CEAM5_HUMAN
ID CEAM5_HUMAN Reviewed; 702 AA.
AC P06731; H9KVA7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 5;
DE AltName: Full=Carcinoembryonic antigen;
DE Short=CEA;
DE AltName: Full=Meconium antigen 100;
DE AltName: CD_antigen=CD66e;
DE Flags: Precursor;
GN Name=CEACAM5; Synonyms=CEA;
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 [GENOMIC DNA].
RX PubMed=3670312; DOI=10.1128/mcb.7.9.3221-3230.1987;
RA Beauchemin N., Benchimol S., Cournoyer D., Fuks A., Stanners C.P.;
RT "Isolation and characterization of full-length functional cDNA clones for
RT human carcinoembryonic antigen.";
RL Mol. Cell. Biol. 7:3221-3230(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3220478; DOI=10.1016/0888-7543(88)90160-7;
RA Barnett T., Goebel S.J., Nothdurft M.A., Elting J.J.;
RT "Carcinoembryonic antigen family: characterization of cDNAs coding for NCA
RT and CEA and suggestion of nonrandom sequence variation in their conserved
RT loop-domains.";
RL Genomics 3:59-66(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2342461; DOI=10.1128/mcb.10.6.2738-2748.1990;
RA Schrewe H., Thompson J., Bona M., Hefta L.J.F., Maruya A., Hassauer M.,
RA Shively J.E., von Kleist S., Zimmermann W.;
RT "Cloning of the complete gene for carcinoembryonic antigen: analysis of its
RT promoter indicates a region conveying cell type-specific expression.";
RL Mol. Cell. Biol. 10:2738-2748(1990).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-702 (ISOFORM 2).
RX PubMed=3814146; DOI=10.1016/0006-291x(87)90304-4;
RA Oikawa S., Nakazato H., Kosaki G.;
RT "Primary structure of human carcinoembryonic antigen (CEA) deduced from
RT cDNA sequence.";
RL Biochem. Biophys. Res. Commun. 142:511-518(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 331-702 (ISOFORM 1).
RX PubMed=3033671; DOI=10.1073/pnas.84.9.2960;
RA Zimmermann W., Ortlieb B., Friedrich R., von Kleist S.;
RT "Isolation and characterization of cDNA clones encoding the human
RT carcinoembryonic antigen reveal a highly conserved repeating structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2960-2964(1987).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2803308; DOI=10.1016/0006-291x(89)91679-3;
RA Oikawa S., Inuzuka C., Kuroki M., Matsuoka Y., Kosaki G., Nakazato H.;
RT "Cell adhesion activity of non-specific cross-reacting antigen (NCA) and
RT carcinoembryonic antigen (CEA) expressed on CHO cell surface: homophilic
RT and heterophilic adhesion.";
RL Biochem. Biophys. Res. Commun. 164:39-45(1989).
RN [8]
RP SUBCELLULAR LOCATION, AND GPI-ANCHOR AT ALA-685.
RX PubMed=2317824;
RA Hefta L.J., Schrewe H., Thompson J.A., Oikawa S., Nakazato H.,
RA Shively J.E.;
RT "Expression of complementary DNA and genomic clones for carcinoembryonic
RT antigen and nonspecific cross-reacting antigen in Chinese hamster ovary and
RT mouse fibroblast cells and characterization of the membrane-expressed
RT products.";
RL Cancer Res. 50:2397-2403(1990).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10436421; DOI=10.1159/000030075;
RA Fraengsmyr L., Baranov V., Hammarstroem S.;
RT "Four carcinoembryonic antigen subfamily members, CEA, NCA, BGP and CGM2,
RT selectively expressed in the normal human colonic epithelium, are integral
RT components of the fuzzy coat.";
RL Tumor Biol. 20:277-292(1999).
RN [10]
RP FUNCTION.
RX PubMed=10910050;
RA Ordonez C., Screaton R.A., Ilantzis C., Stanners C.P.;
RT "Human carcinoembryonic antigen functions as a general inhibitor of
RT anoikis.";
RL Cancer Res. 60:3419-3424(2000).
RN [11]
RP FUNCTION, MUTAGENESIS OF SER-66; TYR-68; LYS-69 AND GLN-78, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10864933; DOI=10.1074/jbc.m909242199;
RA Taheri M., Saragovi U., Fuks A., Makkerh J., Mort J., Stanners C.P.;
RT "Self recognition in the Ig superfamily. Identification of precise
RT subdomains in carcinoembryonic antigen required for intercellular
RT adhesion.";
RL J. Biol. Chem. 275:26935-26943(2000).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-560.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP SUBUNIT.
RX PubMed=26483485; DOI=10.1073/pnas.1509511112;
RA Bonsor D.A., Gunther S., Beadenkopf R., Beckett D., Sundberg E.J.;
RT "Diverse oligomeric states of CEACAM IgV domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13561-13566(2015).
RN [15]
RP 3D-STRUCTURE MODELING OF 35-676.
RX PubMed=10854848; DOI=10.1016/s0014-5793(00)01612-4;
RA Boehm M.K., Perkins S.J.;
RT "Structural models for carcinoembryonic antigen and its complex with the
RT single-chain Fv antibody molecule MFE23.";
RL FEBS Lett. 475:11-16(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 34-144 IN COMPLEX WITH E.COLI DR
RP ADHESIN, FUNCTION (MICROBIAL INFECTION), SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF PHE-63; SER-66; VAL-73; ASP-74; GLN-78; ILE-125; LEU-129 AND
RP GLU-133.
RX PubMed=18086185; DOI=10.1111/j.1365-2958.2007.06054.x;
RA Korotkova N., Yang Y., Le Trong I., Cota E., Demeler B., Marchant J.,
RA Thomas W.E., Stenkamp R.E., Moseley S.L., Matthews S.;
RT "Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen
RT triggers receptor dissociation.";
RL Mol. Microbiol. 67:420-434(2008).
CC -!- FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion,
CC intracellular signaling and tumor progression (PubMed:2803308,
CC PubMed:10910050, PubMed:10864933). Mediates homophilic and heterophilic
CC cell adhesion with other carcinoembryonic antigen-related cell adhesion
CC molecules, such as CEACAM6 (PubMed:2803308). Plays a role as an
CC oncogene by promoting tumor progression; induces resistance to anoikis
CC of colorectal carcinoma cells (PubMed:10910050).
CC {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:10910050,
CC ECO:0000269|PubMed:2803308}.
CC -!- FUNCTION: (Microbial infection) Receptor for E.coli Dr adhesins.
CC Binding of E.coli Dr adhesins leads to dissociation of the homodimer.
CC {ECO:0000269|PubMed:18086185}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18086185,
CC ECO:0000269|PubMed:26483485}.
CC -!- INTERACTION:
CC P06731; P06731: CEACAM5; NbExp=7; IntAct=EBI-3914938, EBI-3914938;
CC P06731; K0BRG7: S; Xeno; NbExp=4; IntAct=EBI-3914938, EBI-16040613;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10864933,
CC ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}; Lipid-anchor,
CC GPI-anchor {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185,
CC ECO:0000269|PubMed:2317824}. Apical cell membrane
CC {ECO:0000269|PubMed:10436421}. Cell surface
CC {ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:2803308}.
CC Note=Localized to the apical glycocalyx surface.
CC {ECO:0000269|PubMed:10436421}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P06731-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06731-2; Sequence=VSP_053414;
CC -!- TISSUE SPECIFICITY: Expressed in columnar epithelial and goblet cells
CC of the colon (at protein level) (PubMed:10436421). Found in
CC adenocarcinomas of endodermally derived digestive system epithelium and
CC fetal colon. {ECO:0000269|PubMed:10436421}.
CC -!- PTM: Complex immunoreactive glycoprotein with a MW of 180 kDa
CC comprising 60% carbohydrate.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62835.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M17303; AAB59513.1; -; Genomic_DNA.
DR EMBL; M29540; AAA51967.1; -; mRNA.
DR EMBL; M59262; AAA62835.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M59255; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59256; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59257; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59258; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59259; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59260; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59261; AAA62835.1; JOINED; Genomic_DNA.
DR EMBL; M59709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M59710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC243967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X16455; CAA34474.1; -; mRNA.
DR EMBL; M15042; AAA51963.1; -; mRNA.
DR EMBL; M16234; AAA51972.1; -; mRNA.
DR CCDS; CCDS12584.1; -. [P06731-1]
DR CCDS; CCDS77302.1; -. [P06731-2]
DR PIR; A36319; A36319.
DR RefSeq; NP_001278413.1; NM_001291484.2.
DR RefSeq; NP_001295327.1; NM_001308398.1.
DR RefSeq; NP_004354.3; NM_004363.5.
DR PDB; 1E07; X-ray; -; A=35-676.
DR PDB; 2QSQ; X-ray; 1.95 A; A/B=34-144.
DR PDB; 2QST; X-ray; 2.90 A; A/B=34-144.
DR PDB; 2VER; NMR; -; N=35-144.
DR PDBsum; 1E07; -.
DR PDBsum; 2QSQ; -.
DR PDBsum; 2QST; -.
DR PDBsum; 2VER; -.
DR AlphaFoldDB; P06731; -.
DR SMR; P06731; -.
DR BioGRID; 107478; 14.
DR DIP; DIP-57769N; -.
DR IntAct; P06731; 9.
DR MINT; P06731; -.
DR STRING; 9606.ENSP00000221992; -.
DR ChEMBL; CHEMBL3712881; -.
DR DrugBank; DB05097; Labetuzumab.
DR DrugBank; DB08217; S-[(1-Hydroxy-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate.
DR GlyConnect; 1071; 257 N-Linked glycans (15 sites).
DR GlyGen; P06731; 29 sites, 155 N-linked glycans (15 sites).
DR iPTMnet; P06731; -.
DR PhosphoSitePlus; P06731; -.
DR BioMuta; CEACAM5; -.
DR DMDM; 317373456; -.
DR jPOST; P06731; -.
DR MassIVE; P06731; -.
DR MaxQB; P06731; -.
DR PaxDb; P06731; -.
DR PeptideAtlas; P06731; -.
DR PRIDE; P06731; -.
DR ProteomicsDB; 46254; -.
DR ProteomicsDB; 51917; -. [P06731-1]
DR ABCD; P06731; 43 sequenced antibodies.
DR Antibodypedia; 3500; 3663 antibodies from 53 providers.
DR DNASU; 1048; -.
DR Ensembl; ENST00000221992.11; ENSP00000221992.5; ENSG00000105388.17. [P06731-1]
DR Ensembl; ENST00000398599.8; ENSP00000381600.4; ENSG00000105388.17. [P06731-2]
DR Ensembl; ENST00000405816.5; ENSP00000385072.1; ENSG00000105388.17. [P06731-1]
DR Ensembl; ENST00000617332.4; ENSP00000482303.1; ENSG00000105388.17. [P06731-1]
DR GeneID; 1048; -.
DR KEGG; hsa:1048; -.
DR MANE-Select; ENST00000221992.11; ENSP00000221992.5; NM_004363.6; NP_004354.3.
DR UCSC; uc002orj.2; human. [P06731-1]
DR CTD; 1048; -.
DR DisGeNET; 1048; -.
DR GeneCards; CEACAM5; -.
DR HGNC; HGNC:1817; CEACAM5.
DR HPA; ENSG00000105388; Tissue enriched (intestine).
DR MIM; 114890; gene.
DR neXtProt; NX_P06731; -.
DR OpenTargets; ENSG00000105388; -.
DR PharmGKB; PA26361; -.
DR VEuPathDB; HostDB:ENSG00000105388; -.
DR eggNOG; ENOG502RXPD; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_024555_7_0_1; -.
DR InParanoid; P06731; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; P06731; -.
DR TreeFam; TF336859; -.
DR PathwayCommons; P06731; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P06731; -.
DR BioGRID-ORCS; 1048; 25 hits in 1074 CRISPR screens.
DR ChiTaRS; CEACAM5; human.
DR EvolutionaryTrace; P06731; -.
DR GeneWiki; CEACAM5; -.
DR GenomeRNAi; 1048; -.
DR Pharos; P06731; Tbio.
DR PRO; PR:P06731; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P06731; protein.
DR Bgee; ENSG00000105388; Expressed in ileal mucosa and 125 other tissues.
DR ExpressionAtlas; P06731; baseline and differential.
DR Genevisible; P06731; HS.
DR GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034235; F:GPI anchor binding; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 7.
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; PF13895; Ig_2; 3.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell adhesion;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Oncogene; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..34
FT CHAIN 35..685
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 5"
FT /id="PRO_0000014566"
FT PROPEP 686..702
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014567"
FT DOMAIN 35..144
FT /note="Ig-like V-type"
FT /evidence="ECO:0000250|UniProtKB:P31997"
FT DOMAIN 145..232
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 240..315
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 323..410
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 418..495
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 501..588
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 593..675
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT LIPID 685
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000269|PubMed:2317824"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:16740002"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 167..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 345..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 437..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 523..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 615..655
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 320
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3814146"
FT /id="VSP_053414"
FT VARIANT 80
FT /note="I -> V (in dbSNP:rs12971352)"
FT /id="VAR_061310"
FT VARIANT 83
FT /note="V -> A (in dbSNP:rs28683503)"
FT /id="VAR_061311"
FT VARIANT 137
FT /note="Q -> P (in dbSNP:rs3815780)"
FT /id="VAR_056028"
FT VARIANT 340
FT /note="A -> D (in dbSNP:rs10407503)"
FT /id="VAR_031091"
FT VARIANT 398
FT /note="E -> K (in dbSNP:rs7249230)"
FT /id="VAR_024493"
FT VARIANT 664
FT /note="R -> S (in dbSNP:rs10423171)"
FT /id="VAR_031092"
FT VARIANT 678
FT /note="G -> R (in dbSNP:rs9621)"
FT /id="VAR_056029"
FT MUTAGEN 63
FT /note="F->I: No effect on dimerization. Reduced affinity
FT for E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 63
FT /note="F->R: Abolishes dimerization. Reduced affinity for
FT E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 66
FT /note="S->N: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:10864933,
FT ECO:0000269|PubMed:18086185"
FT MUTAGEN 68
FT /note="Y->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:10864933"
FT MUTAGEN 68
FT /note="Y->F: No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:10864933"
FT MUTAGEN 69
FT /note="K->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:10864933"
FT MUTAGEN 73
FT /note="V->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 74
FT /note="D->A: No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 74
FT /note="D->L,R: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 78
FT /note="Q->L,R: Abolishes dimerization. Reduced affinity for
FT E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:10864933,
FT ECO:0000269|PubMed:18086185"
FT MUTAGEN 125
FT /note="I->A: Abolishes dimerization. Reduced affinity for
FT E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 129
FT /note="L->A,C: No effect on dimerization. Reduced affinity
FT for E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 129
FT /note="L->S: Abolishes dimerization. Reduced affinity for
FT E.coli Dr adhesins."
FT /evidence="ECO:0000269|PubMed:18086185"
FT MUTAGEN 133
FT /note="E->A: Abolishes dimerization."
FT /evidence="ECO:0000269|PubMed:18086185"
FT CONFLICT 641
FT /note="F -> L (in Ref. 3; AAA62835)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="T -> Q (in Ref. 3; AAA62835)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="V -> A (in Ref. 3; AAA62835)"
FT /evidence="ECO:0000305"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 60..72
FT /evidence="ECO:0007829|PDB:2QSQ"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2QSQ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2QSQ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2QSQ"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:2QSQ"
SQ SEQUENCE 702 AA; 76796 MW; 6299AE26CDDBDB5C CRC64;
MESPSAPPHR WCIPWQRLLL TASLLTFWNP PTTAKLTIES TPFNVAEGKE VLLLVHNLPQ
HLFGYSWYKG ERVDGNRQII GYVIGTQQAT PGPAYSGREI IYPNASLLIQ NIIQNDTGFY
TLHVIKSDLV NEEATGQFRV YPELPKPSIS SNNSKPVEDK DAVAFTCEPE TQDATYLWWV
NNQSLPVSPR LQLSNGNRTL TLFNVTRNDT ASYKCETQNP VSARRSDSVI LNVLYGPDAP
TISPLNTSYR SGENLNLSCH AASNPPAQYS WFVNGTFQQS TQELFIPNIT VNNSGSYTCQ
AHNSDTGLNR TTVTTITVYA EPPKPFITSN NSNPVEDEDA VALTCEPEIQ NTTYLWWVNN
QSLPVSPRLQ LSNDNRTLTL LSVTRNDVGP YECGIQNELS VDHSDPVILN VLYGPDDPTI
SPSYTYYRPG VNLSLSCHAA SNPPAQYSWL IDGNIQQHTQ ELFISNITEK NSGLYTCQAN
NSASGHSRTT VKTITVSAEL PKPSISSNNS KPVEDKDAVA FTCEPEAQNT TYLWWVNGQS
LPVSPRLQLS NGNRTLTLFN VTRNDARAYV CGIQNSVSAN RSDPVTLDVL YGPDTPIISP
PDSSYLSGAN LNLSCHSASN PSPQYSWRIN GIPQQHTQVL FIAKITPNNN GTYACFVSNL
ATGRNNSIVK SITVSASGTS PGLSAGATVG IMIGVLVGVA LI
