ID   ITB4_MOUSE              Reviewed;        1818 AA.
AC   A2A863; A2A865; A2A866; Q6PCS0; Q8R3J1; Q91W15;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Integrin beta-4;
DE   AltName: CD_antigen=CD104;
DE   Flags: Precursor;
GN   Name=Itgb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=8359687; DOI=10.1016/0378-1119(93)90421-x;
RA   Kennel S.J., Foote L.J., Cimino L., Rizzo M.G., Chang L.Y., Sacchi A.;
RT   "Sequence of a cDNA encoding the beta 4 subunit of murine integrin.";
RL   Gene 130:209-216(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1818 (ISOFORM 2).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1071 AND SER-1470, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a
CC       critical structural role in the hemidesmosome of epithelial cells. Is
CC       required for the regulation of keratinocyte polarity and motility.
CC       ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is
CC       essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this
CC       binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and
CC       this binding is essential for IGF2 signaling.
CC       {ECO:0000250|UniProtKB:P16144}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4 associates
CC       with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via
CC       cytoplasmic region). Interacts (via cytoplasmic region) with DST
CC       isoform 3 (via N-terminus). Interacts (via cytoplasmic domain) with DST
CC       (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is found in a
CC       ternary complex with NRG1 and ERBB3. ITGA6:ITGB4 is found in a ternary
CC       complex with IGF1 and IGF1R. ITGA6:ITGB4 interacts with IGF2.
CC       {ECO:0000250|UniProtKB:P16144}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-
CC       anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}.
CC       Note=Colocalizes with DST at the leading edge of migrating
CC       keratinocytes. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2A863-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A863-2; Sequence=VSP_037636;
CC       Name=3;
CC         IsoId=A2A863-3; Sequence=VSP_037636, VSP_037637;
CC   -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin
CC       and probably also recruit BP230. {ECO:0000250}.
CC   -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation-
CC       binding sites: the ligand-associated metal ion-binding site (LIMBS or
CC       SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent
CC       MIDAS site (ADMIDAS). This domain is also part of the ligand-binding
CC       site. {ECO:0000250|UniProtKB:P05106}.
CC   -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
CC       proximal region, enhancing stability and cell surface expression.
CC       Palmitoylation also promotes secondary association with tertaspanins
CC       (By similarity). {ECO:0000250|UniProtKB:P16144}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR   EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL645647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006632; AAH06632.1; -; mRNA.
DR   EMBL; BC025194; AAH25194.1; -; mRNA.
DR   EMBL; BC059192; AAH59192.1; -; mRNA.
DR   PIR; JN0786; JN0786.
DR   RefSeq; XP_006532635.1; XM_006532572.3. [A2A863-1]
DR   RefSeq; XP_006532636.1; XM_006532573.3. [A2A863-3]
DR   RefSeq; XP_006532637.1; XM_006532574.2.
DR   AlphaFoldDB; A2A863; -.
DR   SMR; A2A863; -.
DR   BioGRID; 228715; 11.
DR   ComplexPortal; CPX-3120; integrin alpha6-beta4 complex.
DR   IntAct; A2A863; 2.
DR   STRING; 10090.ENSMUSP00000127604; -.
DR   GlyCosmos; A2A863; 5 sites, No reported glycans.
DR   GlyGen; A2A863; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; A2A863; -.
DR   PhosphoSitePlus; A2A863; -.
DR   MaxQB; A2A863; -.
DR   PaxDb; 10090-ENSMUSP00000102068; -.
DR   PeptideAtlas; A2A863; -.
DR   ProteomicsDB; 301690; -. [A2A863-1]
DR   ProteomicsDB; 301691; -. [A2A863-2]
DR   ProteomicsDB; 301692; -. [A2A863-3]
DR   Antibodypedia; 3934; 1159 antibodies from 44 providers.
DR   DNASU; 192897; -.
DR   Ensembl; ENSMUST00000068981.13; ENSMUSP00000070811.7; ENSMUSG00000020758.16. [A2A863-2]
DR   Ensembl; ENSMUST00000106458.2; ENSMUSP00000102066.2; ENSMUSG00000020758.16. [A2A863-1]
DR   Ensembl; ENSMUST00000106460.9; ENSMUSP00000102068.3; ENSMUSG00000020758.16. [A2A863-3]
DR   Ensembl; ENSMUST00000106461.8; ENSMUSP00000102069.2; ENSMUSG00000020758.16. [A2A863-1]
DR   GeneID; 192897; -.
DR   UCSC; uc007mji.1; mouse. [A2A863-2]
DR   AGR; MGI:96613; -.
DR   CTD; 3691; -.
DR   MGI; MGI:96613; Itgb4.
DR   VEuPathDB; HostDB:ENSMUSG00000020758; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   GeneTree; ENSGT01100000263555; -.
DR   HOGENOM; CLU_237558_0_0_1; -.
DR   InParanoid; A2A863; -.
DR   OrthoDB; 5475862at2759; -.
DR   PhylomeDB; A2A863; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-MMU-3000170; Syndecan interactions.
DR   Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR   BioGRID-ORCS; 192897; 2 hits in 63 CRISPR screens.
DR   ChiTaRS; Itgb4; mouse.
DR   PRO; PR:A2A863; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; A2A863; Protein.
DR   Bgee; ENSMUSG00000020758; Expressed in substantia propria of cornea and 130 other cell types or tissues.
DR   ExpressionAtlas; A2A863; baseline and differential.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005938; C:cell cortex; ISO:MGI.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0030056; C:hemidesmosome; IDA:MGI.
DR   GO; GO:0008305; C:integrin complex; IDA:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR   GO; GO:0031994; F:insulin-like growth factor I binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0038132; F:neuregulin binding; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR   GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR   GO; GO:0031581; P:hemidesmosome assembly; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IGI:MGI.
DR   GO; GO:0035878; P:nail development; ISO:MGI.
DR   GO; GO:0032290; P:peripheral nervous system myelin formation; IGI:MGI.
DR   GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR   GO; GO:0043589; P:skin morphogenesis; ISO:MGI.
DR   GO; GO:0061450; P:trophoblast cell migration; IMP:MGI.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 4.10.1240.30; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR012013; Integrin_bsu-4.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF42; INTEGRIN BETA-4; 1.
DR   Pfam; PF03160; Calx-beta; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002513; Integrin_B4; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00237; Calx_beta; 1.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF141072; CalX-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
DR   Genevisible; A2A863; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Integrin; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..1818
FT                   /note="Integrin beta-4"
FT                   /id="PRO_0000379078"
FT   TOPO_DOM        29..712
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        734..1818
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..74
FT                   /note="PSI"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          132..310
FT                   /note="VWFA"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          458..504
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          505..544
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          545..583
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          584..621
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DOMAIN          981..1086
FT                   /note="Calx-beta"
FT   DOMAIN          1131..1220
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1224..1323
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1526..1621
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1639..1735
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          195..200
FT                   /note="Involved in NRG1- and IGF1-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16144"
FT   REGION          734..751
FT                   /note="Palmitoylated on several cysteines"
FT                   /evidence="ECO:0000250"
FT   REGION          1115..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1402..1433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           473..475
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1005..1007
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in LIMBS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="in MIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   BINDING         351
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in ADMIDAS binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64632"
FT   MOD_RES         1071
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64632"
FT   MOD_RES         1451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16144"
FT   MOD_RES         1454
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16144"
FT   MOD_RES         1470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1483
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16144"
FT   MOD_RES         1490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64632"
FT   MOD_RES         1526
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16144"
FT   MOD_RES         1787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64632"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        581
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        619
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..49
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        39..457
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        42..62
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        52..73
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        246..289
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        459..478
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        470..481
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        483..492
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        494..522
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        505..520
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        514..525
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        527..538
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        545..559
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        553..564
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        566..575
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        577..600
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        584..598
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        592..603
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        605..616
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        628..673
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        634..653
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        637..650
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   DISULFID        682..708
FT                   /evidence="ECO:0000250|UniProtKB:P05106"
FT   VAR_SEQ         1372..1436
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8359687"
FT                   /id="VSP_037636"
FT   VAR_SEQ         1515
FT                   /note="Q -> QGLPPIWEDGRSRLPLSWTLGSLSRAHMKGVPASRGSPDSIILAGQS
FT                   AAPSWGT (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037637"
FT   CONFLICT        17
FT                   /note="A -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67..68
FT                   /note="EL -> DV (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="D -> V (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="P -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="S -> T (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        666
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        709..713
FT                   /note="PPGSF -> LPAPS (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        851
FT                   /note="E -> K (in Ref. 3; AAH59192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        877
FT                   /note="T -> A (in Ref. 1 and 3; AAH06632/AAH59192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        972
FT                   /note="G -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105..1107
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1204
FT                   /note="Q -> K (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1292
FT                   /note="E -> D (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1537
FT                   /note="P -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1552
FT                   /note="M -> T (in Ref. 1 and 3;
FT                   AAH06632/AAH25194/AAH59192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1564..1566
FT                   /note="NGG -> TCV (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1590..1592
FT                   /note="HSY -> YSH (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1653
FT                   /note="L -> P (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1662..1663
FT                   /note="RP -> SR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1744
FT                   /note="H -> N (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1759
FT                   /note="V -> M (in Ref. 3; AAH25194)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1818 AA;  201650 MW;  CA41A7E6B4E20B59 CRC64;
     MAGPCCSPWV KLLLLAAMLS ASLPGDLANR CKKAQVKSCT ECIRVDKSCA YCTDELFKER
     RCNTQAELLA AGCRGESILV MESSLEITEN TQIDTSLHRS QVSPQGLQVR LRPGEERSFV
     FQVFEPLESP VDLYILMDFS NSMSDDLDNL KQMGQNLAKI LRQLTSDYTI GFGKFVDKVS
     VPQTDMRPEK LKEPWPNSDP PFSFKNVISL TENVEEFWNK LQGERISGNL DAPEGGFDAI
     LQTAVCTRDI GWRADSTHLL VFSTESAFHY EADGANVLAG IMNRNDEKCH LDASGAYTQY
     KTQDYPSVPT LVRLLAKHNI IPIFAVTNYS YSYYEKLHKY FPVSSLGVLQ EDSSNIVELL
     EEAFYRIRSN LDIRALDSPR GLRTEVTSDT LQKTETGSFH IKRGEVGTYN VHLRAVEDID
     GTHVCQLAKE DQGGNIHLKP SFSDGLRMDA SVICDVCPCE LQKEVRSARC HFRGDFMCGH
     CVCNEGWSGK TCNCSTGSLS DTQPCLREGE DKPCSGHGEC QCGRCVCYGE GRYEGHFCEY
     DNFQCPRTSG FLCNDRGRCS MGECVCEPGW TGRSCDCPLS NATCIDSNGG ICNGRGYCEC
     GRCHCNQQSL YTDTTCEINY SAIRLGLCED LRSCVQCQAW GTGEKKGRAC DDCPFKVKMV
     DELKKAEEVV EYCSFRDEDD DCTYSYNVEG DGSPGPNSTV LVHKKKDCPP GSFWWLIPLL
     IFLLLLLALL LLLCWKYCAC CKACLGLLPC CNRGHMVGFK EDHYMLRENL MASDHLDTPM
     LRSGNLKGRD TVRWKITNNV QRPGFATHAA STSPTELVPY GLSLRLGRLC TENLMKPGTR
     ECDQLRQEVE ENLNEVYRQV SGAHKLQQTK FRQQPNTGKK QDHTIVDTVL LAPRSAKQML
     LKLTEKQVEQ GSFHELKVAP GYYTVTAEQD ARGMVEFQEG VELVDVRVPL FIRPEDDDEK
     QLLVEAIDVP VGTATLGRRL VNITIIKEQA SGVVSFEQPE YSVSRGDQVA RIPVIRHILD
     NGKSQVSYST QDNTAHGHRD YVPVEGELLF HPGETWKELQ VKLLELQEVD SLLRGRQVRR
     FQVQLSNPKF GARLGQPSTT TVILGEHDET DRSLINQTLS SPPPPHGDLG APQNPNAKAA
     GSRKIHFNWL PPPGKPMGYR VKYWIQGDSE SEAHLLDSKV PSVELTNLYP YCDYEMKVCA
     YGAQGEGPYS SLVSCRTHQE VPSEPGRLAF NVVSSTVTQL SWAEPAETNG EITAYEVCYG
     LVNEDNRPIG PMKKVLVDNP KNRMLLIENL RESQPYRYTV KARNGAGWGP EREAIINLAT
     QPKRPMSIPI IPDIPIVDAQ GGEDYENFLM YSDDVLRSPA SSQRPSVSDD TGCGWKFEPL
     LGEELDLRRV TWRLPPELIP RLSASSGRSD EDGSVAGGVE GEGSGWIRGA TPRPPGEHLV
     NGRMDFAYPG SANSLHRMTA ANVAYGTHLS PHLSHRVLST SSTLTRDYHS LTRTEHSHSG
     TLPRDYSTLT SLSSQDSRGA VGVPDTPTRL VFSALGPTSL KVSWQEPQCD RMLLGYSVEY
     QLLNGGEMHR LNIPNPGQTS VVVEDLLPNH SYVFRVRAQS QEGWGREREG VITIESQVHP
     QSPLCPLPGS AFTLSTPSAP GPLVFTALSP DSLQLSWERP RRPNGDILGY LVTCEMAQGG
     APARTFRVDG DNPESRLTVP GLSENVPYKF KVQARTTEGF GPEREGIITI ESQVGGPFPQ
     LGSHSGLFQN PVQSEFSSVT STHSTTTEPF LMDGLTLGTQ RLEAGGSLTR HVTQEFVTRT
     LTASGSLSTH MDQQFFQT
//