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 24-JAN-2024, entry version 171. 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; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-2817707, EBI-8643161; 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CCDS4351.3; -. DR RefSeq; NP_114114.2; NM_031908.4. DR AlphaFoldDB; Q9BXJ5; -. DR SMR; Q9BXJ5; -. DR BioGRID; 125389; 65. 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; 9606-ENSP00000377545; -. DR PeptideAtlas; Q9BXJ5; -. DR ProteomicsDB; 79439; -. DR Antibodypedia; 16666; 272 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 AGR; HGNC:14325; -. 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; MPGPCSC; -. DR OrthoDB; 3013859at2759; -. DR PhylomeDB; Q9BXJ5; -. DR TreeFam; TF329591; -. DR PathwayCommons; Q9BXJ5; -. DR SignaLink; Q9BXJ5; -. DR BioGRID-ORCS; 114898; 10 hits in 1141 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 106 other cell types or tissues. DR ExpressionAtlas; Q9BXJ5; baseline and differential. 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 PANTHER; PTHR15427:SF28; COMPLEMENT C1Q TUMOR NECROSIS FACTOR-RELATED PROTEIN 2; 1. DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1. DR Pfam; PF00386; C1q; 1. DR Pfam; PF01391; Collagen; 2. DR PRINTS; PR00007; COMPLEMNTC1Q. DR SMART; SM00110; C1Q; 1. DR SUPFAM; SSF49842; TNF-like; 1. DR PROSITE; PS50871; C1Q; 1. DR Genevisible; Q9BXJ5; HS. 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 //