##gff-version 3 Q15848 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15340161,ECO:0000269|PubMed:8947845;Dbxref=PMID:15340161,PMID:8947845 Q15848 UniProtKB Chain 19 244 . . . ID=PRO_0000003543;Note=Adiponectin Q15848 UniProtKB Domain 42 107 . . . Note=Collagen-like Q15848 UniProtKB Domain 108 244 . . . Note=C1q;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00368 Q15848 UniProtKB Region 40 101 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15848 UniProtKB Compositional bias 58 72 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15848 UniProtKB Site 62 62 . . . Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Site 86 86 . . . Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Site 104 104 . . . Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Site 230 230 . . . Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 33 33 . . . Note=5-hydroxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3Y5Z3 Q15848 UniProtKB Modified residue 36 36 . . . Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60994 Q15848 UniProtKB Modified residue 44 44 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 47 47 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 53 53 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 65 65 . . . Note=5-hydroxylysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 68 68 . . . Note=5-hydroxylysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 71 71 . . . Note=4-hydroxyproline%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 76 76 . . . Note=4-hydroxyproline%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 77 77 . . . Note=5-hydroxylysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 91 91 . . . Note=4-hydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 95 95 . . . Note=4-hydroxyproline%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Modified residue 101 101 . . . Note=5-hydroxylysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Glycosylation 21 21 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19855092;Dbxref=PMID:19855092 Q15848 UniProtKB Glycosylation 22 22 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19855092;Dbxref=PMID:19855092 Q15848 UniProtKB Glycosylation 65 65 . . . Note=O-linked (Gal...) hydroxylysine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Glycosylation 68 68 . . . Note=O-linked (Gal...) hydroxylysine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Glycosylation 77 77 . . . Note=O-linked (Gal...) hydroxylysine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Glycosylation 101 101 . . . Note=O-linked (Gal...) hydroxylysine%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Disulfide bond 36 36 . . . Note=Interchain%3B in form MMW and form HMW;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12878598,ECO:0000269|PubMed:16497731;Dbxref=PMID:12878598,PMID:16497731 Q15848 UniProtKB Natural variant 84 84 . . . ID=VAR_013273;Note=Does not form high molecular weight multimers. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11812766,ECO:0000269|PubMed:12354786,ECO:0000269|PubMed:12878598;Dbxref=dbSNP:rs199646033,PMID:11812766,PMID:12354786,PMID:12878598 Q15848 UniProtKB Natural variant 90 90 . . . ID=VAR_027395;Note=Does not form high molecular weight multimers. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12354786,ECO:0000269|PubMed:12878598;Dbxref=dbSNP:rs62625753,PMID:12354786,PMID:12878598 Q15848 UniProtKB Natural variant 111 111 . . . ID=VAR_027396;Note=Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12354786;Dbxref=dbSNP:rs17366743,PMID:12354786 Q15848 UniProtKB Natural variant 112 112 . . . ID=VAR_013274;Note=In ADPOD%3B does not assemble into trimers resulting in impaired secretion from the cell. R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10918532,ECO:0000269|PubMed:12086969,ECO:0000269|PubMed:12878598;Dbxref=dbSNP:rs121917815,PMID:10918532,PMID:12086969,PMID:12878598 Q15848 UniProtKB Natural variant 117 117 . . . ID=VAR_013275;Note=V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11812766;Dbxref=dbSNP:rs747223144,PMID:11812766 Q15848 UniProtKB Natural variant 164 164 . . . ID=VAR_013276;Note=In ADPOD%3B does not assemble into trimers resulting in impaired secretion from the cell. I->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11812766,ECO:0000269|PubMed:12086969,ECO:0000269|PubMed:12878598;Dbxref=dbSNP:rs185847354,PMID:11812766,PMID:12086969,PMID:12878598 Q15848 UniProtKB Natural variant 221 221 . . . ID=VAR_013277;Note=R->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11812766,ECO:0000269|PubMed:12086969;Dbxref=dbSNP:rs138773406,PMID:11812766,PMID:12086969 Q15848 UniProtKB Natural variant 241 241 . . . ID=VAR_013278;Note=H->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11812766,ECO:0000269|PubMed:12086969;Dbxref=dbSNP:rs141205818,PMID:11812766,PMID:12086969 Q15848 UniProtKB Mutagenesis 20 20 . . . Note=No change in sialylated isoforms. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19855092;Dbxref=PMID:19855092 Q15848 UniProtKB Mutagenesis 21 21 . . . Note=Some loss of sialylated isoforms. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19855092;Dbxref=PMID:19855092 Q15848 UniProtKB Mutagenesis 22 22 . . . Note=Abolishes sialylated isoforms. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19855092;Dbxref=PMID:19855092 Q15848 UniProtKB Mutagenesis 33 33 . . . Note=No effect on formation of HMW multimers. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Mutagenesis 36 36 . . . Note=Impaired formation of MMW and HMW multimers. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12878598,ECO:0000269|PubMed:16497731;Dbxref=PMID:12878598,PMID:16497731 Q15848 UniProtKB Mutagenesis 65 65 . . . Note=Impaired formation of HMW multimers%3B when associated with R-68. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Mutagenesis 68 68 . . . Note=Impaired formation of HMW multimers%3B when associated with R-65. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Mutagenesis 77 77 . . . Note=Impaired formation of HMW multimers%3B when associated with R-101. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Mutagenesis 101 101 . . . Note=Impaired formation of HMW multimers%3B when associated with R-77. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497731;Dbxref=PMID:16497731 Q15848 UniProtKB Beta strand 114 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 126 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U6N Q15848 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Turn 145 147 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 156 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 180 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 195 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 210 216 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 222 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66 Q15848 UniProtKB Beta strand 233 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6U66