LAMB3_HUMAN
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 03-AUG-2022, entry version 207.
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 H-JEB 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 GABEB 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 GABEB 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, Herlitz type (H-JEB)
CC [MIM:226700]: An infantile and lethal form of junctional epidermolysis
CC bullosa, a group of blistering skin diseases characterized by tissue
CC separation which occurs within the dermo-epidermal basement In the
CC Herlitz type, death occurs usually within the first six months of life.
CC Occasionally, children survive to teens. It is marked by bullous
CC lesions at birth and extensive denudation of skin and mucous membranes
CC that may be hemorrhagic. {ECO:0000269|PubMed:7550237}. Note=The disease
CC is caused by variants 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, associated
CC with hair and tooth 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; 142.
DR ComplexPortal; CPX-1774; Laminin-332 complex variant A.
DR ComplexPortal; CPX-3165; Laminin-332 complex variant B.
DR IntAct; Q13751; 25.
DR MINT; Q13751; -.
DR STRING; 9606.ENSP00000375778; -.
DR ChEMBL; CHEMBL2364187; -.
DR GlyGen; Q13751; 4 sites, 1 O-linked glycan (1 site).
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; Q13751; -.
DR PeptideAtlas; Q13751; -.
DR PRIDE; Q13751; -.
DR ProteomicsDB; 59674; -.
DR Antibodypedia; 1958; 391 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 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; WKVYQYL; -.
DR OrthoDB; 88170at2759; -.
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; 14 hits in 1078 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 134 other tissues.
DR ExpressionAtlas; Q13751; baseline and differential.
DR Genevisible; Q13751; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 6.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00136; LamNT; 1.
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.
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 GABEB; 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 GABEB; 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 GABEB; 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 H-JEB; 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
