ADIPL_HUMAN
ID ADIPL_HUMAN Reviewed; 302 AA.
AC Q5T7M4; Q5EBL5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Adipolin;
DE AltName: Full=Adipose-derived insulin-sensitizing factor;
DE AltName: Full=C1q and TNF related protein 12 {ECO:0000303|PubMed:22275362};
DE AltName: Full=Complement C1q tumor necrosis factor-related protein 12;
DE Contains:
DE RecName: Full=Adipolin fC1QTNF12;
DE AltName: Full=Adipolin fCTRP12;
DE AltName: Full=Adipolin full-length form;
DE Contains:
DE RecName: Full=Adipolin gC1QTNF12;
DE AltName: Full=Adipolin cleaved form;
DE AltName: Full=Adipolin gCTRP12;
DE Flags: Precursor;
GN Name=C1QTNF12 {ECO:0000312|HGNC:HGNC:32308};
GN Synonyms=C1QDC2, CTRP12, FAM132A {ECO:0000312|HGNC:HGNC:32308};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22275362; DOI=10.1074/jbc.m111.303651;
RA Wei Z., Peterson J.M., Lei X., Cebotaru L., Wolfgang M.J., Baldeviano G.C.,
RA Wong G.W.;
RT "C1q/TNF-related protein-12 (CTRP12), a novel adipokine that improves
RT insulin sensitivity and glycemic control in mouse models of obesity and
RT diabetes.";
RL J. Biol. Chem. 287:10301-10315(2012).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24492466; DOI=10.1530/joe-13-0537;
RA Tan B.K., Lewandowski K.C., O'Hare J.P., Randeva H.S.;
RT "Insulin regulates the novel adipokine adipolin/CTRP12: in vivo and ex vivo
RT effects.";
RL J. Endocrinol. 221:111-119(2014).
CC -!- FUNCTION: Insulin-sensitizing adipocyte-secreted protein (adipokine)
CC that regulates glucose metabolism in liver and adipose tissue. Promotes
CC glucose uptake in adipocytes and suppresses de novo glucose production
CC in hepatocytes via the PI3K-Akt signaling pathway. Administration lead
CC to reduction of blood glucose. Able to attenuate inflammation in fat
CC tissue. {ECO:0000250|UniProtKB:Q8R2Z0}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked. May interact with ERFE (By
CC similarity). {ECO:0000250|UniProtKB:Q8R2Z0}.
CC -!- SUBCELLULAR LOCATION: [Adipolin fC1QTNF12]: Secreted
CC {ECO:0000269|PubMed:22275362}.
CC -!- SUBCELLULAR LOCATION: [Adipolin gC1QTNF12]: Secreted
CC {ECO:0000269|PubMed:22275362}. Note=In sera is the predominant form.
CC {ECO:0000269|PubMed:22275362}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed by adipose tissues.
CC {ECO:0000269|PubMed:22275362}.
CC -!- INDUCTION: By insulin in subcutaneous adipose tissue.
CC {ECO:0000269|PubMed:24492466}.
CC -!- PTM: Processed into Adipolin fC1QTNF12 and Adipolin gC1QTNF12 by FURIN.
CC Insulin enhances endogenous C1QTNF12 cleavage.
CC {ECO:0000250|UniProtKB:Q8R2Z0}.
CC -!- SIMILARITY: Belongs to the adipolin/erythroferrone family.
CC {ECO:0000305}.
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DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089443; AAH89443.1; -; mRNA.
DR CCDS; CCDS30554.1; -.
DR RefSeq; NP_001014980.1; NM_001014980.2.
DR AlphaFoldDB; Q5T7M4; -.
DR STRING; 9606.ENSP00000329137; -.
DR GlyGen; Q5T7M4; 1 site.
DR PhosphoSitePlus; Q5T7M4; -.
DR BioMuta; C1QTNF12; -.
DR DMDM; 145558864; -.
DR MassIVE; Q5T7M4; -.
DR PaxDb; Q5T7M4; -.
DR PeptideAtlas; Q5T7M4; -.
DR PRIDE; Q5T7M4; -.
DR ProteomicsDB; 64664; -.
DR Antibodypedia; 12127; 49 antibodies from 13 providers.
DR DNASU; 388581; -.
DR Ensembl; ENST00000330388.2; ENSP00000329137.2; ENSG00000184163.3.
DR GeneID; 388581; -.
DR KEGG; hsa:388581; -.
DR MANE-Select; ENST00000330388.2; ENSP00000329137.2; NM_001014980.3; NP_001014980.1.
DR UCSC; uc001adl.3; human.
DR CTD; 388581; -.
DR DisGeNET; 388581; -.
DR GeneCards; C1QTNF12; -.
DR HGNC; HGNC:32308; C1QTNF12.
DR HPA; ENSG00000184163; Tissue enhanced (intestine, kidney, skin).
DR MIM; 616593; gene.
DR neXtProt; NX_Q5T7M4; -.
DR OpenTargets; ENSG00000184163; -.
DR PharmGKB; PA162386101; -.
DR VEuPathDB; HostDB:ENSG00000184163; -.
DR eggNOG; ENOG502QQVR; Eukaryota.
DR GeneTree; ENSGT00940000160300; -.
DR HOGENOM; CLU_057344_1_0_1; -.
DR InParanoid; Q5T7M4; -.
DR OMA; RCRGRDK; -.
DR OrthoDB; 1462460at2759; -.
DR PhylomeDB; Q5T7M4; -.
DR TreeFam; TF331282; -.
DR PathwayCommons; Q5T7M4; -.
DR BioGRID-ORCS; 388581; 15 hits in 1067 CRISPR screens.
DR GenomeRNAi; 388581; -.
DR Pharos; Q5T7M4; Tbio.
DR PRO; PR:Q5T7M4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T7M4; protein.
DR Bgee; ENSG00000184163; Expressed in mucosa of transverse colon and 101 other tissues.
DR Genevisible; Q5T7M4; HS.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0046323; P:glucose import; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046326; P:positive regulation of glucose import; IBA:GO_Central.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0046324; P:regulation of glucose import; ISS:UniProtKB.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..302
FT /note="Adipolin fC1QTNF12"
FT /evidence="ECO:0000250|UniProtKB:Q8R2Z0"
FT /id="PRO_0000284354"
FT CHAIN 98..302
FT /note="Adipolin gC1QTNF12"
FT /evidence="ECO:0000250|UniProtKB:Q8R2Z0"
FT /id="PRO_0000430248"
FT DOMAIN 147..302
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 28..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 97..98
FT /note="Cleavage; by FURIN"
FT /evidence="ECO:0000250|UniProtKB:Q8R2Z0"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 14
FT /note="G -> R (in dbSNP:rs7539412)"
FT /id="VAR_054065"
SQ SEQUENCE 302 AA; 32416 MW; 7A3AA620CD94B31A CRC64;
MRRWAWAAVV VLLGPQLVLL GGVGARREAQ RTQQPGQRAD PPNATASASS REGLPEAPKP
SQASGPEFSD AHMTWLNFVR RPDDGALRKR CGSRDKKPRD LFGPPGPPGA EVTAETLLHE
FQELLKEATE RRFSGLLDPL LPQGAGLRLV GEAFHCRLQG PRRVDKRTLV ELHGFQAPAA
QGAFLRGSGL SLASGRFTAP VSGIFQFSAS LHVDHSELQG KARLRARDVV CVLICIESLC
QRHTCLEAVS GLESNSRVFT LQVQGLLQLQ AGQYASVFVD NGSGAVLTIQ AGSSFSGLLL
GT
