MEMBRANE PROTEIN COMPLEX SUBUNIT 10; 1. DR Pfam; PF21203; ECM10; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Angiogenesis; Endoplasmic reticulum; KW Glycoprotein; Intellectual disability; Membrane; Proteomics identification; KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:32439656" FT CHAIN 26..262 FT /note="ER membrane protein complex subunit 10" FT /id="PRO_0000315048" FT TOPO_DOM 26..221 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:32439656" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 243..262 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:32439656" FT CARBOHYD 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:32439656" FT VAR_SEQ 228..262 FT /note="MYIIPVVLFLMMSGAPDTGGQGGGGGGGGGGGSGR -> HIILGGAVLLTAL FT RPAAPGPAPPPQEA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15163304, FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:20680400" FT /id="VSP_030473" FT CONFLICT 63 FT /note="D -> G (in Ref. 1; AAO23975)" FT /evidence="ECO:0000305" FT CONFLICT 245 FT /note="T -> A (in Ref. 4; AAH32948/AAH35001)" FT /evidence="ECO:0000305" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 69..77 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 88..91 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 92..103 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 108..114 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:6WW7" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 156..162 FT /evidence="ECO:0007829|PDB:8J0O" FT TURN 175..179 FT /evidence="ECO:0007829|PDB:8J0O" FT STRAND 183..188 FT /evidence="ECO:0007829|PDB:8J0O" FT HELIX 198..206 FT /evidence="ECO:0007829|PDB:8J0O" SQ SEQUENCE 262 AA; 27347 MW; 816940C105B95AA1 CRC64; MAAASAGATR LLLLLLMAVA APSRARGSGC RAGTGARGAG AEGREGEACG TVGLLLEHSF EIDDSANFRK RGSLLWNQQD GTLSLSQRQL SEEERGRLRD VAALNGLYRV RIPRRPGALD GLEAGGYVSS FVPACSLVES HLSDQLTLHV DVAGNVVGVS VVTHPGGCRG HEVEDVDLEL FNTSVQLQPP TTAPGPETAA FIERLEMEQA QKAKNPQEQK SFFAKYWMYI IPVVLFLMMS GAPDTGGQGG GGGGGGGGGS GR //