##gff-version 3
Q60994	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Chain	18	247	.	.	.	ID=PRO_0000003544;Note=Adiponectin	
Q60994	UniProtKB	Domain	45	110	.	.	.	Note=Collagen-like	
Q60994	UniProtKB	Domain	111	247	.	.	.	Note=C1q;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00368	
Q60994	UniProtKB	Region	44	105	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q60994	UniProtKB	Compositional bias	61	75	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q60994	UniProtKB	Site	79	79	.	.	.	Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Site	98	98	.	.	.	Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Site	107	107	.	.	.	Note=Not hydroxylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Site	233	233	.	.	.	Note=Not glycosylated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Modified residue	36	36	.	.	.	Note=5-hydroxylysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3Y5Z3	
Q60994	UniProtKB	Modified residue	39	39	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19592500;Dbxref=PMID:19592500	
Q60994	UniProtKB	Modified residue	47	47	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q60994	UniProtKB	Modified residue	50	50	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q60994	UniProtKB	Modified residue	56	56	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q60994	UniProtKB	Modified residue	68	68	.	.	.	Note=5-hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Modified residue	71	71	.	.	.	Note=5-hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Modified residue	80	80	.	.	.	Note=5-hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Modified residue	94	94	.	.	.	Note=4-hydroxyproline;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11912203;Dbxref=PMID:11912203	
Q60994	UniProtKB	Modified residue	104	104	.	.	.	Note=5-hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Glycosylation	23	23	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19855092;Dbxref=PMID:19855092	
Q60994	UniProtKB	Glycosylation	24	24	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19855092;Dbxref=PMID:19855092	
Q60994	UniProtKB	Glycosylation	68	68	.	.	.	Note=O-linked (Gal...) hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Glycosylation	71	71	.	.	.	Note=O-linked (Gal...) hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Glycosylation	80	80	.	.	.	Note=O-linked (Gal...) hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Glycosylation	104	104	.	.	.	Note=O-linked (Gal...) hydroxylysine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11912203,ECO:0000269|PubMed:23209641;Dbxref=PMID:11912203,PMID:23209641	
Q60994	UniProtKB	Disulfide bond	39	39	.	.	.	Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q60994	UniProtKB	Mutagenesis	39	39	.	.	.	Note=No change in the interaction with CTRP9. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18787108;Dbxref=PMID:18787108	
Q60994	UniProtKB	Mutagenesis	68	68	.	.	.	Note=Impaired formation of HMW multimers%3B when associated with R-71%3B R-80 and R-104. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16621799;Dbxref=PMID:16621799	
Q60994	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Impaired formation of HMW multimers%3B when associated with R-68%3B R-80 and R-104. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16621799;Dbxref=PMID:16621799	
Q60994	UniProtKB	Mutagenesis	80	80	.	.	.	Note=Impaired formation of HMW multimers%3B when associated with R-68%3B R-71 and R-104. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16621799;Dbxref=PMID:16621799	
Q60994	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Impaired formation of HMW multimers%3B when associated with R-68%3B R-71 and R-80. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16621799;Dbxref=PMID:16621799	
Q60994	UniProtKB	Sequence conflict	50	50	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Sequence conflict	74	74	.	.	.	Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Sequence conflict	113	113	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Sequence conflict	117	117	.	.	.	Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Sequence conflict	148	148	.	.	.	Note=G->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Sequence conflict	243	243	.	.	.	Note=Y->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60994	UniProtKB	Beta strand	117	121	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	130	132	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C3H	
Q60994	UniProtKB	Beta strand	137	140	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Turn	148	150	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	152	154	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C3H	
Q60994	UniProtKB	Beta strand	159	172	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	174	180	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	183	190	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	197	208	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	213	218	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28	
Q60994	UniProtKB	Beta strand	236	244	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1C28