ID SE1L1_HUMAN Reviewed; 794 AA. AC Q9UBV2; Q6UWT6; Q9P1T9; Q9UHK7; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 3. DT 27-MAR-2024, entry version 192. DE RecName: Full=Protein sel-1 homolog 1; DE AltName: Full=Suppressor of lin-12-like protein 1; DE Short=Sel-1L; DE Flags: Precursor; GN Name=SEL1L; Synonyms=TSA305; ORFNames=UNQ128/PRO1063; 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). RC TISSUE=Pancreas; RX PubMed=10496078; DOI=10.1007/s100380050171; RA Harada Y., Ozaki K., Suzuki M., Fujiwara T., Takahashi E., Nakamura Y., RA Tanigami A.; RT "Complete cDNA sequence and genomic organization of a human pancreas- RT specific gene homologous to Caenorhabditis elegans sel-1."; RL J. Hum. Genet. 44:330-336(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Pancreas; RX PubMed=10746565; DOI=10.1007/s004390051032; RA Biunno I., Bernard L., Dear P., Cattaneo M., Volorio S., Zannini L., RA Bankier A., Zollo M.; RT "SEL1L, the human homolog of C. elegans sel-1: refined physical mapping, RT gene structure and identification of polymorphic markers."; RL Hum. Genet. 106:227-235(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [4] RP GLYCOSYLATION AT ASN-272. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [5] RP FUNCTION, INTERACTION WITH SYVN1, IDENTIFICATION IN A COMPLEX WITH SYVN1 RP AND DERL2, AND SUBCELLULAR LOCATION. RX PubMed=16186509; DOI=10.1073/pnas.0505014102; RA Lilley B.N., Ploegh H.L.; RT "Multiprotein complexes that link dislocation, ubiquitination, and RT extraction of misfolded proteins from the endoplasmic reticulum membrane."; RL Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005). RN [6] RP GLYCOSYLATION, AND INTERACTION WITH ERLEC1; HSPA5; OS9 AND SYVN1. RX PubMed=18502753; DOI=10.1074/jbc.m709336200; RA Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.; RT "Human XTP3-B forms an endoplasmic reticulum quality control scaffold with RT the HRD1-SEL1L ubiquitin ligase complex and BiP."; RL J. Biol. Chem. 283:20914-20924(2008). RN [7] RP INTERACTION WITH ERLEC1; OS9 AND SYVN1. RX PubMed=18264092; DOI=10.1038/ncb1689; RA Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.; RT "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L RT ubiquitin ligase complex for ERAD."; RL Nat. Cell Biol. 10:272-282(2008). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-431 AND ASN-608. 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 [9] RP INTERACTION WITH EDEM1. RX PubMed=19524542; DOI=10.1016/j.molcel.2009.05.018; RA Cormier J.H., Tamura T., Sunryd J.C., Hebert D.N.; RT "EDEM1 recognition and delivery of misfolded proteins to the SEL1L- RT containing ERAD complex."; RL Mol. Cell 34:627-633(2009). RN [10] RP INTERACTION WITH FOXRED2. RX PubMed=19706418; DOI=10.1073/pnas.0900742106; RA Riemer J., Appenzeller-Herzog C., Johansson L., Bodenmiller B., RA Hartmann-Petersen R., Ellgaard L.; RT "A luminal flavoprotein in endoplasmic reticulum-associated degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:14831-14836(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP INTERACTION WITH LPL. RX PubMed=25066055; DOI=10.1016/j.cmet.2014.06.015; RA Sha H., Sun S., Francisco A.B., Ehrhardt N., Xue Z., Liu L., Lawrence P., RA Mattijssen F., Guber R.D., Panhwar M.S., Brenna J.T., Shi H., Xue B., RA Kersten S., Bensadoun A., Peterfy M., Long Q., Qi L.; RT "The ER-associated degradation adaptor protein Sel1L regulates LPL RT secretion and lipid metabolism."; RL Cell Metab. 20:458-470(2014). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP FUNCTION, AND INTERACTION WITH SYVN1. RX PubMed=26471130; DOI=10.1111/febs.13564; RA Hosokawa N., Wada I.; RT "Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin RT ligase regulates ERAD-L."; RL FEBS J. 283:157-172(2016). RN [15] RP IDENTIFICATION IN THE HRD1 COMPLEX. RX PubMed=28827405; DOI=10.1242/jcs.206847; RA Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J., RA Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.; RT "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex RT formation for ER-associated degradation (ERAD)."; RL J. Cell Sci. 130:3322-3335(2017). RN [16] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL148 (MICROBIAL INFECTION). RX PubMed=29997207; DOI=10.1128/jvi.00688-18; RA Nguyen C.C., Siddiquey M.N.A., Zhang H., Li G., Kamil J.P.; RT "Human Cytomegalovirus Tropism Modulator UL148 Interacts with SEL1L, a RT Cellular Factor That Governs Endoplasmic Reticulum-Associated Degradation RT of the Viral Envelope Glycoprotein gO."; RL J. Virol. 92:0-0(2018). CC -!- FUNCTION: Plays a role in the endoplasmic reticulum quality control CC (ERQC) system also called ER-associated degradation (ERAD) involved in CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum CC proteins (PubMed:16186509, PubMed:29997207). Enhances SYVN1 stability. CC Plays a role in LPL maturation and secretion. Required for normal CC differentiation of the pancreas epithelium, and for normal exocrine CC function and survival of pancreatic cells. May play a role in Notch CC signaling. {ECO:0000250|UniProtKB:Q9Z2G6, ECO:0000269|PubMed:16186509, CC ECO:0000269|PubMed:29997207}. CC -!- SUBUNIT: Homodimer and homooligomer (By similarity). May form a complex CC with ERLEC1, HSPA5, OS9, and SYVN1 (PubMed:18502753, PubMed:18264092). CC Interacts with FOXRED2 and EDEM1 (PubMed:19524542, PubMed:19706418). CC Interacts with LPL (PubMed:25066055). Interacts with LMF1; may CC stabilize the complex formed by LPL and LMF1 and thereby promote the CC export of LPL dimers (By similarity). Component of the HRD1 complex, CC which comprises at least SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP, CC OS9, SEL1L and UBE2J1 (PubMed:16186509, PubMed:28827405). SYNV1 CC assembles with SEL1L and FAM8A1 through its transmembrane domains, but CC interaction with its cytoplasmic domain is required to confer stability CC to FAM8A1 and enhance recruitment of HERPUD1 (PubMed:28827405). The CC interaction with SYNV1/HRD1 is direct (PubMed:26471130). CC {ECO:0000250|UniProtKB:Q9Z2G6, ECO:0000269|PubMed:16186509, CC ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753, CC ECO:0000269|PubMed:19524542, ECO:0000269|PubMed:19706418, CC ECO:0000269|PubMed:25066055, ECO:0000269|PubMed:26471130, CC ECO:0000269|PubMed:28827405}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL148. {ECO:0000269|PubMed:29997207}. CC -!- INTERACTION: CC Q9UBV2; P00533: EGFR; NbExp=2; IntAct=EBI-358766, EBI-297353; CC Q9UBV2; O75460-1: ERN1; NbExp=2; IntAct=EBI-358766, EBI-15600828; CC Q9UBV2; Q8IWF2: FOXRED2; NbExp=6; IntAct=EBI-358766, EBI-10763361; CC Q9UBV2; Q16288: NTRK3; NbExp=2; IntAct=EBI-358766, EBI-3936704; CC Q9UBV2; Q13438: OS9; NbExp=11; IntAct=EBI-358766, EBI-725454; CC Q9UBV2; Q86TM6: SYVN1; NbExp=20; IntAct=EBI-358766, EBI-947849; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:16186509}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:16186509}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBV2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBV2-2; Sequence=VSP_013322, VSP_013323; CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12754519, CC ECO:0000269|PubMed:18502753, ECO:0000269|PubMed:19159218}. CC -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42246/SEL1L"; 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; AB024763; BAA89204.1; -; Genomic_DNA. DR EMBL; AB020335; BAA87904.1; -; mRNA. DR EMBL; AF052059; AAF29413.1; -; mRNA. DR EMBL; AF157516; AAF24176.1; -; Genomic_DNA. DR EMBL; AF198647; AAL40905.1; -; Genomic_DNA. DR EMBL; AF198631; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198632; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198633; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198634; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198635; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198636; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198637; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198638; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198639; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198640; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198641; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198642; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198643; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198644; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198645; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AF198646; AAL40905.1; JOINED; Genomic_DNA. DR EMBL; AY358651; AAQ89014.1; -; mRNA. DR CCDS; CCDS58333.1; -. [Q9UBV2-2] DR CCDS; CCDS9876.1; -. [Q9UBV2-1] DR RefSeq; NP_001231913.1; NM_001244984.1. [Q9UBV2-2] DR RefSeq; NP_005056.3; NM_005065.5. [Q9UBV2-1] DR AlphaFoldDB; Q9UBV2; -. DR SMR; Q9UBV2; -. DR BioGRID; 112300; 254. DR CORUM; Q9UBV2; -. DR DIP; DIP-46259N; -. DR IntAct; Q9UBV2; 50. DR MINT; Q9UBV2; -. DR STRING; 9606.ENSP00000337053; -. DR TCDB; 3.A.16.1.4; the endoplasmic reticular retrotranslocon (er-rt) family. DR GlyConnect; 1669; 12 N-Linked glycans (5 sites). DR GlyCosmos; Q9UBV2; 6 sites, 11 glycans. DR GlyGen; Q9UBV2; 14 sites, 11 N-linked glycans (5 sites), 2 O-linked glycans (8 sites). DR iPTMnet; Q9UBV2; -. DR PhosphoSitePlus; Q9UBV2; -. DR SwissPalm; Q9UBV2; -. DR BioMuta; SEL1L; -. DR DMDM; 62512184; -. DR EPD; Q9UBV2; -. DR jPOST; Q9UBV2; -. DR MassIVE; Q9UBV2; -. DR MaxQB; Q9UBV2; -. DR PaxDb; 9606-ENSP00000337053; -. DR PeptideAtlas; Q9UBV2; -. DR ProteomicsDB; 84077; -. [Q9UBV2-1] DR ProteomicsDB; 84078; -. [Q9UBV2-2] DR Pumba; Q9UBV2; -. DR Antibodypedia; 13274; 289 antibodies from 30 providers. DR DNASU; 6400; -. DR Ensembl; ENST00000336735.9; ENSP00000337053.4; ENSG00000071537.14. [Q9UBV2-1] DR Ensembl; ENST00000555824.5; ENSP00000450709.1; ENSG00000071537.14. [Q9UBV2-2] DR GeneID; 6400; -. DR KEGG; hsa:6400; -. DR MANE-Select; ENST00000336735.9; ENSP00000337053.4; NM_005065.6; NP_005056.3. DR UCSC; uc001xvo.5; human. [Q9UBV2-1] DR AGR; HGNC:10717; -. DR CTD; 6400; -. DR DisGeNET; 6400; -. DR GeneCards; SEL1L; -. DR HGNC; HGNC:10717; SEL1L. DR HPA; ENSG00000071537; Tissue enriched (pancreas). DR MIM; 602329; gene. DR neXtProt; NX_Q9UBV2; -. DR OpenTargets; ENSG00000071537; -. DR PharmGKB; PA35639; -. DR VEuPathDB; HostDB:ENSG00000071537; -. DR eggNOG; KOG1550; Eukaryota. DR GeneTree; ENSGT00940000156671; -. DR HOGENOM; CLU_007931_2_1_1; -. DR InParanoid; Q9UBV2; -. DR OMA; DMLAKPR; -. DR OrthoDB; 1378605at2759; -. DR PhylomeDB; Q9UBV2; -. DR TreeFam; TF315257; -. DR PathwayCommons; Q9UBV2; -. DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD. DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis. DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC). DR SignaLink; Q9UBV2; -. DR BioGRID-ORCS; 6400; 90 hits in 1160 CRISPR screens. DR ChiTaRS; SEL1L; human. DR GeneWiki; SEL1L; -. DR GenomeRNAi; 6400; -. DR Pharos; Q9UBV2; Tbio. DR PRO; PR:Q9UBV2; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9UBV2; Protein. DR Bgee; ENSG00000071537; Expressed in body of pancreas and 213 other cell types or tissues. DR ExpressionAtlas; Q9UBV2; baseline and differential. DR Genevisible; Q9UBV2; HS. DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; TAS:ParkinsonsUK-UCL. DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IMP:UniProtKB. DR GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; TAS:ParkinsonsUK-UCL. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB. DR CDD; cd00062; FN2; 1. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR11102:SF70; PROTEIN SEL-1 HOMOLOG 1; 1. DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1. DR Pfam; PF00040; fn2; 1. DR Pfam; PF08238; Sel1; 11. DR PRINTS; PR00013; FNTYPEII. DR SMART; SM00059; FN2; 1. DR SMART; SM00671; SEL1; 11. DR SUPFAM; SSF81901; HCP-like; 3. DR SUPFAM; SSF57440; Kringle-like; 1. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Host-virus interaction; Membrane; Notch signaling pathway; Phosphoprotein; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..794 FT /note="Protein sel-1 homolog 1" FT /id="PRO_0000022294" FT TOPO_DOM 22..738 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 739..759 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 760..794 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 122..170 FT /note="Fibronectin type-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT REPEAT 183..218 FT /note="Sel1-like 1" FT REPEAT 219..254 FT /note="Sel1-like 2" FT REPEAT 255..290 FT /note="Sel1-like 3" FT REPEAT 291..326 FT /note="Sel1-like 4" FT REPEAT 373..409 FT /note="Sel1-like 5" FT REPEAT 410..446 FT /note="Sel1-like 6" FT REPEAT 447..482 FT /note="Sel1-like 7" FT REPEAT 483..518 FT /note="Sel1-like 8" FT REPEAT 519..554 FT /note="Sel1-like 9" FT REPEAT 627..662 FT /note="Sel1-like 10" FT REPEAT 664..699 FT /note="Sel1-like 11" FT REGION 21..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 22..737 FT /note="Interaction with ERLEC1, OS9 and SYVN1" FT REGION 64..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 352..537 FT /note="Important for homodimerization and oligomerization" FT /evidence="ECO:0000250|UniProtKB:Q9Z2G6" FT REGION 643..723 FT /note="Interaction with SYVN1" FT /evidence="ECO:0000250|UniProtKB:Q9Z2G6" FT REGION 738..794 FT /note="Mediates retention in the endoplasmic reticulum" FT REGION 766..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 29..49 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 770..794 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 195 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 217 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 431 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 608 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 127..153 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DISULFID 141..168 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT VAR_SEQ 298..301 FT /note="GYRY -> VSRL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_013322" FT VAR_SEQ 302..794 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_013323" FT VARIANT 162 FT /note="D -> G (in dbSNP:rs11499034)" FT /id="VAR_029303" FT VARIANT 714 FT /note="V -> I (in dbSNP:rs1051193)" FT /id="VAR_053963" FT CONFLICT 186 FT /note="M -> V (in Ref. 2; AAF29413/AAL40905)" FT /evidence="ECO:0000305" SQ SEQUENCE 794 AA; 88755 MW; 323EB03DC7485459 CRC64; MRVRIGLTLL LCAVLLSLAS ASSDEEGSQD ESLDSKTTLT SDESVKDHTT AGRVVAGQIF LDSEESELES SIQEEEDSLK SQEGESVTED ISFLESPNPE NKDYEEPKKV RKPALTAIEG TAHGEPCHFP FLFLDKEYDE CTSDGREDGR LWCATTYDYK ADEKWGFCET EEEAAKRRQM QEAEMMYQTG MKILNGSNKK SQKREAYRYL QKAASMNHTK ALERVSYALL FGDYLPQNIQ AAREMFEKLT EEGSPKGQTA LGFLYASGLG VNSSQAKALV YYTFGALGGN LIAHMVLGYR YWAGIGVLQS CESALTHYRL VANHVASDIS LTGGSVVQRI RLPDEVENPG MNSGMLEEDL IQYYQFLAEK GDVQAQVGLG QLHLHGGRGV EQNHQRAFDY FNLAANAGNS HAMAFLGKMY SEGSDIVPQS NETALHYFKK AADMGNPVGQ SGLGMAYLYG RGVQVNYDLA LKYFQKAAEQ GWVDGQLQLG SMYYNGIGVK RDYKQALKYF NLASQGGHIL AFYNLAQMHA SGTGVMRSCH TAVELFKNVC ERGRWSERLM TAYNSYKDGD YNAAVIQYLL LAEQGYEVAQ SNAAFILDQR EASIVGENET YPRALLHWNR AASQGYTVAR IKLGDYHFYG FGTDVDYETA FIHYRLASEQ QHSAQAMFNL GYMHEKGLGI KQDIHLAKRF YDMAAEASPD AQVPVFLALC KLGVVYFLQY IRETNIRDMF TQLDMDQLLG PEWDLYLMTI IALLLGTVIA YRQRQHQDMP APRPPGPRPA PPQQEGPPEQ QPPQ //