##gff-version 3 P06731 UniProtKB Signal peptide 1 34 . . . . P06731 UniProtKB Chain 35 685 . . . ID=PRO_0000014566;Note=Carcinoembryonic antigen-related cell adhesion molecule 5 P06731 UniProtKB Propeptide 686 702 . . . ID=PRO_0000014567;Note=Removed in mature form;Ontology_term=ECO:0000255;evidence=ECO:0000255 P06731 UniProtKB Domain 35 144 . . . Note=Ig-like V-type;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31997 P06731 UniProtKB Domain 145 232 . . . Note=Ig-like C2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Domain 240 315 . . . Note=Ig-like C2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Domain 323 410 . . . Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Domain 418 495 . . . Note=Ig-like C2-type 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Domain 501 588 . . . Note=Ig-like C2-type 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Domain 593 675 . . . Note=Ig-like C2-type 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Lipidation 685 685 . . . Note=GPI-anchor amidated alanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2317824;Dbxref=PMID:2317824 P06731 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 115 115 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 182 182 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 204 204 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 208 208 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 246 246 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00498,ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218 P06731 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 274 274 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 292 292 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 309 309 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 330 330 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 351 351 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 360 360 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 375 375 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 432 432 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 466 466 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 480 480 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 508 508 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 529 529 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 553 553 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 560 560 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00498,ECO:0000269|PubMed:16740002;Dbxref=PMID:16740002 P06731 UniProtKB Glycosylation 580 580 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 612 612 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 650 650 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Glycosylation 665 665 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P06731 UniProtKB Disulfide bond 167 215 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Disulfide bond 259 299 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Disulfide bond 345 393 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Disulfide bond 437 477 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Disulfide bond 523 571 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Disulfide bond 615 655 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P06731 UniProtKB Alternative sequence 320 320 . . . ID=VSP_053414;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:3814146;Dbxref=PMID:3814146 P06731 UniProtKB Natural variant 80 80 . . . ID=VAR_061310;Note=I->V;Dbxref=dbSNP:rs12971352 P06731 UniProtKB Natural variant 83 83 . . . ID=VAR_061311;Note=V->A;Dbxref=dbSNP:rs28683503 P06731 UniProtKB Natural variant 137 137 . . . ID=VAR_056028;Note=Q->P;Dbxref=dbSNP:rs3815780 P06731 UniProtKB Natural variant 340 340 . . . ID=VAR_031091;Note=A->D;Dbxref=dbSNP:rs10407503 P06731 UniProtKB Natural variant 398 398 . . . ID=VAR_024493;Note=E->K;Dbxref=dbSNP:rs7249230 P06731 UniProtKB Natural variant 664 664 . . . ID=VAR_031092;Note=R->S;Dbxref=dbSNP:rs10423171 P06731 UniProtKB Natural variant 678 678 . . . ID=VAR_056029;Note=G->R;Dbxref=dbSNP:rs9621 P06731 UniProtKB Mutagenesis 63 63 . . . Note=No effect on dimerization. Reduced affinity for E.coli Dr adhesins. F->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 63 63 . . . Note=Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 66 66 . . . Note=Abolishes dimerization. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10864933,ECO:0000269|PubMed:18086185;Dbxref=PMID:10864933,PMID:18086185 P06731 UniProtKB Mutagenesis 68 68 . . . Note=Abolishes dimerization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10864933;Dbxref=PMID:10864933 P06731 UniProtKB Mutagenesis 68 68 . . . Note=No effect on dimerization. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10864933;Dbxref=PMID:10864933 P06731 UniProtKB Mutagenesis 69 69 . . . Note=Abolishes dimerization. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10864933;Dbxref=PMID:10864933 P06731 UniProtKB Mutagenesis 73 73 . . . Note=Abolishes dimerization. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 74 74 . . . Note=No effect on dimerization. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 74 74 . . . Note=Abolishes dimerization. D->L%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 78 78 . . . Note=Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Q->L%2CR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10864933,ECO:0000269|PubMed:18086185;Dbxref=PMID:10864933,PMID:18086185 P06731 UniProtKB Mutagenesis 125 125 . . . Note=Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 129 129 . . . Note=No effect on dimerization. Reduced affinity for E.coli Dr adhesins. L->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 129 129 . . . Note=Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Mutagenesis 133 133 . . . Note=Abolishes dimerization. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086185;Dbxref=PMID:18086185 P06731 UniProtKB Sequence conflict 641 641 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06731 UniProtKB Sequence conflict 646 646 . . . Note=T->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06731 UniProtKB Sequence conflict 689 689 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P06731 UniProtKB Beta strand 37 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 51 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 60 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Helix 75 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Turn 84 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 88 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Helix 114 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 118 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ P06731 UniProtKB Beta strand 132 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QSQ