SE1L1_HUMAN
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 03-AUG-2022, entry version 183.
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; O75460-1: ERN1; NbExp=2; IntAct=EBI-358766, EBI-15600828;
CC Q9UBV2; Q8IWF2: FOXRED2; NbExp=6; IntAct=EBI-358766, EBI-10763361;
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="http://atlasgeneticsoncology.org/Genes/SEL1LID42246ch14q24.html";
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; 239.
DR CORUM; Q9UBV2; -.
DR DIP; DIP-46259N; -.
DR IntAct; Q9UBV2; 41.
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 GlyGen; Q9UBV2; 7 sites, 11 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
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; Q9UBV2; -.
DR PeptideAtlas; Q9UBV2; -.
DR PRIDE; Q9UBV2; -.
DR ProteomicsDB; 84077; -. [Q9UBV2-1]
DR ProteomicsDB; 84078; -. [Q9UBV2-2]
DR Antibodypedia; 13274; 272 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 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 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; 87 hits in 1078 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 211 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; TAS:ParkinsonsUK-UCL.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.10.10.10; -; 1.
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 Pfam; PF00040; fn2; 1.
DR Pfam; PF08238; Sel1; 12.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00671; SEL1; 11.
DR SUPFAM; SSF57440; SSF57440; 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
