C1QT2_HUMAN
ID C1QT2_HUMAN Reviewed; 285 AA.
AC Q9BXJ5;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Complement C1q tumor necrosis factor-related protein 2;
DE Flags: Precursor;
GN Name=C1QTNF2; Synonyms=CTRP2; ORFNames=UNQ6349/PRO21054;
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 [MRNA].
RA Piddington C.S., Bishop P.;
RT "Homo sapiens complement-c1q tumor necrosis factor-related protein.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=31439668; DOI=10.1074/jbc.ra119.009230;
RA Lei X., Wong G.W.;
RT "C1q/TNF-related protein 2 (CTRP2) deletion promotes adipose tissue
RT lipolysis and hepatic triglyceride secretion.";
RL J. Biol. Chem. 294:15638-15649(2019).
CC -!- FUNCTION: Involved in the regulation of lipid metabolism in adipose
CC tissue and liver. {ECO:0000250|UniProtKB:Q9D8U4}.
CC -!- SUBUNIT: May interact with ERFE. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BXJ5; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2817707, EBI-17183751;
CC Q9BXJ5; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2817707, EBI-11524452;
CC Q9BXJ5; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2817707, EBI-8643161;
CC Q9BXJ5; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-2817707, EBI-741528;
CC Q9BXJ5; O95872: GPANK1; NbExp=3; IntAct=EBI-2817707, EBI-751540;
CC Q9BXJ5; P84074: HPCA; NbExp=6; IntAct=EBI-2817707, EBI-12197079;
CC Q9BXJ5; P37235: HPCAL1; NbExp=11; IntAct=EBI-2817707, EBI-749311;
CC Q9BXJ5; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-2817707, EBI-751501;
CC Q9BXJ5; Q53G59: KLHL12; NbExp=6; IntAct=EBI-2817707, EBI-740929;
CC Q9BXJ5; P06239-3: LCK; NbExp=3; IntAct=EBI-2817707, EBI-13287659;
CC Q9BXJ5; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-2817707, EBI-10274069;
CC Q9BXJ5; O75431: MTX2; NbExp=3; IntAct=EBI-2817707, EBI-7415268;
CC Q9BXJ5; P61601: NCALD; NbExp=12; IntAct=EBI-2817707, EBI-749635;
CC Q9BXJ5; P62166: NCS1; NbExp=3; IntAct=EBI-2817707, EBI-746987;
CC Q9BXJ5; O94818-2: NOL4; NbExp=3; IntAct=EBI-2817707, EBI-10190763;
CC Q9BXJ5; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-2817707, EBI-10181968;
CC Q9BXJ5; Q8TCD6: PHOSPHO2; NbExp=3; IntAct=EBI-2817707, EBI-2861380;
CC Q9BXJ5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2817707, EBI-11955057;
CC Q9BXJ5; O60220: TIMM8A; NbExp=3; IntAct=EBI-2817707, EBI-1049822;
CC Q9BXJ5; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2817707, EBI-2130429;
CC Q9BXJ5; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2817707, EBI-10173939;
CC Q9BXJ5; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2817707, EBI-947187;
CC Q9BXJ5; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-2817707, EBI-14096082;
CC Q9BXJ5; P62760: VSNL1; NbExp=3; IntAct=EBI-2817707, EBI-740943;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in adipose tissue.
CC {ECO:0000269|PubMed:31439668}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11699.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH54506.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF329836; AAK17960.1; -; mRNA.
DR EMBL; AY358839; AAQ89198.1; -; mRNA.
DR EMBL; AC091842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011699; AAH11699.2; ALT_INIT; mRNA.
DR EMBL; BC054506; AAH54506.2; ALT_INIT; mRNA.
DR CCDS; CCDS4351.2; -.
DR RefSeq; NP_114114.2; NM_031908.4.
DR AlphaFoldDB; Q9BXJ5; -.
DR SMR; Q9BXJ5; -.
DR BioGRID; 125389; 64.
DR IntAct; Q9BXJ5; 47.
DR STRING; 9606.ENSP00000377545; -.
DR iPTMnet; Q9BXJ5; -.
DR PhosphoSitePlus; Q9BXJ5; -.
DR BioMuta; C1QTNF2; -.
DR DMDM; 20177866; -.
DR MassIVE; Q9BXJ5; -.
DR PaxDb; Q9BXJ5; -.
DR PeptideAtlas; Q9BXJ5; -.
DR PRIDE; Q9BXJ5; -.
DR ProteomicsDB; 79439; -.
DR Antibodypedia; 16666; 256 antibodies from 31 providers.
DR DNASU; 114898; -.
DR Ensembl; ENST00000652664.2; ENSP00000498651.1; ENSG00000145861.9.
DR GeneID; 114898; -.
DR KEGG; hsa:114898; -.
DR MANE-Select; ENST00000652664.2; ENSP00000498651.1; NM_031908.6; NP_114114.3.
DR UCSC; uc003lyd.4; human.
DR CTD; 114898; -.
DR GeneCards; C1QTNF2; -.
DR HGNC; HGNC:14325; C1QTNF2.
DR HPA; ENSG00000145861; Low tissue specificity.
DR MIM; 618647; gene.
DR neXtProt; NX_Q9BXJ5; -.
DR OpenTargets; ENSG00000145861; -.
DR PharmGKB; PA25629; -.
DR VEuPathDB; HostDB:ENSG00000145861; -.
DR eggNOG; ENOG502QT1U; Eukaryota.
DR GeneTree; ENSGT00940000159591; -.
DR HOGENOM; CLU_001074_0_3_1; -.
DR InParanoid; Q9BXJ5; -.
DR OMA; AMIPWVL; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q9BXJ5; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q9BXJ5; -.
DR SignaLink; Q9BXJ5; -.
DR BioGRID-ORCS; 114898; 9 hits in 1062 CRISPR screens.
DR ChiTaRS; C1QTNF2; human.
DR GenomeRNAi; 114898; -.
DR Pharos; Q9BXJ5; Tbio.
DR PRO; PR:Q9BXJ5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BXJ5; protein.
DR Bgee; ENSG00000145861; Expressed in ascending aorta and 104 other tissues.
DR ExpressionAtlas; Q9BXJ5; baseline and differential.
DR Genevisible; Q9BXJ5; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
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 Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 2.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Collagen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..285
FT /note="Complement C1q tumor necrosis factor-related protein
FT 2"
FT /id="PRO_0000003530"
FT DOMAIN 40..141
FT /note="Collagen-like"
FT DOMAIN 145..281
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 33..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 29952 MW; 7E31FF9868D4EDFA CRC64;
MIPWVLLACA LPCAADPLLG AFARRDFRKG SPQLVCSLPG PQGPPGPPGA PGPSGMMGRM
GFPGKDGQDG HDGDRGDSGE EGPPGRTGNR GKPGPKGKAG AIGRAGPRGP KGVNGTPGKH
GTPGKKGPKG KKGEPGLPGP CSCGSGHTKS AFSVAVTKSY PRERLPIKFD KILMNEGGHY
NASSGKFVCG VPGIYYFTYD ITLANKHLAI GLVHNGQYRI RTFDANTGNH DVASGSTILA
LKQGDEVWLQ IFYSEQNGLF YDPYWTDSLF TGFLIYADQD DPNEV
