##gff-version 3 P16573 UniProtKB Signal peptide 1 34 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P16573 UniProtKB Chain 35 519 . . . ID=PRO_0000014564;Note=Carcinoembryonic antigen-related cell adhesion molecule 1 P16573 UniProtKB Topological domain 35 425 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16573 UniProtKB Transmembrane 426 446 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16573 UniProtKB Topological domain 447 519 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16573 UniProtKB Domain 42 140 . . . Note=Ig-like V-type;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31997 P16573 UniProtKB Domain 147 232 . . . Note=Ig-like C2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Domain 237 317 . . . Note=Ig-like C2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Domain 325 403 . . . Note=Ig-like C2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Region 39 142 . . . Note=Required for homophilic binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8831574;Dbxref=PMID:8831574 P16573 UniProtKB Region 445 457 . . . Note=Interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8576129;Dbxref=PMID:8576129 P16573 UniProtKB Region 447 519 . . . Note=Interaction with FLNA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16291724;Dbxref=PMID:16291724 P16573 UniProtKB Region 455 519 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16573 UniProtKB Region 484 519 . . . Note=Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 P16573 UniProtKB Region 513 516 . . . Note=Essential for interaction with PTPN11 and PTPN6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31809 P16573 UniProtKB Compositional bias 467 513 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16573 UniProtKB Modified residue 35 35 . . . Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P13688 P16573 UniProtKB Modified residue 488 488 . . . Note=Phosphotyrosine%3B by SRC%2C LCK%2C INSR and EGFR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15467833,ECO:0000269|PubMed:16054098,ECO:0000269|PubMed:7518458,ECO:0000269|PubMed:7626603,ECO:0000269|PubMed:9712832;Dbxref=PMID:15467833,PMID:16054098,PMID:7518458,PMID:7626603,PMID:9712832 P16573 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16054098,ECO:0000269|PubMed:7518458;Dbxref=PMID:16054098,PMID:7518458 P16573 UniProtKB Modified residue 513 513 . . . Note=Phosphotyrosine%3B by INSR%2C SRC and LCK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16054098;Dbxref=PMID:16054098 P16573 UniProtKB Glycosylation 87 87 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 104 104 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 113 113 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 148 148 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 152 152 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 173 173 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 197 197 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 224 224 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 256 256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 288 288 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 292 292 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 302 302 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 315 315 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 331 331 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Glycosylation 374 374 . . . Note=N-linked (GlcNAc...) asparagine%3B atypical;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P31809,ECO:0000255|PROSITE-ProRule:PRU00498 P16573 UniProtKB Disulfide bond 167 215 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Disulfide bond 259 299 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Disulfide bond 344 392 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16573 UniProtKB Alternative sequence 455 458 . . . ID=VSP_002504;Note=In isoform 2. GSDH->SGSF;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:1637321,ECO:0000303|PubMed:8504806,ECO:0000303|PubMed:8536699;Dbxref=PMID:1637321,PMID:8504806,PMID:8536699 P16573 UniProtKB Alternative sequence 459 519 . . . ID=VSP_002505;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:1637321,ECO:0000303|PubMed:8504806,ECO:0000303|PubMed:8536699;Dbxref=PMID:1637321,PMID:8504806,PMID:8536699 P16573 UniProtKB Natural variant 49 49 . . . Note=In allele b. K->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 55 55 . . . Note=In allele b. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 70 70 . . . Note=In allele b. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 73 73 . . . Note=In allele b. L->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 74 74 . . . Note=In allele b. N->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 75 75 . . . Note=In allele b. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 76 76 . . . Note=In allele b. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 86 86 . . . Note=In allele b. D->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 88 88 . . . Note=In allele b. M->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 90 90 . . . Note=In allele b. K->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 92 92 . . . Note=In allele b. G->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 99 99 . . . Note=In allele b. E->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 118 118 . . . Note=In allele b. R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 119 119 . . . Note=In allele b. A->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 125 125 . . . Note=In allele b. F->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Natural variant 127 127 . . . Note=In allele b. Q->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1637321,ECO:0000269|PubMed:8504806;Dbxref=PMID:15489334,PMID:1637321,PMID:8504806 P16573 UniProtKB Mutagenesis 488 488 . . . Note=Phosphorylated on serine. Decreases bile acid transport Doesn't phosphorylated by EGFR. Doesn't increase interaction with SHC1. Completely inhibits insulin-stimulated phosphorylation. No effect on INSR internalization and INS degradation. Prevents CEACAM1 phosphorylation and the increase in its binding to FASN in the presence of INSR. No effect on cell-surface expression in response to INS. Abolishes phosphorylation by INSR. Abolishes indirect interaction with INSR. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15467833,ECO:0000269|PubMed:16054098,ECO:0000269|PubMed:7518458,ECO:0000269|PubMed:7592607,ECO:0000269|PubMed:7626603,ECO:0000269|PubMed:9712832;Dbxref=PMID:15467833,PMID:16054098,PMID:7518458,PMID:7592607,PMID:7626603,PMID:9712832 P16573 UniProtKB Mutagenesis 502 503 . . . Note=Phosphorylated on tyrosine. Impairs bile acid transport. TS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7518458;Dbxref=PMID:7518458 P16573 UniProtKB Mutagenesis 503 503 . . . Note=Abolishes phosphorylation by EGFR. Reduces interaction with SHC1. Completely inhibits insulin-stimulated phosphorylation. No effect on INSR internalization and INS degradation. In L-SACC1%3B completely inhibits insulin-stimulated phosphorylation%3B develops hyperinsulinemia resulting from impaired insulin clearance%3B the hyperinsulinemia causes secondary insulin resistance with impaired glucose tolerance and random%2C but not fasting%2C hyperglycemia%3B insulin doesn't significantly decrease FASN activity in liver. Prevents CEACAM1 phosphorylation and the increase in its binding to FASN in the presence of INSR. No effect on cell-surface expression in response to INS. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11694516,ECO:0000269|PubMed:11850617,ECO:0000269|PubMed:15467833,ECO:0000269|PubMed:16054098,ECO:0000269|PubMed:7592607,ECO:0000269|PubMed:7626603,ECO:0000269|PubMed:9712832;Dbxref=PMID:11694516,PMID:11850617,PMID:15467833,PMID:16054098,PMID:7592607,PMID:7626603,PMID:9712832 P16573 UniProtKB Mutagenesis 503 503 . . . Note=Preserves the ability of INSR to induce CEACAM1 phosphorylation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16054098;Dbxref=PMID:16054098 P16573 UniProtKB Mutagenesis 513 513 . . . Note=Increases INSR internalization and INS degradation. Phosphorylated by INSR. Prevents the increase in CEACAM1 binding to FASN by INSR. Decreases cell-surface expression in response to INS. Doesn't affect phosphorylation by INSR. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16054098,ECO:0000269|PubMed:7592607,ECO:0000269|PubMed:9712832;Dbxref=PMID:16054098,PMID:7592607,PMID:9712832