ID M3XW64_MUSPF Unreviewed; 244 AA.
AC M3XW64;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Adiponectin {ECO:0000313|Ensembl:ENSMPUP00000003314.1, ECO:0000313|RefSeq:XP_004745276.1, ECO:0000313|RefSeq:XP_012908054.1};
GN Name=ADIPOQ {ECO:0000313|Ensembl:ENSMPUP00000003314.1,
GN ECO:0000313|RefSeq:XP_004745276.1, ECO:0000313|RefSeq:XP_012908054.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003314.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003314.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004745276.1, ECO:0000313|RefSeq:XP_012908054.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004745276.1,
RC ECO:0000313|RefSeq:XP_012908054.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AEYP01017244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004745276.1; XM_004745219.3.
DR RefSeq; XP_012908054.1; XM_013052600.2.
DR STRING; 9669.ENSMPUP00000003314; -.
DR Ensembl; ENSMPUT00000003379.1; ENSMPUP00000003314.1; ENSMPUG00000003346.1.
DR GeneID; 101672501; -.
DR KEGG; mpuf:101672501; -.
DR CTD; 9370; -.
DR eggNOG; ENOG502QRY3; Eukaryota.
DR GeneTree; ENSGT00940000159828; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR OMA; DSTFMGF; -.
DR OrthoDB; 4246467at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005179; F:hormone activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0033691; F:sialic acid binding; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0070994; P:detection of oxidative stress; IEA:Ensembl.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0090317; P:negative regulation of intracellular protein transport; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:2000590; P:negative regulation of metanephric mesenchymal cell migration; IEA:Ensembl.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:2000584; P:negative regulation of platelet-derived growth factor receptor-alpha signaling pathway; IEA:Ensembl.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:2000478; P:positive regulation of metanephric podocyte development; IEA:Ensembl.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000534; P:positive regulation of renal albumin absorption; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF20; ADIPONECTIN; 1.
DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..244
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118058"
FT DOMAIN 108..244
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 41..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 244 AA; 26334 MW; 1037087DDC95E1A7 CRC64;
MLLPRAVLLL LVLPTHGQNS VTEGPGVLLP PPKGACTGWV AGIPGHPGHN GTPGRDGRDG
TPGEKGEKGD PGLIGPKGDT GETGVTGVEG PRGFPGTPGR KGEPGESAYV HRSAFSVGLE
SRVTVPNVPI RFTKIFYNLQ NHYDGTTGKF HCNIPGLYYF SYHITVYLKD VKVSLYKKDK
AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGDGN SYGVYADNVH DSTFTGFLLY
HDTN
//
