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   24-JAN-2024, entry version 206.
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; 58.
DR   ELM; P50895; -.
DR   IntAct; P50895; 37.
DR   MINT; P50895; -.
DR   STRING; 9606.ENSP00000270233; -.
DR   GlyConnect; 1026; 9 N-Linked glycans (2 sites).
DR   GlyCosmos; P50895; 5 sites, 9 glycans.
DR   GlyGen; P50895; 7 sites, 9 N-linked glycans (2 sites), 2 O-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; 9606-ENSP00000270233; -.
DR   PeptideAtlas; P50895; -.
DR   ProteomicsDB; 56268; -.
DR   Pumba; P50895; -.
DR   ABCD; P50895; 1 sequenced antibody.
DR   Antibodypedia; 17750; 487 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   AGR; HGNC:6722; -.
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; GYMTIRT; -.
DR   OrthoDB; 4211322at2759; -.
DR   PhylomeDB; P50895; -.
DR   TreeFam; TF330534; -.
DR   PathwayCommons; P50895; -.
DR   SignaLink; P50895; -.
DR   BioGRID-ORCS; 4059; 18 hits in 1156 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 163 other cell types or tissues.
DR   ExpressionAtlas; P50895; baseline and differential.
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: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: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   CDD; cd00096; Ig; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR11973:SF17; BASAL CELL ADHESION MOLECULE; 1.
DR   PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; P50895; HS.
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
//