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Laminin subunit beta-3 (Epiligrin subunit bata) (Kalinin B1 chain) (Kalinin subunit beta) (Laminin B1k chain) (Laminin-5 subunit beta) (Nicein subunit beta)

 LAMB3_HUMAN             Reviewed;        1172 AA.
Q13751; D3DT88; O14947; Q14733; Q9UJK4; Q9UJL1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 182.
RecName: Full=Laminin subunit beta-3;
AltName: Full=Epiligrin subunit bata;
AltName: Full=Kalinin B1 chain;
AltName: Full=Kalinin subunit beta;
AltName: Full=Laminin B1k chain;
AltName: Full=Laminin-5 subunit beta;
AltName: Full=Nicein subunit beta;
Flags: Precursor;
Name=LAMB3; Synonyms=LAMNB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 172-190.
PubMed=7512558;
Gerecke D.R., Wagman D.W., Champliaud M.-F., Burgeson R.E.;
"The complete primary structure for a novel laminin chain, the laminin
B1k chain.";
J. Biol. Chem. 269:11073-11080(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7774918; DOI=10.1016/0888-7543(95)80125-6;
Pulkkinen L., Gerecke D.R., Christiano A.M., Wagman D.W.,
Burgeson R.E., Uitto J.;
"Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a
candidate gene in junctional epidermolysis bullosa.";
Genomics 25:192-198(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epidermis;
PubMed=8530036; DOI=10.1006/geno.1995.1141;
Morishima Y., Ariyama T., Yamanishi K., Abe T., Ueda E., Yasuno H.,
Inazawa J.;
"Chromosomal loci of 50 human keratinocyte cDNAs assigned by
fluorescence in situ hybridization.";
Genomics 28:273-279(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11296269; DOI=10.1073/pnas.091484998;
Robbins P.B., Lin Q., Goodnough J.B., Tian H., Chen X., Khavari P.A.;
"In vivo restoration of laminin 5 beta 3 expression and function in
junctional epidermolysis bullosa.";
Proc. Natl. Acad. Sci. U.S.A. 98:5193-5198(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-852.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH ECM1.
PubMed=19275936; DOI=10.1016/j.matbio.2009.02.003;
Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A.,
Geentjens K., Sasaki T., Oyama N., Merregaert J.;
"ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332
through its serum albumin subdomain-like 2 domain.";
Matrix Biol. 28:160-169(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INVOLVEMENT IN AI1A.
PubMed=23958762; DOI=10.1177/0022034513502054;
Kim J.W., Seymen F., Lee K.E., Ko J., Yildirim M., Tuna E.B.,
Gencay K., Shin T.J., Kyun H.K., Simmer J.P., Hu J.C.;
"LAMB3 mutations causing autosomal-dominant amelogenesis imperfecta.";
J. Dent. Res. 92:899-904(2013).
[11]
INVOLVEMENT IN AI1A.
PubMed=23632796; DOI=10.1038/ejhg.2013.76;
Poulter J.A., El-Sayed W., Shore R.C., Kirkham J., Inglehearn C.F.,
Mighell A.J.;
"Whole-exome sequencing, without prior linkage, identifies a mutation
in LAMB3 as a cause of dominant hypoplastic amelogenesis imperfecta.";
Eur. J. Hum. Genet. 22:132-135(2014).
[12]
VARIANT H-JEB LEU-679.
PubMed=7550237; DOI=10.1002/humu.1380060115;
Pulkkinen L., McGrath J.A., Christiano A.M., Uitto J.;
"Detection of sequence variants in the gene encoding the beta 3 chain
of laminin 5 (LAMB3).";
Hum. Mutat. 6:77-84(1995).
[13]
VARIANT GABEB LYS-210.
PubMed=9767254; DOI=10.1046/j.1365-2133.1998.02377.x;
Mellerio J.E., Eady R.A.J., Atherton D.J., Lake B.D., McGrath J.A.;
"E210K mutation in the gene encoding the beta3 chain of laminin-5
(LAMB3) is predictive of a phenotype of generalized atrophic benign
epidermolysis bullosa.";
Br. J. Dermatol. 139:325-331(1998).
[14]
VARIANT [LARGE SCALE ANALYSIS] CYS-450.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[15]
VARIANTS GABEB ALA-199; GLN-207 AND LYS-210.
PubMed=17476356; DOI=10.1172/JCI30465;
Pasmooij A.M.G., Pas H.H., Bolling M.C., Jonkman M.F.;
"Revertant mosaicism in junctional epidermolysis bullosa due to
multiple correcting second-site mutations in LAMB3.";
J. Clin. Invest. 117:1240-1248(2007).
-!- FUNCTION: Binding to cells via a high affinity receptor, laminin
is thought to mediate the attachment, migration and organization
of cells into tissues during embryonic development by interacting
with other extracellular matrix components.
-!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
different polypeptide chains (alpha, beta, gamma), which are bound
to each other by disulfide bonds into a cross-shaped molecule
comprising one long and three short arms with globules at each
end. Beta-3 is a subunit of laminin-5 (laminin-332 or
epiligrin/kalinin/nicein). Interacts with ECM1.
{ECO:0000269|PubMed:19275936}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- TISSUE SPECIFICITY: Found in the basement membranes (major
component).
-!- DOMAIN: The alpha-helical domains I and II are thought to interact
with other laminin chains to form a coiled coil structure.
-!- DOMAIN: Domain VI is globular.
-!- DISEASE: Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
[MIM:226700]: An infantile and lethal form of junctional
epidermolysis bullosa, a group of blistering skin diseases
characterized by tissue separation which occurs within the dermo-
epidermal basement In the Herlitz type, death occurs usually
within the first six months of life. Occasionally, children
survive to teens. It is marked by bullous lesions at birth and
extensive denudation of skin and mucous membranes that may be
hemorrhagic. {ECO:0000269|PubMed:7550237}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB)
[MIM:226650]: A non-lethal, adult form of junctional epidermolysis
bullosa characterized by life-long blistering of the skin,
associated with hair and tooth abnormalities.
{ECO:0000269|PubMed:17476356, ECO:0000269|PubMed:9767254}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Amelogenesis imperfecta 1A (AI1A) [MIM:104530]: A form of
amelogenesis imperfecta, a disorder characterized by defective
enamel formation. The enamel may be hypoplastic, hypomineralized
or both, and affected teeth may be discoloured, sensitive or prone
to disintegration. {ECO:0000269|PubMed:23632796,
ECO:0000269|PubMed:23958762}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; L25541; AAA61834.1; -; mRNA.
EMBL; U17760; AAC51352.1; -; Genomic_DNA.
EMBL; U17745; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17746; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17747; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17748; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17749; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17750; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17751; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17752; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17753; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17754; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17755; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17756; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17757; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17758; AAC51352.1; JOINED; Genomic_DNA.
EMBL; U17759; AAC51352.1; JOINED; Genomic_DNA.
EMBL; D37766; BAA22263.1; -; mRNA.
EMBL; AY035783; AAK61364.1; -; mRNA.
EMBL; AL023754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93448.1; -; Genomic_DNA.
EMBL; CH471100; EAW93449.1; -; Genomic_DNA.
EMBL; BC075838; AAH75838.1; -; mRNA.
CCDS; CCDS1487.1; -.
PIR; A53612; A53612.
RefSeq; NP_000219.2; NM_000228.2.
RefSeq; NP_001017402.1; NM_001017402.1.
RefSeq; NP_001121113.1; NM_001127641.1.
RefSeq; XP_005273181.1; XM_005273124.4.
UniGene; Hs.497636; -.
ProteinModelPortal; Q13751; -.
SMR; Q13751; -.
BioGrid; 110108; 22.
ComplexPortal; CPX-1774; Laminin-332 complex variant A.
ComplexPortal; CPX-3165; Laminin-332 complex variant B.
IntAct; Q13751; 21.
MINT; Q13751; -.
STRING; 9606.ENSP00000348384; -.
ChEMBL; CHEMBL2364187; -.
iPTMnet; Q13751; -.
PhosphoSitePlus; Q13751; -.
SwissPalm; Q13751; -.
BioMuta; LAMB3; -.
DMDM; 2497600; -.
EPD; Q13751; -.
MaxQB; Q13751; -.
PaxDb; Q13751; -.
PeptideAtlas; Q13751; -.
PRIDE; Q13751; -.
ProteomicsDB; 59674; -.
DNASU; 3914; -.
Ensembl; ENST00000356082; ENSP00000348384; ENSG00000196878.
Ensembl; ENST00000367030; ENSP00000355997; ENSG00000196878.
Ensembl; ENST00000391911; ENSP00000375778; ENSG00000196878.
GeneID; 3914; -.
KEGG; hsa:3914; -.
UCSC; uc001hhg.4; human.
CTD; 3914; -.
DisGeNET; 3914; -.
EuPathDB; HostDB:ENSG00000196878.12; -.
GeneCards; LAMB3; -.
GeneReviews; LAMB3; -.
HGNC; HGNC:6490; LAMB3.
HPA; CAB078183; -.
HPA; HPA008069; -.
MalaCards; LAMB3; -.
MIM; 104530; phenotype.
MIM; 150310; gene.
MIM; 226650; phenotype.
MIM; 226700; phenotype.
neXtProt; NX_Q13751; -.
OpenTargets; ENSG00000196878; -.
Orphanet; 79402; Generalized junctional epidermolysis bullosa, non-Herlitz type.
Orphanet; 100031; Hypoplastic amelogenesis imperfecta.
Orphanet; 79404; Junctional epidermolysis bullosa, Herlitz type.
PharmGKB; PA30278; -.
eggNOG; KOG0994; Eukaryota.
eggNOG; ENOG410XPEG; LUCA.
GeneTree; ENSGT00780000121851; -.
HOGENOM; HOG000113279; -.
HOVERGEN; HBG052302; -.
InParanoid; Q13751; -.
KO; K06244; -.
OMA; WWQSQND; -.
OrthoDB; EOG091G019I; -.
PhylomeDB; Q13751; -.
TreeFam; TF352481; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-2214320; Anchoring fibril formation.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
SIGNOR; Q13751; -.
ChiTaRS; LAMB3; human.
GeneWiki; Laminin,_beta_3; -.
GenomeRNAi; 3914; -.
PMAP-CutDB; Q13751; -.
PRO; PR:Q13751; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000196878; -.
CleanEx; HS_LAMB3; -.
ExpressionAtlas; Q13751; baseline and differential.
Genevisible; Q13751; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
Gene3D; 2.60.120.1490; -; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR008211; Laminin_N.
InterPro; IPR038684; Laminin_N_sf.
Pfam; PF00053; Laminin_EGF; 6.
Pfam; PF00055; Laminin_N; 1.
SMART; SM00180; EGF_Lam; 6.
SMART; SM00136; LamNT; 1.
PROSITE; PS00022; EGF_1; 5.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01248; EGF_LAM_1; 5.
PROSITE; PS50027; EGF_LAM_2; 6.
PROSITE; PS51117; LAMININ_NTER; 1.
1: Evidence at protein level;
Amelogenesis imperfecta; Basement membrane; Cell adhesion;
Coiled coil; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Epidermolysis bullosa;
Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 1172 Laminin subunit beta-3.
/FTId=PRO_0000017071.
DOMAIN 22 249 Laminin N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00466}.
DOMAIN 250 315 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 316 378 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 379 430 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 431 480 Laminin EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 481 533 Laminin EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 534 580 Laminin EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
REGION 579 785 Domain II.
REGION 786 816 Domain alpha.
REGION 817 1170 Domain I.
COILED 723 757 {ECO:0000255}.
COILED 831 884 {ECO:0000255}.
COILED 948 1133 {ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 810 810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 250 259 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 252 279 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 281 290 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 293 313 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 316 325 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 318 343 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 346 355 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 358 376 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 379 392 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 381 399 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 401 410 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 413 428 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 431 444 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 433 451 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 453 462 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 465 478 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 481 493 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 483 500 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 502 511 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 519 531 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 534 546 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 536 553 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 555 564 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 567 578 {ECO:0000255|PROSITE-ProRule:PRU00460}.
DISULFID 581 581 Interchain. {ECO:0000305}.
DISULFID 584 584 Interchain. {ECO:0000305}.
DISULFID 1171 1171 Interchain. {ECO:0000305}.
VARIANT 181 181 N -> D (in dbSNP:rs2235542).
/FTId=VAR_037309.
VARIANT 199 199 G -> A (in GABEB; somatic second-site
mutation; dbSNP:rs121912486).
{ECO:0000269|PubMed:17476356}.
/FTId=VAR_037310.
VARIANT 207 207 K -> Q (in GABEB; somatic second-site
mutation; dbSNP:rs121912487).
{ECO:0000269|PubMed:17476356}.
/FTId=VAR_037311.
VARIANT 210 210 E -> K (in GABEB; dbSNP:rs121912482).
{ECO:0000269|PubMed:17476356,
ECO:0000269|PubMed:9767254}.
/FTId=VAR_004170.
VARIANT 292 292 R -> L (in dbSNP:rs12091253).
/FTId=VAR_037312.
VARIANT 438 438 S -> T (in dbSNP:rs2229468).
/FTId=VAR_034060.
VARIANT 450 450 R -> C (in a colorectal cancer sample;
somatic mutation; dbSNP:rs200895463).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035820.
VARIANT 527 527 V -> M (in dbSNP:rs2076349).
/FTId=VAR_037313.
VARIANT 679 679 P -> L (in H-JEB; dbSNP:rs201223111).
{ECO:0000269|PubMed:7550237}.
/FTId=VAR_004171.
VARIANT 690 690 N -> S (in dbSNP:rs2229466).
/FTId=VAR_034061.
VARIANT 852 852 M -> L (in dbSNP:rs12748250).
{ECO:0000269|Ref.6}.
/FTId=VAR_034062.
VARIANT 926 926 A -> D (in dbSNP:rs2076222).
/FTId=VAR_037314.
VARIANT 988 988 R -> W (in dbSNP:rs2229467).
/FTId=VAR_034063.
CONFLICT 124 124 Q -> R (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 269 269 Missing (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 388 388 P -> A (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 426 427 QG -> RR (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 440 441 RD -> E (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 489 500 LSPQCNQFTGQC -> PQPTVQPVHRAV (in Ref. 3;
BAA22263). {ECO:0000305}.
CONFLICT 603 603 R -> P (in Ref. 1; AAA61834).
{ECO:0000305}.
CONFLICT 815 815 G -> A (in Ref. 1; AAA61834).
{ECO:0000305}.
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


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