##gff-version 3 P16284 UniProtKB Signal peptide 1 27 . . . . P16284 UniProtKB Chain 28 738 . . . ID=PRO_0000014895;Note=Platelet endothelial cell adhesion molecule P16284 UniProtKB Topological domain 28 601 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Transmembrane 602 620 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Topological domain 621 738 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Domain 35 121 . . . Note=Ig-like C2-type 1 P16284 UniProtKB Domain 145 233 . . . Note=Ig-like C2-type 2 P16284 UniProtKB Domain 236 315 . . . Note=Ig-like C2-type 3 P16284 UniProtKB Domain 328 401 . . . Note=Ig-like C2-type 4 P16284 UniProtKB Domain 424 493 . . . Note=Ig-like C2-type 5 P16284 UniProtKB Domain 499 591 . . . Note=Ig-like C2-type 6 P16284 UniProtKB Region 658 715 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16284 UniProtKB Region 709 729 . . . Note=Membrane-bound segment which detaches upon phosphorylation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21464369;Dbxref=PMID:21464369 P16284 UniProtKB Region 721 738 . . . Note=May play a role in cytoprotective signaling P16284 UniProtKB Motif 688 693 . . . Note=ITIM motif 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Motif 711 716 . . . Note=ITIM motif 2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Compositional bias 661 677 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16284 UniProtKB Compositional bias 682 698 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16284 UniProtKB Compositional bias 699 715 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P16284 UniProtKB Modified residue 690 690 . . . Note=Phosphotyrosine%3B by FER;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19342684,ECO:0000269|PubMed:21464369;Dbxref=PMID:19342684,PMID:21464369 P16284 UniProtKB Modified residue 713 713 . . . Note=Phosphotyrosine%3B by FER;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19342684,ECO:0000269|PubMed:21464369,ECO:0000269|PubMed:9298995;Dbxref=PMID:19342684,PMID:21464369,PMID:9298995 P16284 UniProtKB Modified residue 729 729 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21464369;Dbxref=PMID:21464369 P16284 UniProtKB Modified residue 734 734 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21464369;Dbxref=PMID:21464369 P16284 UniProtKB Lipidation 622 622 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17139370;Dbxref=PMID:17139370 P16284 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:26702061,ECO:0007744|PDB:5C14;Dbxref=PMID:26702061 P16284 UniProtKB Glycosylation 84 84 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19349973,ECO:0000269|PubMed:26702061,ECO:0007744|PDB:5C14;Dbxref=PMID:19349973,PMID:26702061 P16284 UniProtKB Glycosylation 151 151 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:26702061,ECO:0007744|PDB:5C14;Dbxref=PMID:19159218,PMID:26702061 P16284 UniProtKB Glycosylation 301 301 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Glycosylation 320 320 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:19349973;Dbxref=PMID:19159218,PMID:19349973 P16284 UniProtKB Glycosylation 344 344 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Glycosylation 356 356 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P16284 UniProtKB Glycosylation 453 453 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218 P16284 UniProtKB Glycosylation 551 551 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973 P16284 UniProtKB Disulfide bond 57 109 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:26702061,ECO:0000269|PubMed:27958302,ECO:0007744|PDB:5C14,ECO:0007744|PDB:5GNI;Dbxref=PMID:26702061,PMID:27958302 P16284 UniProtKB Disulfide bond 152 206 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00114,ECO:0000269|PubMed:26702061,ECO:0000269|PubMed:27958302,ECO:0007744|PDB:5C14,ECO:0007744|PDB:5GNI;Dbxref=PMID:26702061,PMID:27958302 P16284 UniProtKB Disulfide bond 256 304 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16284 UniProtKB Disulfide bond 347 386 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16284 UniProtKB Disulfide bond 431 476 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16284 UniProtKB Disulfide bond 523 572 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 P16284 UniProtKB Alternative sequence 664 681 . . . ID=VSP_011806;Note=In isoform Delta12. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Alternative sequence 682 702 . . . ID=VSP_011807;Note=In isoform Delta13. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Alternative sequence 703 729 . . . ID=VSP_011808;Note=In isoform Delta14-15. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Alternative sequence 703 721 . . . ID=VSP_011809;Note=In isoform Delta14. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Alternative sequence 722 729 . . . ID=VSP_011810;Note=In isoform Delta15. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Alternative sequence 730 738 . . . ID=VSP_011811;Note=In isoform Delta14-15 and isoform Delta15. RTEGSLDGT->ENGRLP;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Natural variant 125 125 . . . ID=VAR_013145;Note=V->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11791967,ECO:0000269|PubMed:1690453,ECO:0000269|PubMed:17212705,ECO:0000269|PubMed:8532023;Dbxref=dbSNP:rs281865545,PMID:11791967,PMID:1690453,PMID:17212705,PMID:8532023 P16284 UniProtKB Natural variant 304 304 . . . ID=VAR_059402;Note=C->Y;Dbxref=dbSNP:rs7209607 P16284 UniProtKB Natural variant 563 563 . . . ID=VAR_059403;Note=S->I;Dbxref=dbSNP:rs12953 P16284 UniProtKB Natural variant 563 563 . . . ID=VAR_059404;Note=S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1700999,ECO:0000269|PubMed:17212705,ECO:0000269|PubMed:7994021,ECO:0000269|Ref.6,ECO:0000269|Ref.9;Dbxref=dbSNP:rs12953,PMID:14702039,PMID:15489334,PMID:1700999,PMID:17212705,PMID:7994021 P16284 UniProtKB Natural variant 670 670 . . . ID=VAR_059405;Note=R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1700999,ECO:0000269|PubMed:17212705,ECO:0000269|Ref.6,ECO:0000269|Ref.9;Dbxref=dbSNP:rs1131012,PMID:14702039,PMID:15489334,PMID:1700999,PMID:17212705 P16284 UniProtKB Mutagenesis 52 52 . . . Note=Probable loss of N-glycosylation. No effect on homophilic cell adhesion%3B when associated with Q-84 and Q-151. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 74 74 . . . Note=Reduced homophilic cell adhesion%3B when associated with E-112%3B E-188 and E-190. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 84 84 . . . Note=Probable loss of N-glycosylation. No effect on homophilic cell adhesion%3B when associated with Q-52 and Q-151. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 89 89 . . . Note=Lacks homophilic binding ability and is distributed over the entire plasma membrane. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19342684;Dbxref=PMID:19342684 P16284 UniProtKB Mutagenesis 112 112 . . . Note=Reduced homophilic cell adhesion%3B when associated with E-74%3B E-188 and E-190. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 151 151 . . . Note=Probable loss of N-glycosylation. No effect on homophilic cell adhesion%3B when associated with Q-52 and Q-84. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 188 188 . . . Note=Reduced homophilic cell adhesion%3B when associated with E-74%3B E-112 and E-190. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 190 190 . . . Note=Reduced homophilic cell adhesion%3B when associated with E-74%3B E-112 and E-188. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27958302;Dbxref=PMID:27958302 P16284 UniProtKB Mutagenesis 622 622 . . . Note=6-fold decrease in association with membrane microdomains. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17139370;Dbxref=PMID:17139370 P16284 UniProtKB Mutagenesis 690 690 . . . Note=No effect on Tyr-713 phosphorylation. Inhibits targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. No effect on interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11%3B when associated with F-713. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18388311,ECO:0000269|PubMed:19342684,ECO:0000269|PubMed:21464369;Dbxref=PMID:18388311,PMID:19342684,PMID:21464369 P16284 UniProtKB Mutagenesis 713 713 . . . Note=Loss of Tyr-690 phosphorylation. Does not inhibit targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. Loss of interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11%3B when associated with F-690. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18388311,ECO:0000269|PubMed:19342684,ECO:0000269|PubMed:21464369;Dbxref=PMID:18388311,PMID:19342684,PMID:21464369 P16284 UniProtKB Sequence conflict 6 6 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Sequence conflict 8 12 . . . Note=GATMW->ADV;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Sequence conflict 80 80 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Sequence conflict 97 97 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Sequence conflict 329 329 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Sequence conflict 430 430 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 P16284 UniProtKB Beta strand 32 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 45 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 53 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 71 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 80 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Helix 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 105 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 123 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 134 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 140 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GNI P16284 UniProtKB Beta strand 147 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 161 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Turn 170 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GNI P16284 UniProtKB Beta strand 174 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 184 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 200 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C14 P16284 UniProtKB Beta strand 222 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GNI P16284 UniProtKB Helix 709 728 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KY5 P16284 UniProtKB Beta strand 731 733 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KY5