##gff-version 3 P17301 UniProtKB Signal peptide 1 29 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2545729;Dbxref=PMID:2545729 P17301 UniProtKB Chain 30 1181 . . . ID=PRO_0000016233;Note=Integrin alpha-2 P17301 UniProtKB Topological domain 30 1132 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Transmembrane 1133 1154 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Topological domain 1155 1181 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Repeat 34 92 . . . Note=FG-GAP 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Repeat 101 161 . . . Note=FG-GAP 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Domain 188 365 . . . Note=VWFA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00219 P17301 UniProtKB Repeat 366 420 . . . Note=FG-GAP 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Repeat 423 475 . . . Note=FG-GAP 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Repeat 477 539 . . . Note=FG-GAP 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Repeat 540 598 . . . Note=FG-GAP 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Repeat 602 664 . . . Note=FG-GAP 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00803 P17301 UniProtKB Region 1155 1161 . . . Note=Interaction with HPS5 P17301 UniProtKB Motif 1157 1161 . . . Note=GFFKR motif P17301 UniProtKB Binding site 499 499 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 501 501 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 503 503 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 507 507 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 563 563 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 565 565 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 567 567 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 571 571 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 627 627 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 629 629 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 631 631 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Binding site 635 635 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08648 P17301 UniProtKB Glycosylation 105 105 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 112 112 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 343 343 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16263699,ECO:0000269|PubMed:19159218,ECO:0000269|PubMed:19349973;Dbxref=PMID:16263699,PMID:19159218,PMID:19349973 P17301 UniProtKB Glycosylation 432 432 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 460 460 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 475 475 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 699 699 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 1057 1057 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 1074 1074 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Glycosylation 1081 1081 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P17301 UniProtKB Disulfide bond 83 92 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Disulfide bond 680 737 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Disulfide bond 789 795 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Disulfide bond 865 876 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Disulfide bond 1019 1050 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Disulfide bond 1055 1060 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P17301 UniProtKB Natural variant 532 532 . . . ID=VAR_076939;Note=I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23368983;Dbxref=dbSNP:rs199808499,PMID:23368983 P17301 UniProtKB Natural variant 534 534 . . . ID=VAR_003977;Note=In alloantigen HPA-5B. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10744142,ECO:0000269|PubMed:2545729,ECO:0000269|PubMed:7901236;Dbxref=dbSNP:rs1801106,PMID:10744142,PMID:2545729,PMID:7901236 P17301 UniProtKB Natural variant 691 691 . . . ID=VAR_029146;Note=N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.2;Dbxref=dbSNP:rs3212557 P17301 UniProtKB Natural variant 927 927 . . . ID=VAR_021855;Note=N->S;Dbxref=dbSNP:rs2287870 P17301 UniProtKB Natural variant 1127 1127 . . . ID=VAR_020036;Note=K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.2;Dbxref=dbSNP:rs3212645 P17301 UniProtKB Mutagenesis 1159 1159 . . . Note=No significant reduction of RAB21-binding by co-immunoprecipitation assay%3B when associated with A-1160 and A-1162. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16754960;Dbxref=PMID:16754960 P17301 UniProtKB Mutagenesis 1160 1160 . . . Note=No effect on RAB21-binding. Significant reduction of RAB21-binding%3B when associated with A-1161. Shows defective cytokinesis on collagen%2C but not on fibronectin%3B when associated with A-1161. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16754960,ECO:0000269|PubMed:18804435;Dbxref=PMID:16754960,PMID:18804435 P17301 UniProtKB Mutagenesis 1161 1161 . . . Note=Significant reduction of RAB21-binding%3B when associated with A-1160. Shows defective cytokinesis on collagen%2C but not on fibronectin%3B when associated with A-1160. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16754960,ECO:0000269|PubMed:18804435;Dbxref=PMID:16754960,PMID:18804435 P17301 UniProtKB Mutagenesis 1162 1162 . . . Note=No significant reduction of RAB21-binding by co-immunoprecipitation assay%3B when associated with A-1159 and A-1160. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16754960,ECO:0000269|PubMed:18804435;Dbxref=PMID:16754960,PMID:18804435 P17301 UniProtKB Mutagenesis 1162 1162 . . . Note=Markedly weakens RAB21-binding. Shows defective cytokinesis on collagen%2C but not on fibronectin. K->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16754960,ECO:0000269|PubMed:18804435;Dbxref=PMID:16754960,PMID:18804435 P17301 UniProtKB Mutagenesis 1164 1164 . . . Note=Significant reduction of RAB21-binding%3B when associated with A-1160%3B A-1161 and A-1165. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16754960;Dbxref=PMID:16754960 P17301 UniProtKB Mutagenesis 1165 1165 . . . Note=Significant reduction of RAB21-binding%3B when associated with A-1160%3B A-1161 and A-1164. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16754960;Dbxref=PMID:16754960 P17301 UniProtKB Sequence conflict 17 17 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P17301 UniProtKB Beta strand 173 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 188 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Beta strand 208 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Turn 226 228 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 232 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 252 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 266 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Beta strand 274 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 292 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Beta strand 304 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 313 317 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 323 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 337 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Beta strand 341 347 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 348 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P P17301 UniProtKB Helix 354 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1V7P