ID LAMB3_HUMAN Reviewed; 1172 AA. AC Q13751; D3DT88; O14947; Q14733; Q9UJK4; Q9UJL1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=Laminin subunit beta-3; DE AltName: Full=Epiligrin subunit bata; DE AltName: Full=Kalinin B1 chain; DE AltName: Full=Kalinin subunit beta; DE AltName: Full=Laminin B1k chain; DE AltName: Full=Laminin-5 subunit beta; DE AltName: Full=Nicein subunit beta; DE Flags: Precursor; GN Name=LAMB3; Synonyms=LAMNB1; 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], AND PROTEIN SEQUENCE OF 172-190. RX PubMed=7512558; DOI=10.1016/s0021-9258(19)78093-4; RA Gerecke D.R., Wagman D.W., Champliaud M.-F., Burgeson R.E.; RT "The complete primary structure for a novel laminin chain, the laminin B1k RT chain."; RL J. Biol. Chem. 269:11073-11080(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7774918; DOI=10.1016/0888-7543(95)80125-6; RA Pulkkinen L., Gerecke D.R., Christiano A.M., Wagman D.W., Burgeson R.E., RA Uitto J.; RT "Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate RT gene in junctional epidermolysis bullosa."; RL Genomics 25:192-198(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Epidermis; RX PubMed=8530036; DOI=10.1006/geno.1995.1141; RA Morishima Y., Ariyama T., Yamanishi K., Abe T., Ueda E., Yasuno H., RA Inazawa J.; RT "Chromosomal loci of 50 human keratinocyte cDNAs assigned by fluorescence RT in situ hybridization."; RL Genomics 28:273-279(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11296269; DOI=10.1073/pnas.091484998; RA Robbins P.B., Lin Q., Goodnough J.B., Tian H., Chen X., Khavari P.A.; RT "In vivo restoration of laminin 5 beta 3 expression and function in RT junctional epidermolysis bullosa."; RL Proc. Natl. Acad. Sci. U.S.A. 98:5193-5198(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-852. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 [8] RP INTERACTION WITH ECM1. RX PubMed=19275936; DOI=10.1016/j.matbio.2009.02.003; RA Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., RA Sasaki T., Oyama N., Merregaert J.; RT "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through RT its serum albumin subdomain-like 2 domain."; RL Matrix Biol. 28:160-169(2009). RN [9] 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 [10] RP INVOLVEMENT IN AI1A. RX PubMed=23958762; DOI=10.1177/0022034513502054; RA Kim J.W., Seymen F., Lee K.E., Ko J., Yildirim M., Tuna E.B., Gencay K., RA Shin T.J., Kyun H.K., Simmer J.P., Hu J.C.; RT "LAMB3 mutations causing autosomal-dominant amelogenesis imperfecta."; RL J. Dent. Res. 92:899-904(2013). RN [11] RP INVOLVEMENT IN AI1A. RX PubMed=23632796; DOI=10.1038/ejhg.2013.76; RA Poulter J.A., El-Sayed W., Shore R.C., Kirkham J., Inglehearn C.F., RA Mighell A.J.; RT "Whole-exome sequencing, without prior linkage, identifies a mutation in RT LAMB3 as a cause of dominant hypoplastic amelogenesis imperfecta."; RL Eur. J. Hum. Genet. 22:132-135(2014). RN [12] RP VARIANT JEB1B LEU-679. RX PubMed=7550237; DOI=10.1002/humu.1380060115; RA Pulkkinen L., McGrath J.A., Christiano A.M., Uitto J.; RT "Detection of sequence variants in the gene encoding the beta 3 chain of RT laminin 5 (LAMB3)."; RL Hum. Mutat. 6:77-84(1995). RN [13] RP VARIANT JEB1A LYS-210. RX PubMed=9767254; DOI=10.1046/j.1365-2133.1998.02377.x; RA Mellerio J.E., Eady R.A.J., Atherton D.J., Lake B.D., McGrath J.A.; RT "E210K mutation in the gene encoding the beta3 chain of laminin-5 (LAMB3) RT is predictive of a phenotype of generalized atrophic benign epidermolysis RT bullosa."; RL Br. J. Dermatol. 139:325-331(1998). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] CYS-450. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [15] RP VARIANTS JEB1A ALA-199; GLN-207 AND LYS-210. RX PubMed=17476356; DOI=10.1172/jci30465; RA Pasmooij A.M.G., Pas H.H., Bolling M.C., Jonkman M.F.; RT "Revertant mosaicism in junctional epidermolysis bullosa due to multiple RT correcting second-site mutations in LAMB3."; RL J. Clin. Invest. 117:1240-1248(2007). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is CC thought to mediate the attachment, migration and organization of cells CC into tissues during embryonic development by interacting with other CC extracellular matrix components. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound to CC each other by disulfide bonds into a cross-shaped molecule comprising CC one long and three short arms with globules at each end. Beta-3 is a CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). CC Interacts with ECM1. {ECO:0000269|PubMed:19275936}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component). CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with CC other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domain VI is globular. CC -!- DISEASE: Epidermolysis bullosa, junctional 1B, severe (JEB1B) CC [MIM:226700]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC Junctional epidermolysis bullosa is characterized by blistering that CC occurs at the level of the lamina lucida in the skin basement membrane. CC JEB1B is an autosomal recessive, severe form characterized by bullous CC lesions appearing at birth, and extensive denudation of skin and mucous CC membranes that may be hemorrhagic. Death occurs usually within the CC first six months of life. Occasionally, children survive to teens. CC {ECO:0000269|PubMed:7550237}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa, junctional 1A, intermediate (JEB1A) CC [MIM:226650]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC Junctional epidermolysis bullosa is characterized by blistering that CC occurs at the level of the lamina lucida in the skin basement membrane. CC JEB1A is an autosomal recessive, non-lethal, adult form characterized CC by life-long blistering of the skin, associated with hair and tooth CC abnormalities. {ECO:0000269|PubMed:17476356, CC ECO:0000269|PubMed:9767254}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Amelogenesis imperfecta 1A (AI1A) [MIM:104530]: A form of CC amelogenesis imperfecta, a disorder characterized by defective enamel CC formation. The enamel may be hypoplastic, hypomineralized or both, and CC affected teeth may be discoloured, sensitive or prone to CC disintegration. {ECO:0000269|PubMed:23632796, CC ECO:0000269|PubMed:23958762}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; L25541; AAA61834.1; -; mRNA. DR EMBL; U17760; AAC51352.1; -; Genomic_DNA. DR EMBL; U17745; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17746; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17747; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17748; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17749; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17750; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17751; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17752; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17753; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17754; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17755; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17756; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17757; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17758; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; U17759; AAC51352.1; JOINED; Genomic_DNA. DR EMBL; D37766; BAA22263.1; -; mRNA. DR EMBL; AY035783; AAK61364.1; -; mRNA. DR EMBL; AL023754; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93448.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93449.1; -; Genomic_DNA. DR EMBL; BC075838; AAH75838.1; -; mRNA. DR CCDS; CCDS1487.1; -. DR PIR; A53612; A53612. DR RefSeq; NP_000219.2; NM_000228.2. DR RefSeq; NP_001017402.1; NM_001017402.1. DR RefSeq; NP_001121113.1; NM_001127641.1. DR RefSeq; XP_005273181.1; XM_005273124.4. DR AlphaFoldDB; Q13751; -. DR SMR; Q13751; -. DR BioGRID; 110108; 151. DR ComplexPortal; CPX-1774; Laminin-332 complex variant A. DR ComplexPortal; CPX-3165; Laminin-332 complex variant B. DR IntAct; Q13751; 28. DR MINT; Q13751; -. DR STRING; 9606.ENSP00000375778; -. DR ChEMBL; CHEMBL2364187; -. DR GlyCosmos; Q13751; 3 sites, No reported glycans. DR GlyGen; Q13751; 6 sites, 2 O-linked glycans (3 sites). DR iPTMnet; Q13751; -. DR MetOSite; Q13751; -. DR PhosphoSitePlus; Q13751; -. DR SwissPalm; Q13751; -. DR BioMuta; LAMB3; -. DR DMDM; 2497600; -. DR EPD; Q13751; -. DR jPOST; Q13751; -. DR MassIVE; Q13751; -. DR MaxQB; Q13751; -. DR PaxDb; 9606-ENSP00000375778; -. DR PeptideAtlas; Q13751; -. DR ProteomicsDB; 59674; -. DR Pumba; Q13751; -. DR Antibodypedia; 1958; 423 antibodies from 28 providers. DR DNASU; 3914; -. DR Ensembl; ENST00000356082.9; ENSP00000348384.3; ENSG00000196878.15. DR Ensembl; ENST00000367030.7; ENSP00000355997.3; ENSG00000196878.15. DR Ensembl; ENST00000391911.5; ENSP00000375778.1; ENSG00000196878.15. DR GeneID; 3914; -. DR KEGG; hsa:3914; -. DR MANE-Select; ENST00000356082.9; ENSP00000348384.3; NM_000228.3; NP_000219.2. DR UCSC; uc001hhg.4; human. DR AGR; HGNC:6490; -. DR CTD; 3914; -. DR DisGeNET; 3914; -. DR GeneCards; LAMB3; -. DR GeneReviews; LAMB3; -. DR HGNC; HGNC:6490; LAMB3. DR HPA; ENSG00000196878; Tissue enhanced (stomach, urinary bladder). DR MalaCards; LAMB3; -. DR MIM; 104530; phenotype. DR MIM; 150310; gene. DR MIM; 226650; phenotype. DR MIM; 226700; phenotype. DR neXtProt; NX_Q13751; -. DR OpenTargets; ENSG00000196878; -. DR Orphanet; 100031; Hypoplastic amelogenesis imperfecta. DR Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa. DR Orphanet; 79404; Severe generalized junctional epidermolysis bullosa. DR PharmGKB; PA30278; -. DR VEuPathDB; HostDB:ENSG00000196878; -. DR eggNOG; KOG0994; Eukaryota. DR GeneTree; ENSGT00940000160731; -. DR HOGENOM; CLU_001560_0_0_1; -. DR InParanoid; Q13751; -. DR OMA; RCLCLPH; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; Q13751; -. DR TreeFam; TF352481; -. DR PathwayCommons; Q13751; -. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-446107; Type I hemidesmosome assembly. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR SignaLink; Q13751; -. DR SIGNOR; Q13751; -. DR BioGRID-ORCS; 3914; 18 hits in 1158 CRISPR screens. DR ChiTaRS; LAMB3; human. DR GeneWiki; Laminin,_beta_3; -. DR GenomeRNAi; 3914; -. DR Pharos; Q13751; Tbio. DR PRO; PR:Q13751; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q13751; Protein. DR Bgee; ENSG00000196878; Expressed in cartilage tissue and 135 other cell types or tissues. DR ExpressionAtlas; Q13751; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0008544; P:epidermis development; TAS:ProtInc. DR CDD; cd22303; cc_LAMB3_C; 1. DR CDD; cd00055; EGF_Lam; 6. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 4. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR PANTHER; PTHR10574:SF268; LAMININ SUBUNIT BETA-3; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00053; Laminin_EGF; 6. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00180; EGF_Lam; 6. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF57196; EGF/Laminin; 6. DR PROSITE; PS00022; EGF_1; 5. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS01248; EGF_LAM_1; 5. DR PROSITE; PS50027; EGF_LAM_2; 6. DR PROSITE; PS51117; LAMININ_NTER; 1. DR Genevisible; Q13751; HS. PE 1: Evidence at protein level; KW Amelogenesis imperfecta; Basement membrane; Cell adhesion; Coiled coil; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Epidermolysis bullosa; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..1172 FT /note="Laminin subunit beta-3" FT /id="PRO_0000017071" FT DOMAIN 22..249 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 250..315 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 316..378 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 379..430 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 431..480 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 481..533 FT /note="Laminin EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 534..580 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT REGION 579..785 FT /note="Domain II" FT REGION 786..816 FT /note="Domain alpha" FT REGION 817..1170 FT /note="Domain I" FT COILED 723..757 FT /evidence="ECO:0000255" FT COILED 831..884 FT /evidence="ECO:0000255" FT COILED 948..1133 FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 604 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 810 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 250..259 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 252..279 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 281..290 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 293..313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 316..325 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 318..343 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 346..355 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 358..376 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 379..392 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 381..399 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 401..410 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 413..428 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 431..444 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 433..451 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 453..462 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 465..478 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 481..493 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 483..500 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 502..511 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 519..531 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 534..546 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 536..553 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 555..564 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 567..578 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 581 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 584 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1171 FT /note="Interchain" FT /evidence="ECO:0000305" FT VARIANT 181 FT /note="N -> D (in dbSNP:rs2235542)" FT /id="VAR_037309" FT VARIANT 199 FT /note="G -> A (in JEB1A; somatic second-site mutation; FT dbSNP:rs121912486)" FT /evidence="ECO:0000269|PubMed:17476356" FT /id="VAR_037310" FT VARIANT 207 FT /note="K -> Q (in JEB1A; somatic second-site mutation; FT dbSNP:rs121912487)" FT /evidence="ECO:0000269|PubMed:17476356" FT /id="VAR_037311" FT VARIANT 210 FT /note="E -> K (in JEB1A; dbSNP:rs121912482)" FT /evidence="ECO:0000269|PubMed:17476356, FT ECO:0000269|PubMed:9767254" FT /id="VAR_004170" FT VARIANT 292 FT /note="R -> L (in dbSNP:rs12091253)" FT /id="VAR_037312" FT VARIANT 438 FT /note="S -> T (in dbSNP:rs2229468)" FT /id="VAR_034060" FT VARIANT 450 FT /note="R -> C (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs200895463)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035820" FT VARIANT 527 FT /note="V -> M (in dbSNP:rs2076349)" FT /id="VAR_037313" FT VARIANT 679 FT /note="P -> L (in JEB1B; dbSNP:rs201223111)" FT /evidence="ECO:0000269|PubMed:7550237" FT /id="VAR_004171" FT VARIANT 690 FT /note="N -> S (in dbSNP:rs2229466)" FT /id="VAR_034061" FT VARIANT 852 FT /note="M -> L (in dbSNP:rs12748250)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_034062" FT VARIANT 926 FT /note="A -> D (in dbSNP:rs2076222)" FT /id="VAR_037314" FT VARIANT 988 FT /note="R -> W (in dbSNP:rs2229467)" FT /id="VAR_034063" FT CONFLICT 124 FT /note="Q -> R (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 269 FT /note="Missing (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="P -> A (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 426..427 FT /note="QG -> RR (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 440..441 FT /note="RD -> E (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 489..500 FT /note="LSPQCNQFTGQC -> PQPTVQPVHRAV (in Ref. 3; BAA22263)" FT /evidence="ECO:0000305" FT CONFLICT 603 FT /note="R -> P (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" FT CONFLICT 815 FT /note="G -> A (in Ref. 1; AAA61834)" FT /evidence="ECO:0000305" SQ SEQUENCE 1172 AA; 129572 MW; 61BC1A60BBD4FA05 CRC64; MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT KPETYCTQYG EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND VNPVSLQLDL DRRFQLQEVM MEFQGPMPAG MLIERSSDFG KTWRVYQYLA ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP NARLNGGKVQ LNLMDLVSGI PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA VSQLRLQGSC FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT EGKNCERCQL HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV CKEHVQGERC DLCKPGFTGL TYANPQGCHR CDCNILGSRR DMPCDEESGR CLCLPNVVGP KCDQCAPYHW KLASGQGCEP CACDPHNSLS PQCNQFTGQC PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG TEGPGCDKAS GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ VASAILSLRR TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR EQFEKISSAD PSGAFRMLST AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL TPTFNKLCGN SRQMACTPIS CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR GFNAQLQRTR QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS QTKQDIARAR RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT MQGTSRSLRL IQDRVAEVQQ VLRPAEKLVT SMTKQLGDFW TRMEELRHQA RQQGAEAVQA QQLAEGASEQ ALSAQEGFER IKQKYAELKD RLGQSSMLGE QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI MLRSADLTGL EKRVEQIRDH INGRVLYYAT CK //