BCAM_HUMAN
ID BCAM_HUMAN Reviewed; 628 AA.
AC P50895; A8MYF9; A9YWT5; A9YWT6; Q86VC7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Basal cell adhesion molecule;
DE AltName: Full=Auberger B antigen;
DE AltName: Full=B-CAM cell surface glycoprotein;
DE AltName: Full=F8/G253 antigen;
DE AltName: Full=Lutheran antigen;
DE AltName: Full=Lutheran blood group glycoprotein;
DE AltName: CD_antigen=CD239;
DE Flags: Precursor;
GN Name=BCAM; Synonyms=LU, MSK19;
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], PROTEIN SEQUENCE OF 32-67 AND 182-203, AND
RP VARIANT ALA-539.
RC TISSUE=Placenta;
RX PubMed=7777537; DOI=10.1073/pnas.92.12.5496;
RA Parsons S.F., Mallinson G., Holmes C.H., Houlihan J.M., Simpson K.L.,
RA Mawby W.J., Spurr N.K., Warne D., Barclay A.N., Anstee D.J.;
RT "The Lutheran blood group glycoprotein, another member of the
RT immunoglobulin superfamily, is widely expressed in human tissues and is
RT developmentally regulated in human liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5496-5500(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-77; ILE-196; LYS-204;
RP HIS-282; ILE-381; GLN-451 AND LEU-581.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-588, AND VARIANT ALA-539.
RX PubMed=7954395;
RA Campbell I.G., Foulkes W.D., Senger G., Trowsdale J., Garin-Chesa P.,
RA Rettig W.J.;
RT "Molecular cloning of the B-CAM cell surface glycoprotein of epithelial
RT cancers: a novel member of the immunoglobulin superfamily.";
RL Cancer Res. 54:5761-5765(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 492-539, AND VARIANT ALA-539.
RA Wang C., Li Q., Guo Z., Yang Y., Zhu Z.;
RT "Molecular basis of Lub(-) individual among Chinese blood donors in
RT Shanghai area.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP LU(A)/LU(B) POLYMORPHISM.
RX PubMed=9166867;
RA Parsons S.F., Mallinson G., Daniels G.L., Green C.A., Smythe J.S.,
RA Anstee D.J.;
RT "Use of domain-deletion mutants to locate Lutheran blood group antigens to
RT each of the five immunoglobulin superfamily domains of the Lutheran
RT glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the
RT Au(a)/Au(b) polymorphisms.";
RL Blood 89:4219-4225(1997).
RN [9]
RP LU(A)/LU(B) POLYMORPHISM.
RX PubMed=9192786;
RA El Nemer W., Rahuel C., Colin Y., Gane P., Cartron J.P., Le Van Kim C.;
RT "Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b)
RT blood group polymorphism.";
RL Blood 89:4608-4616(1997).
RN [10]
RP FUNCTION.
RX PubMed=9616226; DOI=10.1172/jci1204;
RA Udani M., Zen Q., Cottman M., Leonard N., Jefferson S., Daymont C.,
RA Truskey G., Telen M.J.;
RT "Basal cell adhesion molecule/lutheran protein. The receptor critical for
RT sickle cell adhesion to laminin.";
RL J. Clin. Invest. 101:2550-2558(1998).
RN [11]
RP GLYCOSYLATION AT ASN-439.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP PHOSPHORYLATION AT SER-596; SER-598 AND SER-621, AND MUTAGENESIS OF
RP SER-621.
RX PubMed=15975931; DOI=10.1074/jbc.m503293200;
RA Gauthier E., Rahuel C., Wautier M.P., El Nemer W., Gane P., Wautier J.L.,
RA Cartron J.P., Colin Y., Le Van Kim C.;
RT "Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion
RT molecule glycoprotein regulates cell adhesion to laminin alpha5.";
RL J. Biol. Chem. 280:30055-30062(2005).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439.
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., Moore R.J.,
RA 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 [14]
RP POLYMORPHISM, AND INVOLVEMENT IN THE LUTHERAN NULL PHENOTYPE.
RX PubMed=17319831; DOI=10.1111/j.1537-2995.2006.01141.x;
RA Karamatic Crew V., Mallinson G., Green C., Poole J., Uchikawa M., Tani Y.,
RA Geisen C., Oldenburg J., Daniels G.;
RT "Different inactivating mutations in the LU genes of three individuals with
RT the Lutheran-null phenotype.";
RL Transfusion 47:492-498(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-262, LAMININ-ALPHA5 BINDING
RP REGION, AND DISULFIDE BONDS.
RX PubMed=17638854; DOI=10.1182/blood-2007-06-094748;
RA Mankelow T.J., Burton N., Stefansdottir F.O., Spring F.A., Parsons S.F.,
RA Pedersen J.S., Oliveira C.L., Lammie D., Wess T., Mohandas N., Chasis J.A.,
RA Brady R.L., Anstee D.J.;
RT "The Laminin 511/521-binding site on the Lutheran blood group glycoprotein
RT is located at the flexible junction of Ig domains 2 and 3.";
RL Blood 110:3398-3406(2007).
CC -!- FUNCTION: Laminin alpha-5 receptor. May mediate intracellular
CC signaling. {ECO:0000269|PubMed:9616226}.
CC -!- INTERACTION:
CC P50895; O95198: KLHL2; NbExp=6; IntAct=EBI-10212133, EBI-746999;
CC P50895; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10212133, EBI-11959885;
CC P50895; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-10212133, EBI-11749135;
CC P50895; Q99750: MDFI; NbExp=3; IntAct=EBI-10212133, EBI-724076;
CC P50895; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10212133, EBI-22310682;
CC P50895; Q9C029: TRIM7; NbExp=3; IntAct=EBI-10212133, EBI-2813981;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Wide tissue distribution (highest in the pancreas
CC and very low in brain). Closely associated with the basal layer of
CC cells in epithelia and the endothelium of blood vessel walls.
CC -!- DEVELOPMENTAL STAGE: Is under developmental control in liver and may
CC also be regulated during differentiation in other tissues. Up-regulated
CC following malignant transformation in some cell types.
CC -!- PTM: Epinephrine-stimulated phosphorylation of Ser-621 by PKA enhances
CC adhesion to laminin. {ECO:0000269|PubMed:15975931}.
CC -!- POLYMORPHISM: BCAM is responsible for the Lutheran blood group system
CC (LU) [MIM:111200]. Lutheran is a complex blood group system consisting
CC of 19 antigens. Antigens Lu(a) and Lu(b) are defined by a polymorphism
CC at position 77: Lu(a) has His-77 and Lu(b) has Arg-77.
CC {ECO:0000269|PubMed:9166867, ECO:0000269|PubMed:9192786}.
CC -!- POLYMORPHISM: Inactivating variants in BCAM are responsible for the
CC recessive Lutheran null phenotype Lu(a-b-) of the Lutheran blood group
CC [MIM:247420]. Autosomal recessive inheritance of the Lutheran null
CC blood group phenotype is extremely rare. There is no obvious associated
CC clinical or hematologic pathology, and all patients have been
CC identified through identification of anti-Lu3 antibodies in their
CC serum. {ECO:0000269|PubMed:17319831}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW57297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=lutheran";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/lu/";
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DR EMBL; X83425; CAA58449.1; -; mRNA.
DR EMBL; AY845133; AAV88096.1; -; Genomic_DNA.
DR EMBL; AC092306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC050450; AAH50450.1; -; mRNA.
DR EMBL; X80026; CAA56327.1; -; mRNA.
DR EMBL; EU307108; ABY27636.1; -; Genomic_DNA.
DR EMBL; EU307109; ABY27637.1; -; Genomic_DNA.
DR CCDS; CCDS12644.1; -.
DR PIR; I37202; I37202.
DR PIR; I38000; I38000.
DR RefSeq; NP_001013275.1; NM_001013257.2.
DR RefSeq; NP_005572.2; NM_005581.4.
DR PDB; 2PET; X-ray; 1.70 A; A=32-262.
DR PDB; 2PF6; X-ray; 2.20 A; A/B=32-262.
DR PDBsum; 2PET; -.
DR PDBsum; 2PF6; -.
DR AlphaFoldDB; P50895; -.
DR SMR; P50895; -.
DR BioGRID; 110237; 48.
DR ELM; P50895; -.
DR IntAct; P50895; 35.
DR STRING; 9606.ENSP00000270233; -.
DR GlyConnect; 1026; 9 N-Linked glycans (2 sites).
DR GlyGen; P50895; 5 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; P50895; -.
DR PhosphoSitePlus; P50895; -.
DR SwissPalm; P50895; -.
DR BioMuta; BCAM; -.
DR DMDM; 92058724; -.
DR CPTAC; CPTAC-174; -.
DR CPTAC; CPTAC-175; -.
DR EPD; P50895; -.
DR jPOST; P50895; -.
DR MassIVE; P50895; -.
DR MaxQB; P50895; -.
DR PaxDb; P50895; -.
DR PeptideAtlas; P50895; -.
DR PRIDE; P50895; -.
DR ProteomicsDB; 56268; -.
DR ABCD; P50895; 1 sequenced antibody.
DR Antibodypedia; 17750; 426 antibodies from 35 providers.
DR DNASU; 4059; -.
DR Ensembl; ENST00000270233.12; ENSP00000270233.5; ENSG00000187244.12.
DR GeneID; 4059; -.
DR KEGG; hsa:4059; -.
DR MANE-Select; ENST00000270233.12; ENSP00000270233.5; NM_005581.5; NP_005572.2.
DR UCSC; uc002ozu.5; human.
DR CTD; 4059; -.
DR DisGeNET; 4059; -.
DR GeneCards; BCAM; -.
DR HGNC; HGNC:6722; BCAM.
DR HPA; ENSG00000187244; Tissue enhanced (kidney).
DR MalaCards; BCAM; -.
DR MIM; 111200; phenotype.
DR MIM; 247420; phenotype.
DR MIM; 612773; gene.
DR neXtProt; NX_P50895; -.
DR OpenTargets; ENSG00000187244; -.
DR PharmGKB; PA30484; -.
DR VEuPathDB; HostDB:ENSG00000187244; -.
DR eggNOG; ENOG502QWC8; Eukaryota.
DR GeneTree; ENSGT00940000161038; -.
DR HOGENOM; CLU_028888_1_0_1; -.
DR InParanoid; P50895; -.
DR OMA; CCRRREK; -.
DR OrthoDB; 864786at2759; -.
DR PhylomeDB; P50895; -.
DR TreeFam; TF330534; -.
DR PathwayCommons; P50895; -.
DR SignaLink; P50895; -.
DR BioGRID-ORCS; 4059; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; BCAM; human.
DR EvolutionaryTrace; P50895; -.
DR GeneWiki; BCAM; -.
DR GenomeRNAi; 4059; -.
DR Pharos; P50895; Tbio.
DR PRO; PR:P50895; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P50895; protein.
DR Bgee; ENSG00000187244; Expressed in metanephros cortex and 161 other tissues.
DR ExpressionAtlas; P50895; baseline and differential.
DR Genevisible; P50895; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IC:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IMP:BHF-UCL.
DR GO; GO:0005055; F:laminin receptor activity; IMP:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:CACAO.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 2.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Blood group antigen; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:7777537"
FT CHAIN 32..628
FT /note="Basal cell adhesion molecule"
FT /id="PRO_0000014850"
FT TOPO_DOM 32..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..142
FT /note="Ig-like V-type 1"
FT DOMAIN 147..257
FT /note="Ig-like V-type 2"
FT DOMAIN 274..355
FT /note="Ig-like C2-type 1"
FT DOMAIN 363..441
FT /note="Ig-like C2-type 2"
FT DOMAIN 448..541
FT /note="Ig-like C2-type 3"
FT REGION 309..312
FT /note="Interaction with laminin alpha5"
FT REGION 579..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 596
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:15975931"
FT MOD_RES 598
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:15975931"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 621
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15975931"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952"
FT DISULFID 53..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17638854"
FT DISULFID 172..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17638854"
FT DISULFID 291..337
FT /evidence="ECO:0000305|PubMed:17638854"
FT DISULFID 384..424
FT /evidence="ECO:0000305|PubMed:17638854"
FT DISULFID 473..522
FT /evidence="ECO:0000305|PubMed:17638854"
FT VARIANT 77
FT /note="R -> H (defines the Lu(a) antigen;
FT dbSNP:rs28399653)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021348"
FT VARIANT 196
FT /note="V -> I (in dbSNP:rs28399654)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021349"
FT VARIANT 204
FT /note="M -> K (in dbSNP:rs28399656)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021350"
FT VARIANT 282
FT /note="R -> H (in dbSNP:rs9967601)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021351"
FT VARIANT 381
FT /note="V -> I (in dbSNP:rs28399626)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021352"
FT VARIANT 451
FT /note="K -> Q (in dbSNP:rs28399630)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021353"
FT VARIANT 539
FT /note="T -> A (in dbSNP:rs1135062)"
FT /evidence="ECO:0000269|PubMed:7777537,
FT ECO:0000269|PubMed:7954395, ECO:0000269|Ref.7"
FT /id="VAR_021354"
FT VARIANT 581
FT /note="Q -> L (in dbSNP:rs28399659)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_021355"
FT MUTAGEN 621
FT /note="S->A: Dramatically reduced cell adhesion."
FT /evidence="ECO:0000269|PubMed:15975931"
FT CONFLICT 225..226
FT /note="RL -> PC (in Ref. 6; CAA56327)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..356
FT /note="EL -> DV (in Ref. 6; CAA56327)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="R -> L (in Ref. 7; ABY27636)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2PF6"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2PF6"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2PET"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:2PET"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 167..179
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2PF6"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:2PET"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:2PET"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2PET"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:2PET"
SQ SEQUENCE 628 AA; 67405 MW; C88F4F5C640C3F5B CRC64;
MEPPDAPAQA RGAPRLLLLA VLLAAHPDAQ AEVRLSVPPL VEVMRGKSVI LDCTPTGTHD
HYMLEWFLTD RSGARPRLAS AEMQGSELQV TMHDTRGRSP PYQLDSQGRL VLAEAQVGDE
RDYVCVVRAG AAGTAEATAR LNVFAKPEAT EVSPNKGTLS VMEDSAQEIA TCNSRNGNPA
PKITWYRNGQ RLEVPVEMNP EGYMTSRTVR EASGLLSLTS TLYLRLRKDD RDASFHCAAH
YSLPEGRHGR LDSPTFHLTL HYPTEHVQFW VGSPSTPAGW VREGDTVQLL CRGDGSPSPE
YTLFRLQDEQ EEVLNVNLEG NLTLEGVTRG QSGTYGCRVE DYDAADDVQL SKTLELRVAY
LDPLELSEGK VLSLPLNSSA VVNCSVHGLP TPALRWTKDS TPLGDGPMLS LSSITFDSNG
TYVCEASLPT VPVLSRTQNF TLLVQGSPEL KTAEIEPKAD GSWREGDEVT LICSARGHPD
PKLSWSQLGG SPAEPIPGRQ GWVSSSLTLK VTSALSRDGI SCEASNPHGN KRHVFHFGTV
SPQTSQAGVA VMAVAVSVGL LLLVVAVFYC VRRKGGPCCR QRREKGAPPP GEPGLSHSGS
EQPEQTGLLM GGASGGARGG SGGFGDEC
