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Database: UniProt
Entry: P16144
LinkDB: P16144
Original site: P16144 
ID   ITB4_HUMAN              Reviewed;        1822 AA.
AC   P16144; A0AVL6; O14690; O14691; O15339; O15340; O15341; Q0VF97;
AC   Q9UIQ4;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 5.
DT   10-APR-2019, entry version 234.
DE   RecName: Full=Integrin beta-4;
DE   AltName: Full=GP150;
DE   AltName: CD_antigen=CD104;
DE   Flags: Precursor;
GN   Name=ITGB4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4A), AND VARIANT PRO-1779.
RX   PubMed=2311577;
RA   Suzuki S., Naitoh Y.;
RT   "Amino acid sequence of a novel integrin beta 4 subunit and primary
RT   expression of the mRNA in epithelial cells.";
RL   EMBO J. 9:757-763(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4B), AND VARIANT PRO-1779.
RX   PubMed=2311578;
RA   Hogervorst F., Kuikman I., von Dem Borne A.E.G.K., Sonnenberg A.;
RT   "Cloning and sequence analysis of beta-4 cDNA: an integrin subunit
RT   that contains a unique 118 kd cytoplasmic domain.";
RL   EMBO J. 9:765-770(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4C).
RC   TISSUE=Pancreas;
RX   PubMed=1976638; DOI=10.1083/jcb.111.4.1593;
RA   Tamura R.N., Rozzo C., Starr L., Chambers J., Reichardt L.F.,
RA   Cooper H.M., Quaranta V.;
RT   "Epithelial integrin alpha 6 beta 4: complete primary structure of
RT   alpha 6 and variant forms of beta 4.";
RL   J. Cell Biol. 111:1593-1604(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-4A; BETA-4B
RP   AND BETA-4C), AND VARIANTS SER-1764 AND PRO-1779.
RX   PubMed=9194858;
RA   Pulkkinen L., Kurtz K.S., Xu Y., Bruckner-Tuderman L., Uitto J.;
RT   "Genomic organization of the integrin beta 4 gene (ITGB4): a
RT   homozygous splice-site mutation in a patient with junctional
RT   epidermolysis bullosa associated with pyloric atresia.";
RL   Lab. Invest. 76:823-833(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BETA-4A; BETA-4B AND
RP   BETA-4C), AND VARIANTS SER-1764 AND PRO-1779.
RC   TISSUE=Lung;
RX   PubMed=9166594; DOI=10.1007/s003359900467;
RA   Iacovacci S., Gagnoux-Palacios L., Zambruno G., Meneguzzi G.,
RA   D'Alessio M.;
RT   "Genomic organization of the human integrin beta 4 gene.";
RL   Mamm. Genome 8:448-450(1997).
RN   [6]
RP   SEQUENCE REVISION.
RA   D'Alessio M.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM BETA-4E), AND
RP   VARIANT PRO-1779.
RX   PubMed=9207246; DOI=10.1006/bbrc.1997.6892;
RA   van Leusden M.R., Kuikman I., Sonnenberg A.;
RT   "The unique cytoplasmic domain of the human integrin variant beta4E is
RT   produced by partial retention of intronic sequences.";
RL   Biochem. Biophys. Res. Commun. 235:826-830(1997).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-4A), AND VARIANT
RP   PRO-1779.
RC   TISSUE=Cerebellum;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 28-46.
RX   PubMed=2542022;
RA   Kajiji S., Tamura R.N., Quaranta V.;
RT   "A novel integrin (alpha E beta 4) from human epithelial cells
RT   suggests a fourth family of integrin adhesion receptors.";
RL   EMBO J. 8:673-680(1989).
RN   [12]
RP   ALTERNATIVE SPLICING (ISOFORM BETA-4D).
RX   PubMed=7982032;
RA   Clarke A.S., Lotz M.M., Mercurio A.M.;
RT   "A novel structural variant of the human beta 4 integrin cDNA.";
RL   Cell Adhes. Commun. 2:1-6(1994).
RN   [13]
RP   INTERACTION WITH DSP.
RX   PubMed=10637308; DOI=10.1091/mbc.11.1.277;
RA   Hopkinson S.B., Jones J.C.;
RT   "The N terminus of the transmembrane protein BP180 interacts with the
RT   N-terminal domain of BP230, thereby mediating keratin cytoskeleton
RT   anchorage to the cell surface at the site of the hemidesmosome.";
RL   Mol. Biol. Cell 11:277-286(2000).
RN   [14]
RP   INTERACTION WITH DST.
RX   PubMed=11375975; DOI=10.1074/jbc.M011005200;
RA   Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F.,
RA   Saurat J.-H., Sonnenberg A., Borradori L.;
RT   "The hemidesmosomal protein bullous pemphigoid antigen 1 and the
RT   integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple
RT   alternative splice variants of ERBIN and analysis of their tissue
RT   expression.";
RL   J. Biol. Chem. 276:32427-32436(2001).
RN   [15]
RP   INVOLVEMENT IN WC-EBS.
RX   PubMed=12485428; DOI=10.1046/j.1523-1747.2002.19609.x;
RA   Jonkman M.F., Pas H.H., Nijenhuis M., Kloosterhuis G., Steege G.;
RT   "Deletion of a cytoplasmic domain of integrin beta4 causes
RT   epidermolysis bullosa simplex.";
RL   J. Invest. Dermatol. 119:1275-1281(2002).
RN   [16]
RP   FUNCTION, INTERACTION WITH COL17A1 AND DST, CHARACTERIZATION OF
RP   VARIANT TRP-1281, AND SUBCELLULAR LOCATION.
RX   PubMed=12482924; DOI=10.1242/jcs.00241;
RA   Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
RT   "Analysis of the interactions between BP180, BP230, plectin and the
RT   integrin alpha6beta4 important for hemidesmosome assembly.";
RL   J. Cell Sci. 116:387-399(2003).
RN   [17]
RP   PALMITOYLATION.
RX   PubMed=15611341; DOI=10.1083/jcb.200404100;
RA   Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
RT   "Palmitoylation supports assembly and function of integrin-tetraspanin
RT   complexes.";
RL   J. Cell Biol. 167:1231-1240(2004).
RN   [18]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-695.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1530, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [21]
RP   FUNCTION, INTERACTION WITH RAC1, AND SUBCELLULAR LOCATION.
RX   PubMed=19403692; DOI=10.1091/mbc.E09-01-0051;
RA   Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
RT   "BPAG1e maintains keratinocyte polarity through beta4 integrin-
RT   mediated modulation of Rac1 and cofilin activities.";
RL   Mol. Biol. Cell 20:2954-2962(2009).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [23]
RP   FUNCTION, BINDING TO NRG1, IDENTIFICATION IN A COMPLEX WITH NRG1 AND
RP   ERBB3, AND NRG1-BINDING REGION.
RX   PubMed=20682778; DOI=10.1074/jbc.M110.113878;
RA   Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
RA   Wang B., Takada Y.K., Takada Y.;
RT   "Direct binding of the EGF-like domain of neuregulin-1 to integrins
RT   ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
RT   signaling.";
RL   J. Biol. Chem. 285:31388-31398(2010).
RN   [24]
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.,
RA   Buerckstuemmer T., 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   [25]
RP   PALMITOYLATION BY DHHC3, AND SUBCELLULAR LOCATION.
RX   PubMed=22314500; DOI=10.1007/s00018-012-0924-6;
RA   Sharma C., Rabinovitz I., Hemler M.E.;
RT   "Palmitoylation by DHHC3 is critical for the function, expression, and
RT   stability of integrin alpha6beta4.";
RL   Cell. Mol. Life Sci. 69:2233-2244(2012).
RN   [26]
RP   FUNCTION, BINDING TO IGF1, IDENTIFICATION IN A COMPLEX WITH IGF1 AND
RP   IGF1R, AND IGF1-BINDING REGION.
RX   PubMed=22351760; DOI=10.1074/jbc.M111.304170;
RA   Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y.,
RA   Sekiguchi K., Takada Y.K., Takada Y.;
RT   "Cross-talk between integrin alpha6beta4 and insulin-like growth
RT   factor-1 receptor (IGF1R) through direct alpha6beta4 binding to IGF1
RT   and subsequent alpha6beta4-IGF1-IGF1R ternary complex formation in
RT   anchorage-independent conditions.";
RL   J. Biol. Chem. 287:12491-12500(2012).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1069; SER-1454;
RP   SER-1457; SER-1474; THR-1487 AND THR-1530, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [28]
RP   FUNCTION, AND INTERACTION WITH IGF2.
RX   PubMed=28873464; DOI=10.1371/journal.pone.0184285;
RA   Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K.,
RA   Takada Y.;
RT   "Direct integrin binding to insulin-like growth factor-2 through the
RT   C-domain is required for insulin-like growth factor receptor type 1
RT   (IGF1R) signaling.";
RL   PLoS ONE 12:E0184285-E0184285(2017).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1126-1320.
RX   PubMed=10428948; DOI=10.1093/emboj/18.15.4087;
RA   de Pereda J.M., Wiche G., Liddington R.C.;
RT   "Crystal structure of a tandem pair of fibronectin type III domains
RT   from the cytoplasmic tail of integrin alpha6beta4.";
RL   EMBO J. 18:4087-4095(1999).
RN   [30]
RP   STRUCTURE BY NMR OF 1515-1622.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the fibronectin type III domain of human
RT   integrin beta-4.";
RL   Submitted (APR-2008) to the PDB data bank.
RN   [31]
RP   VARIANTS EB-PA TYR-61; CYS-252; ARG-562 AND TRP-1281.
RX   PubMed=9792864; DOI=10.1086/302116;
RA   Pulkkinen L., Rouan F., Bruckner-Tuderman L., Wallerstein R.,
RA   Garzon M., Brown T., Smith L., Carter W.G., Uitto J.;
RT   "Novel ITGB4 mutations in lethal and nonlethal variants of
RT   epidermolysis bullosa with pyloric atresia: missense versus
RT   nonsense.";
RL   Am. J. Hum. Genet. 63:1376-1387(1998).
RN   [32]
RP   VARIANT EB-PA GLY-245.
RX   PubMed=9422533;
RA   Pulkkinen L., Kim D.U., Uitto J.;
RT   "Epidermolysis bullosa with pyloric atresia: novel mutations in the
RT   beta-4 integrin gene (ITGB4).";
RL   Am. J. Pathol. 152:157-166(1998).
RN   [33]
RP   VARIANT EB-PA PRO-156.
RX   PubMed=9546354;
RA   Pulkkinen L., Bruckner-Tuderman L., August C., Uitto J.;
RT   "Compound heterozygosity for missense (L156P) and nonsense (R554X)
RT   mutations in the beta-4 integrin gene (ITGB4) underlies mild,
RT   nonlethal phenotype of epidermolysis bullosa with pyloric atresia.";
RL   Am. J. Pathol. 152:935-941(1998).
RN   [34]
RP   VARIANT EB-PA ARG-38.
RX   PubMed=9892956; DOI=10.1046/j.1365-2133.1998.02515.x;
RA   Mellerio J.E., Pulkkinen L., McMillan J.R., Lake B.D., Horn H.M.,
RA   Tidman M.J., Harper J.I., McGrath J.A., Uitto J., Eady R.A.J.;
RT   "Pyloric atresia-junctional epidermolysis bullosa syndrome: mutations
RT   in the integrin beta4 gene (ITGB4) in two unrelated patients with mild
RT   disease.";
RL   Br. J. Dermatol. 139:862-871(1998).
RN   [35]
RP   VARIANT EB-PA TRP-1281.
RX   PubMed=10873890; DOI=10.1053/ajkd.2000.8293;
RA   Kambham N., Tanji N., Seigle R.L., Markowitz G.S., Pulkkinen L.,
RA   Uitto J., D'Agati V.D.;
RT   "Congenital focal segmental glomerulosclerosis associated with beta4
RT   integrin mutation and epidermolysis bullosa.";
RL   Am. J. Kidney Dis. 36:190-196(2000).
RN   [36]
RP   VARIANT GABEB ASP-931.
RX   PubMed=10792571; DOI=10.1046/j.1523-1747.2000.00960-3.x;
RA   Inoue M., Tamai K., Shimizu H., Owaribe K., Nakama T., Hashimoto T.,
RA   McGrath J.A.;
RT   "A homozygous missense mutation in the cytoplasmic tail of beta4
RT   integrin, G931D, that disrupts hemidesmosome assembly and underlies
RT   non-Herlitz junctional epidermolysis bullosa without pyloric
RT   atresia?";
RL   J. Invest. Dermatol. 114:1061-1064(2000).
RN   [37]
RP   VARIANTS EB-PA.
RX   PubMed=11251584; DOI=10.1046/j.1365-2133.2001.04038.x;
RA   Ashton G.H.S., Sorelli P., Mellerio J.E., Keane F.M., Eady R.A.J.,
RA   McGrath J.A.;
RT   "Alpha 6 beta 4 integrin abnormalities in junctional epidermolysis
RT   bullosa with pyloric atresia.";
RL   Br. J. Dermatol. 144:408-414(2001).
RN   [38]
RP   VARIANTS HIS-98 AND LEU-844.
RX   PubMed=11289717; DOI=10.1007/s100380170122;
RA   Hirano A., Nagai H., Harada H., Terada Y., Haga S., Kajiwara T.,
RA   Emi M.;
RT   "Nine novel single-nucleotide polymorphisms in the integrin beta4
RT   (ITGB4) gene in the Japanese population.";
RL   J. Hum. Genet. 46:35-37(2001).
RN   [39]
RP   VARIANTS EB-PA TYR-131; CYS-252; ASP-273; CYS-283; ASP-325; PRO-336
RP   AND HIS-1225, AND VARIANT GLN-1216.
RX   PubMed=11328943; DOI=10.1203/00006450-200105000-00003;
RA   Nakano A., Pulkkinen L., Murrell D., Rico J., Lucky A.W., Garzon M.,
RA   Stevens C.A., Robertson S., Pfendner E., Uitto J.;
RT   "Epidermolysis bullosa with congenital pyloric atresia: novel
RT   mutations in the beta 4 integrin gene (ITGB4) and genotype/phenotype
RT   correlations.";
RL   Pediatr. Res. 49:618-626(2001).
CC   -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. Plays
CC       a critical structural role in the hemidesmosome of epithelial
CC       cells. Is required for the regulation of keratinocyte polarity and
CC       motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this
CC       binding is essential for NRG1-ERBB signaling (PubMed:20682778).
CC       ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1
CC       signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this
CC       binding is essential for IGF2 signaling (PubMed:28873464).
CC       {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692,
CC       ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760,
CC       ECO:0000269|PubMed:28873464}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4
CC       associates with alpha-6. Interacts (via cytoplasmic region) with
CC       COL17A1 (via cytoplasmic region). Interacts (via cytoplasmic
CC       region) with DST isoform 3 (via N-terminus). Isoform beta-4a
CC       interacts (via cytoplasmic domain) with DST (via N-terminus).
CC       Interacts with RAC1. ITGA6:ITGB4 is found in a ternary complex
CC       with NRG1 and ERBB3 (PubMed:20682778). ITGA6:ITGB4 is found in a
CC       ternary complex with IGF1 and IGF1R (PubMed:22351760). ITGA6:ITGB4
CC       interacts with IGF2 (PubMed:28873464).
CC       {ECO:0000269|PubMed:10637308, ECO:0000269|PubMed:11375975,
CC       ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692,
CC       ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760,
CC       ECO:0000269|PubMed:28873464}.
CC   -!- INTERACTION:
CC       Q96B67:ARRDC3; NbExp=3; IntAct=EBI-948678, EBI-2875665;
CC       Q8R5M8-2:Cadm1 (xeno); NbExp=3; IntAct=EBI-948678, EBI-5651941;
CC       P23229:ITGA6; NbExp=3; IntAct=EBI-948678, EBI-2436548;
CC       Q15149:PLEC; NbExp=7; IntAct=EBI-948678, EBI-297903;
CC       Q9QXS1-3:Plec (xeno); NbExp=4; IntAct=EBI-948678, EBI-16145475;
CC       Q05397:PTK2; NbExp=7; IntAct=EBI-948678, EBI-702142;
CC       O95136:S1PR2; NbExp=2; IntAct=EBI-948678, EBI-10634606;
CC       Q99500:S1PR3; NbExp=3; IntAct=EBI-948678, EBI-10634734;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell membrane; Lipid-anchor. Cell junction,
CC       hemidesmosome. Note=Colocalizes with DST at the leading edge of
CC       migrating keratinocytes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=Beta-4C;
CC         IsoId=P16144-1; Sequence=Displayed;
CC       Name=Beta-4A;
CC         IsoId=P16144-2; Sequence=VSP_002749;
CC       Name=Beta-4B;
CC         IsoId=P16144-3; Sequence=VSP_002749, VSP_002750;
CC       Name=Beta-4D;
CC         IsoId=P16144-4; Sequence=VSP_002749, VSP_002751;
CC       Name=Beta-4E;
CC         IsoId=P16144-5; Sequence=VSP_002747, VSP_002748;
CC   -!- TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly
CC       expressed by epithelia. Isoform beta-4D is also expressed in colon
CC       and placenta. Isoform beta-4E is also expressed in epidermis,
CC       lung, duodenum, heart, spleen and stomach.
CC   -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and
CC       plectin and probably also recruit BP230.
CC   -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
CC       proximal region, enhancing stability and cell surface expression.
CC       Palmitoylation also promotes secundary association with
CC       tertaspanins. {ECO:0000269|PubMed:15611341,
CC       ECO:0000269|PubMed:22314500}.
CC   -!- DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB-
CC       PA) [MIM:226730]: An autosomal recessive, frequently lethal,
CC       epidermolysis bullosa with variable involvement of skin, nails,
CC       mucosa, and with variable effects on the digestive system. It is
CC       characterized by mucocutaneous fragility, aplasia cutis congenita,
CC       and gastrointestinal atresia, which most commonly affects the
CC       pylorus. Pyloric atresia is a primary manifestation rather than a
CC       scarring process secondary to epidermolysis bullosa.
CC       {ECO:0000269|PubMed:10873890, ECO:0000269|PubMed:11251584,
CC       ECO:0000269|PubMed:11328943, ECO:0000269|PubMed:9422533,
CC       ECO:0000269|PubMed:9546354, ECO:0000269|PubMed:9792864,
CC       ECO:0000269|PubMed:9892956}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB)
CC       [MIM:226650]: A non-lethal, adult form of junctional epidermolysis
CC       bullosa characterized by life-long blistering of the skin,
CC       associated with hair and tooth abnormalities.
CC       {ECO:0000269|PubMed:10792571}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC-
CC       EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa
CC       characterized by blistering limited to palmar and plantar areas of
CC       the skin. {ECO:0000269|PubMed:12485428}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA37656.1; Type=Frameshift; Positions=1413, 1429; Evidence={ECO:0000305};
CC       Sequence=CAA37656.1; Type=Frameshift; Positions=1414, 1429; Evidence={ECO:0000305};
DR   EMBL; X51841; CAA36134.1; -; mRNA.
DR   EMBL; X52186; CAA36433.1; -; mRNA.
DR   EMBL; X53587; CAA37656.1; ALT_FRAME; mRNA.
DR   EMBL; U66541; AAC51634.1; -; Genomic_DNA.
DR   EMBL; U66530; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66531; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66532; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66533; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66534; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66535; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66536; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66537; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66538; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66539; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66540; AAC51634.1; JOINED; Genomic_DNA.
DR   EMBL; U66541; AAC51633.1; -; Genomic_DNA.
DR   EMBL; U66530; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66531; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66532; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66533; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66534; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66535; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66536; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66537; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66538; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66539; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66540; AAC51633.1; JOINED; Genomic_DNA.
DR   EMBL; U66541; AAC51632.1; -; Genomic_DNA.
DR   EMBL; U66530; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66531; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66532; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66533; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66534; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66535; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66536; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66537; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66538; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66539; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; U66540; AAC51632.1; JOINED; Genomic_DNA.
DR   EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89305.1; -; Genomic_DNA.
DR   EMBL; BC118916; AAI18917.1; -; mRNA.
DR   EMBL; BC126411; AAI26412.1; -; mRNA.
DR   EMBL; AJ251004; CAB61345.1; -; Genomic_DNA.
DR   EMBL; Y11107; CAB61345.1; JOINED; Genomic_DNA.
DR   EMBL; AF011375; AAB65421.1; -; mRNA.
DR   EMBL; AF011376; AAB65422.1; -; Genomic_DNA.
DR   CCDS; CCDS11727.1; -. [P16144-1]
DR   CCDS; CCDS32736.1; -. [P16144-3]
DR   CCDS; CCDS58599.1; -. [P16144-2]
DR   PIR; JC5545; JC5545.
DR   PIR; S12380; A36429.
DR   RefSeq; NP_000204.3; NM_000213.4. [P16144-1]
DR   RefSeq; NP_001005619.1; NM_001005619.1. [P16144-3]
DR   RefSeq; NP_001005731.1; NM_001005731.2. [P16144-2]
DR   RefSeq; NP_001308052.1; NM_001321123.1. [P16144-2]
DR   UniGene; Hs.632226; -.
DR   PDB; 1QG3; X-ray; 2.15 A; A/B=1126-1320.
DR   PDB; 2YRZ; NMR; -; A=1518-1622.
DR   PDB; 3F7P; X-ray; 2.75 A; C/D/E=1126-1369.
DR   PDB; 3F7Q; X-ray; 1.75 A; A/B=1126-1355.
DR   PDB; 3F7R; X-ray; 2.04 A; A=1126-1369.
DR   PDB; 3FQ4; X-ray; 1.49 A; A/B=989-1107.
DR   PDB; 3FSO; X-ray; 1.41 A; A/B=989-1107.
DR   PDB; 3H6A; X-ray; 1.61 A; A/B=989-1107.
DR   PDB; 4Q58; X-ray; 4.00 A; C/D=1126-1320.
DR   PDB; 4WTW; X-ray; 1.61 A; A/B=1527-1618.
DR   PDB; 4WTX; X-ray; 1.50 A; A=1642-1736.
DR   PDBsum; 1QG3; -.
DR   PDBsum; 2YRZ; -.
DR   PDBsum; 3F7P; -.
DR   PDBsum; 3F7Q; -.
DR   PDBsum; 3F7R; -.
DR   PDBsum; 3FQ4; -.
DR   PDBsum; 3FSO; -.
DR   PDBsum; 3H6A; -.
DR   PDBsum; 4Q58; -.
DR   PDBsum; 4WTW; -.
DR   PDBsum; 4WTX; -.
DR   ProteinModelPortal; P16144; -.
DR   SMR; P16144; -.
DR   BioGrid; 109897; 36.
DR   ComplexPortal; CPX-1822; Integrin alpha6-beta4 complex.
DR   CORUM; P16144; -.
DR   DIP; DIP-40182N; -.
DR   ELM; P16144; -.
DR   IntAct; P16144; 89.
DR   MINT; P16144; -.
DR   STRING; 9606.ENSP00000200181; -.
DR   DrugBank; DB05122; R1295.
DR   GlyConnect; 1417; -.
DR   iPTMnet; P16144; -.
DR   PhosphoSitePlus; P16144; -.
DR   SwissPalm; P16144; -.
DR   BioMuta; ITGB4; -.
DR   DMDM; 317373584; -.
DR   EPD; P16144; -.
DR   jPOST; P16144; -.
DR   MaxQB; P16144; -.
DR   PaxDb; P16144; -.
DR   PeptideAtlas; P16144; -.
DR   PRIDE; P16144; -.
DR   ProteomicsDB; 53292; -.
DR   ProteomicsDB; 53293; -. [P16144-2]
DR   ProteomicsDB; 53294; -. [P16144-3]
DR   ProteomicsDB; 53295; -. [P16144-4]
DR   ProteomicsDB; 53296; -. [P16144-5]
DR   Ensembl; ENST00000200181; ENSP00000200181; ENSG00000132470. [P16144-1]
DR   Ensembl; ENST00000449880; ENSP00000400217; ENSG00000132470. [P16144-3]
DR   Ensembl; ENST00000450894; ENSP00000405536; ENSG00000132470. [P16144-2]
DR   Ensembl; ENST00000579662; ENSP00000463651; ENSG00000132470. [P16144-2]
DR   GeneID; 3691; -.
DR   KEGG; hsa:3691; -.
DR   UCSC; uc002jpg.3; human. [P16144-1]
DR   CTD; 3691; -.
DR   DisGeNET; 3691; -.
DR   EuPathDB; HostDB:ENSG00000132470.13; -.
DR   GeneCards; ITGB4; -.
DR   GeneReviews; ITGB4; -.
DR   H-InvDB; HIX0039036; -.
DR   HGNC; HGNC:6158; ITGB4.
DR   HPA; CAB002422; -.
DR   HPA; CAB005258; -.
DR   HPA; HPA036348; -.
DR   HPA; HPA036349; -.
DR   MalaCards; ITGB4; -.
DR   MIM; 131800; phenotype.
DR   MIM; 147557; gene.
DR   MIM; 226650; phenotype.
DR   MIM; 226730; phenotype.
DR   neXtProt; NX_P16144; -.
DR   OpenTargets; ENSG00000132470; -.
DR   Orphanet; 158684; Epidermolysis bullosa simplex with pyloric atresia.
DR   Orphanet; 79402; Junctional epidermolysis bullosa, generalized intermediate.
DR   Orphanet; 79403; Junctional epidermolysis bullosa-pyloric atresia syndrome.
DR   Orphanet; 251393; Localized junctional epidermolysis bullosa, non-Herlitz type.
DR   PharmGKB; PA29957; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000231105; -.
DR   HOVERGEN; HBG006189; -.
DR   InParanoid; P16144; -.
DR   KO; K06525; -.
DR   OMA; KVKYWIQ; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P16144; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000170; Syndecan interactions.
DR   Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR   SignaLink; P16144; -.
DR   SIGNOR; P16144; -.
DR   ChiTaRS; ITGB4; human.
DR   EvolutionaryTrace; P16144; -.
DR   GeneWiki; ITGB4; -.
DR   GenomeRNAi; 3691; -.
DR   PRO; PR:P16144; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000132470; Expressed in 215 organ(s), highest expression level in tibial nerve.
DR   ExpressionAtlas; P16144; baseline and differential.
DR   Genevisible; P16144; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0097186; P:amelogenesis; IMP:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0035878; P:nail development; IMP:UniProtKB.
DR   GO; GO:0072001; P:renal system development; IMP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
DR   GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR013111; EGF_extracell.
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; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF42; PTHR10082:SF42; 1.
DR   Pfam; PF03160; Calx-beta; 1.
DR   Pfam; PF07974; EGF_2; 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   SMART; SM00423; PSI; 1.
DR   SUPFAM; SSF141072; SSF141072; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disease mutation; Disulfide bond; Epidermolysis bullosa; Glycoprotein;
KW   Integrin; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000269|PubMed:2542022}.
FT   CHAIN        28   1822       Integrin beta-4.
FT                                /FTId=PRO_0000016346.
FT   TOPO_DOM     28    710       Extracellular. {ECO:0000255}.
FT   TRANSMEM    711    733       Helical. {ECO:0000255}.
FT   TOPO_DOM    734   1822       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       29     73       PSI.
FT   DOMAIN      131    329       VWFA.
FT   REPEAT      456    502       I.
FT   REPEAT      503    542       II.
FT   REPEAT      543    581       III.
FT   REPEAT      582    619       IV.
FT   DOMAIN      979   1084       Calx-beta.
FT   DOMAIN     1129   1218       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1222   1321       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1530   1625       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1643   1739       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   REGION      194    199       Involved in NRG1- and IGF1-binding.
FT                                {ECO:0000269|PubMed:20682778,
FT                                ECO:0000269|PubMed:22351760}.
FT   REGION      456    619       Cysteine-rich tandem repeats.
FT   REGION      732    749       Palmitoylated on several cysteines.
FT   MOD_RES     771    771       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64632}.
FT   MOD_RES    1069   1069       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1119   1119       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64632}.
FT   MOD_RES    1454   1454       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1457   1457       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1474   1474       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1487   1487       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1494   1494       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64632}.
FT   MOD_RES    1530   1530       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1791   1791       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64632}.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    491    491       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    579    579       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    617    617       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    695    695       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16335952}.
FT   DISULFID     30    455       {ECO:0000250}.
FT   DISULFID     38     48       {ECO:0000250}.
FT   DISULFID     41     72       {ECO:0000250}.
FT   DISULFID     51     61       {ECO:0000250}.
FT   DISULFID    245    288       {ECO:0000250}.
FT   DISULFID    424    671       {ECO:0000250}.
FT   DISULFID    452    457       {ECO:0000250}.
FT   DISULFID    468    479       {ECO:0000250}.
FT   DISULFID    476    512       {ECO:0000250}.
FT   DISULFID    481    490       {ECO:0000250}.
FT   DISULFID    492    503       {ECO:0000250}.
FT   DISULFID    518    523       {ECO:0000250}.
FT   DISULFID    520    551       {ECO:0000250}.
FT   DISULFID    525    536       {ECO:0000250}.
FT   DISULFID    557    562       {ECO:0000250}.
FT   DISULFID    564    573       {ECO:0000250}.
FT   DISULFID    575    582       {ECO:0000250}.
FT   DISULFID    596    601       {ECO:0000250}.
FT   DISULFID    598    648       {ECO:0000250}.
FT   DISULFID    603    614       {ECO:0000250}.
FT   DISULFID    626    635       {ECO:0000250}.
FT   DISULFID    632    706       {ECO:0000250}.
FT   DISULFID    651    680       {ECO:0000250}.
FT   VAR_SEQ     851    964       LNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAP
FT                                RSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGM
FT                                VEFQEGVELVDVRVPLFIRPEDDDEKQLLVEA -> VRTQE
FT                                LGLAGDVAERGLQADLRCTQAPADQVPAAAQCREKARPHHC
FT                                GHSADGAPLGQAGPAEAYREAGGTEGLPRPQGGPRLLHPHC
FT                                RPGRPGHGGVPGGRGAGGRTGAPLYPA (in isoform
FT                                Beta-4E). {ECO:0000303|PubMed:9207246}.
FT                                /FTId=VSP_002747.
FT   VAR_SEQ     965   1822       Missing (in isoform Beta-4E).
FT                                {ECO:0000303|PubMed:9207246}.
FT                                /FTId=VSP_002748.
FT   VAR_SEQ    1370   1439       Missing (in isoform Beta-4A, isoform
FT                                Beta-4B and isoform Beta-4D).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:2311577,
FT                                ECO:0000303|PubMed:2311578,
FT                                ECO:0000303|PubMed:9194858}.
FT                                /FTId=VSP_002749.
FT   VAR_SEQ    1519   1519       H -> HGLPPIWEHGRSRLPLSWALGSRSRAQMKGFPPSRG
FT                                PRDSIILAGRPAAPSWGP (in isoform Beta-4B).
FT                                {ECO:0000303|PubMed:2311578,
FT                                ECO:0000303|PubMed:9194858}.
FT                                /FTId=VSP_002750.
FT   VAR_SEQ    1678   1685       CEMAQGGG -> W (in isoform Beta-4D).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002751.
FT   VARIANT      38     38       C -> R (in EB-PA; mild form;
FT                                dbSNP:rs121912465).
FT                                {ECO:0000269|PubMed:9892956}.
FT                                /FTId=VAR_010652.
FT   VARIANT      61     61       C -> Y (in EB-PA; lethal form;
FT                                dbSNP:rs80338755).
FT                                {ECO:0000269|PubMed:9792864}.
FT                                /FTId=VAR_004006.
FT   VARIANT      98     98       R -> H (in dbSNP:rs143114124).
FT                                {ECO:0000269|PubMed:11289717}.
FT                                /FTId=VAR_011292.
FT   VARIANT     131    131       D -> Y (in EB-PA; lethal form).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011293.
FT   VARIANT     156    156       L -> P (in EB-PA; mild form;
FT                                dbSNP:rs121912461).
FT                                {ECO:0000269|PubMed:9546354}.
FT                                /FTId=VAR_004007.
FT   VARIANT     245    245       C -> G (in EB-PA; lethal form).
FT                                {ECO:0000269|PubMed:9422533}.
FT                                /FTId=VAR_004008.
FT   VARIANT     252    252       R -> C (in EB-PA; mild form;
FT                                dbSNP:rs201494421).
FT                                {ECO:0000269|PubMed:11328943,
FT                                ECO:0000269|PubMed:9792864}.
FT                                /FTId=VAR_004009.
FT   VARIANT     273    273       G -> D (in EB-PA; lethal form;
FT                                dbSNP:rs1476568580).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011294.
FT   VARIANT     283    283       R -> C (in EB-PA; dbSNP:rs1422797135).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011295.
FT   VARIANT     325    325       V -> D (in EB-PA; dbSNP:rs1304888529).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011296.
FT   VARIANT     336    336       L -> P (in EB-PA; mild form).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011297.
FT   VARIANT     478    478       Q -> H (in dbSNP:rs8079267).
FT                                /FTId=VAR_027803.
FT   VARIANT     562    562       C -> R (in EB-PA; mild form;
FT                                dbSNP:rs121912463).
FT                                {ECO:0000269|PubMed:9792864}.
FT                                /FTId=VAR_004010.
FT   VARIANT     844    844       R -> L (in dbSNP:rs140819116).
FT                                {ECO:0000269|PubMed:11289717}.
FT                                /FTId=VAR_011298.
FT   VARIANT     931    931       G -> D (in GABEB; dbSNP:rs121912466).
FT                                {ECO:0000269|PubMed:10792571}.
FT                                /FTId=VAR_011299.
FT   VARIANT    1216   1216       H -> Q (in dbSNP:rs149284152).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011300.
FT   VARIANT    1225   1225       R -> H (in EB-PA; mild form;
FT                                dbSNP:rs121912468).
FT                                {ECO:0000269|PubMed:11328943}.
FT                                /FTId=VAR_011301.
FT   VARIANT    1281   1281       R -> W (in EB-PA; mild form; abolishes
FT                                interaction with PLEC and reduces
FT                                interaction with COL17A1;
FT                                dbSNP:rs121912467).
FT                                {ECO:0000269|PubMed:10873890,
FT                                ECO:0000269|PubMed:12482924,
FT                                ECO:0000269|PubMed:9792864}.
FT                                /FTId=VAR_004011.
FT   VARIANT    1764   1764       T -> S (in dbSNP:rs1051486).
FT                                {ECO:0000269|PubMed:9166594,
FT                                ECO:0000269|PubMed:9194858}.
FT                                /FTId=VAR_055971.
FT   VARIANT    1779   1779       L -> P (in dbSNP:rs871443).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:2311577,
FT                                ECO:0000269|PubMed:2311578,
FT                                ECO:0000269|PubMed:9166594,
FT                                ECO:0000269|PubMed:9194858,
FT                                ECO:0000269|PubMed:9207246}.
FT                                /FTId=VAR_027804.
FT   CONFLICT     27     27       Missing (in Ref. 5; CAB61345).
FT                                {ECO:0000305}.
FT   CONFLICT     43     43       R -> Y (in Ref. 11; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     46     46       K -> P (in Ref. 11; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    621    704       IHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDEL
FT                                KRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHK
FT                                KK -> STRASARTYAPACSARRGAPARRRGARVRNATSRS
FT                                RWWTSLREARRWWCAAPSGTRMTTAPTATPWKVTAPLGPTA
FT                                LSWCTRRR (in Ref. 5; CAB61345).
FT                                {ECO:0000305}.
FT   CONFLICT    802    804       GFA -> WLC (in Ref. 8; AAB65422).
FT                                {ECO:0000305}.
FT   CONFLICT   1414   1429       HGPPDDGGAGGKGGSL -> TAPRTTAARAGRAAAV (in
FT                                Ref. 3; CAA37656). {ECO:0000305}.
FT   CONFLICT   1755   1755       P -> L (in Ref. 10; AAI18917).
FT                                {ECO:0000305}.
FT   CONFLICT   1777   1777       Missing (in Ref. 5; CAB61345).
FT                                {ECO:0000305}.
FT   STRAND      990    995       {ECO:0000244|PDB:3FSO}.
FT   STRAND      997   1002       {ECO:0000244|PDB:3FSO}.
FT   HELIX      1003   1005       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1006   1016       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1022   1033       {ECO:0000244|PDB:3FSO}.
FT   TURN       1035   1037       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1043   1048       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1054   1061       {ECO:0000244|PDB:3FSO}.
FT   TURN       1070   1073       {ECO:0000244|PDB:3FQ4}.
FT   STRAND     1076   1087       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1096   1103       {ECO:0000244|PDB:3FSO}.
FT   STRAND     1131   1137       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1139   1141       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1143   1148       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1156   1163       {ECO:0000244|PDB:3F7Q}.
FT   HELIX      1168   1170       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1172   1183       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1191   1200       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1203   1207       {ECO:0000244|PDB:3F7P}.
FT   STRAND     1211   1214       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1227   1230       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1232   1234       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1236   1239       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1252   1260       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1262   1264       {ECO:0000244|PDB:3F7R}.
FT   STRAND     1266   1268       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1271   1275       {ECO:0000244|PDB:1QG3}.
FT   STRAND     1282   1286       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1294   1302       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1310   1314       {ECO:0000244|PDB:3F7Q}.
FT   HELIX      1316   1318       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1334   1336       {ECO:0000244|PDB:3F7Q}.
FT   STRAND     1344   1348       {ECO:0000244|PDB:3F7P}.
FT   STRAND     1522   1524       {ECO:0000244|PDB:2YRZ}.
FT   STRAND     1535   1538       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1544   1547       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1557   1566       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1573   1577       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1584   1587       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1595   1604       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1612   1617       {ECO:0000244|PDB:4WTW}.
FT   STRAND     1648   1653       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1656   1662       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1671   1680       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1683   1685       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1688   1694       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1697   1703       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1712   1722       {ECO:0000244|PDB:4WTX}.
FT   STRAND     1724   1732       {ECO:0000244|PDB:4WTX}.
SQ   SEQUENCE   1822 AA;  202167 MW;  09710FFBBD719469 CRC64;
     MAGPRPSPWA RLLLAALISV SLSGTLANRC KKAPVKSCTE CVRVDKDCAY CTDEMFRDRR
     CNTQAELLAA GCQRESIVVM ESSFQITEET QIDTTLRRSQ MSPQGLRVRL RPGEERHFEL
     EVFEPLESPV DLYILMDFSN SMSDDLDNLK KMGQNLARVL SQLTSDYTIG FGKFVDKVSV
     PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVDEFRNKL QGERISGNLD APEGGFDAIL
     QTAVCTRDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MSRNDERCHL DTTGTYTQYR
     TQDYPSVPTL VRLLAKHNII PIFAVTNYSY SYYEKLHTYF PVSSLGVLQE DSSNIVELLE
     EAFNRIRSNL DIRALDSPRG LRTEVTSKMF QKTRTGSFHI RRGEVGIYQV QLRALEHVDG
     THVCQLPEDQ KGNIHLKPSF SDGLKMDAGI ICDVCTCELQ KEVRSARCSF NGDFVCGQCV
     CSEGWSGQTC NCSTGSLSDI QPCLREGEDK PCSGRGECQC GHCVCYGEGR YEGQFCEYDN
     FQCPRTSGFL CNDRGRCSMG QCVCEPGWTG PSCDCPLSNA TCIDSNGGIC NGRGHCECGR
     CHCHQQSLYT DTICEINYSA IHPGLCEDLR SCVQCQAWGT GEKKGRTCEE CNFKVKMVDE
     LKRAEEVVVR CSFRDEDDDC TYSYTMEGDG APGPNSTVLV HKKKDCPPGS FWWLIPLLLL
     LLPLLALLLL LCWKYCACCK ACLALLPCCN RGHMVGFKED HYMLRENLMA SDHLDTPMLR
     SGNLKGRDVV RWKVTNNMQR PGFATHAASI NPTELVPYGL SLRLARLCTE NLLKPDTREC
     AQLRQEVEEN LNEVYRQISG VHKLQQTKFR QQPNAGKKQD HTIVDTVLMA PRSAKPALLK
     LTEKQVEQRA FHDLKVAPGY YTLTADQDAR GMVEFQEGVE LVDVRVPLFI RPEDDDEKQL
     LVEAIDVPAG TATLGRRLVN ITIIKEQARD VVSFEQPEFS VSRGDQVARI PVIRRVLDGG
     KSQVSYRTQD GTAQGNRDYI PVEGELLFQP GEAWKELQVK LLELQEVDSL LRGRQVRRFH
     VQLSNPKFGA HLGQPHSTTI IIRDPDELDR SFTSQMLSSQ PPPHGDLGAP QNPNAKAAGS
     RKIHFNWLPP SGKPMGYRVK YWIQGDSESE AHLLDSKVPS VELTNLYPYC DYEMKVCAYG
     AQGEGPYSSL VSCRTHQEVP SEPGRLAFNV VSSTVTQLSW AEPAETNGEI TAYEVCYGLV
     NDDNRPIGPM KKVLVDNPKN RMLLIENLRE SQPYRYTVKA RNGAGWGPER EAIINLATQP
     KRPMSIPIIP DIPIVDAQSG EDYDSFLMYS DDVLRSPSGS QRPSVSDDTG CGWKFEPLLG
     EELDLRRVTW RLPPELIPRL SASSGRSSDA EAPHGPPDDG GAGGKGGSLP RSATPGPPGE
     HLVNGRMDFA FPGSTNSLHR MTTTSAAAYG THLSPHVPHR VLSTSSTLTR DYNSLTRSEH
     SHSTTLPRDY STLTSVSSHD SRLTAGVPDT PTRLVFSALG PTSLRVSWQE PRCERPLQGY
     SVEYQLLNGG ELHRLNIPNP AQTSVVVEDL LPNHSYVFRV RAQSQEGWGR EREGVITIES
     QVHPQSPLCP LPGSAFTLST PSAPGPLVFT ALSPDSLQLS WERPRRPNGD IVGYLVTCEM
     AQGGGPATAF RVDGDSPESR LTVPGLSENV PYKFKVQART TEGFGPEREG IITIESQDGG
     PFPQLGSRAG LFQHPLQSEY SSITTTHTSA TEPFLVDGLT LGAQHLEAGG SLTRHVTQEF
     VSRTLTTSGT LSTHMDQQFF QT
//
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