EMC10_HUMAN
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 03-AUG-2022, entry version 126.
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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176,
CC PubMed:32439656). Preferentially accommodates proteins with
CC transmembrane domains that are weakly hydrophobic or contain
CC destabilizing features such as charged and aromatic residues
CC (PubMed:30415835, PubMed:29809151, PubMed:29242231). 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:30415835, PubMed:29809151). It is also required for the
CC post-translational insertion of tail-anchored/TA proteins in
CC endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). 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};
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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_206538.3. [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 PDBsum; 6WW7; -.
DR PDBsum; 6Z3W; -.
DR PDBsum; 7ADO; -.
DR PDBsum; 7ADP; -.
DR AlphaFoldDB; Q5UCC4; -.
DR SMR; Q5UCC4; -.
DR BioGRID; 129844; 51.
DR ComplexPortal; CPX-5848; Endoplasmic reticulum membrane complex, EMC8 variant.
DR ComplexPortal; CPX-5881; Endoplasmic reticulum membrane complex, EMC9 variant.
DR IntAct; Q5UCC4; 21.
DR MINT; Q5UCC4; -.
DR STRING; 9606.ENSP00000334037; -.
DR TCDB; 3.A.27.1.1; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR GlyConnect; 1224; 4 N-Linked glycans (1 site).
DR GlyGen; Q5UCC4; 4 sites, 4 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; Q5UCC4; -.
DR PhosphoSitePlus; Q5UCC4; -.
DR BioMuta; EMC10; -.
DR DMDM; 74708213; -.
DR EPD; Q5UCC4; -.
DR jPOST; Q5UCC4; -.
DR MassIVE; Q5UCC4; -.
DR MaxQB; Q5UCC4; -.
DR PaxDb; Q5UCC4; -.
DR PeptideAtlas; Q5UCC4; -.
DR PRIDE; Q5UCC4; -.
DR ProteomicsDB; 65243; -. [Q5UCC4-1]
DR ProteomicsDB; 65244; -. [Q5UCC4-2]
DR TopDownProteomics; Q5UCC4-1; -. [Q5UCC4-1]
DR Antibodypedia; 53684; 75 antibodies from 18 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 CTD; 284361; -.
DR DisGeNET; 284361; -.
DR GeneCards; EMC10; -.
DR HGNC; HGNC:27609; EMC10.
DR HPA; ENSG00000161671; Tissue enhanced (skeletal).
DR MIM; 614545; gene.
DR MIM; 619264; phenotype.
DR neXtProt; NX_Q5UCC4; -.
DR OpenTargets; ENSG00000161671; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA162378790; -.
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; 1514526at2759; -.
DR PhylomeDB; Q5UCC4; -.
DR TreeFam; TF314052; -.
DR PathwayCommons; Q5UCC4; -.
DR SignaLink; Q5UCC4; -.
DR BioGRID-ORCS; 284361; 12 hits in 1073 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 175 other tissues.
DR ExpressionAtlas; Q5UCC4; baseline and differential.
DR Genevisible; Q5UCC4; HS.
DR GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of 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:1900745; P:positive regulation of p38MAPK cascade; ISS: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 InterPro; IPR029615; Emc10.
DR PANTHER; PTHR21397:SF4; PTHR21397:SF4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Endoplasmic reticulum;
KW Glycoprotein; Intellectual disability; Membrane; Reference proteome;
KW 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 52..59
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:7ADO"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7ADO"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6WW7"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:7ADO"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:7ADO"
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
