C1QT2_MOUSE
ID C1QT2_MOUSE Reviewed; 294 AA.
AC Q9D8U4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Complement C1q tumor necrosis factor-related protein 2;
DE Short=mCTRP2;
DE Flags: Precursor;
GN Name=C1qtnf2; Synonyms=Crtp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=15231994; DOI=10.1073/pnas.0403760101;
RA Wong G.W., Wang J., Hug C., Tsao T.S., Lodish H.F.;
RT "A family of Acrp30/adiponectin structural and functional paralogs.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10302-10307(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 INTERACTION WITH ERFE.
RX PubMed=22351773; DOI=10.1074/jbc.m111.336834;
RA Seldin M.M., Peterson J.M., Byerly M.S., Wei Z., Wong G.W.;
RT "Myonectin (CTRP15), a novel myokine that links skeletal muscle to systemic
RT lipid homeostasis.";
RL J. Biol. Chem. 287:11968-11980(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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:0000269|PubMed:31439668}.
CC -!- SUBUNIT: May interact with ERFE.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are born at the expected Mendelian
CC ratio and appear normal with no gross developmental abnormalities. A
CC reduction of body weight is observed in male, but not female, due to
CC increased metabolic rate and energy expenditure. CTRP2 deficiency up-
CC regulates the expression of lipolytic enzymes and protein kinase A
CC signaling, resulting in enhanced adipose tissue lipolysis. Knockout
CC mice also have altered hepatic and plasma lipid profiles. In contrast
CC to lipid metabolism, whole-body glucose metabolism is not affected.
CC {ECO:0000269|PubMed:31439668}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
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DR EMBL; DQ002395; AAY21927.1; -; mRNA.
DR EMBL; AK007683; BAB25187.1; -; mRNA.
DR EMBL; AL670472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030324; AAH30324.1; -; mRNA.
DR CCDS; CCDS24558.1; -.
DR RefSeq; NP_081255.1; NM_026979.5.
DR AlphaFoldDB; Q9D8U4; -.
DR SMR; Q9D8U4; -.
DR STRING; 10090.ENSMUSP00000051652; -.
DR iPTMnet; Q9D8U4; -.
DR PhosphoSitePlus; Q9D8U4; -.
DR MaxQB; Q9D8U4; -.
DR PaxDb; Q9D8U4; -.
DR PRIDE; Q9D8U4; -.
DR ProteomicsDB; 273728; -.
DR Antibodypedia; 16666; 256 antibodies from 31 providers.
DR DNASU; 69183; -.
DR Ensembl; ENSMUST00000057679; ENSMUSP00000051652; ENSMUSG00000046491.
DR GeneID; 69183; -.
DR KEGG; mmu:69183; -.
DR UCSC; uc007imr.2; mouse.
DR CTD; 114898; -.
DR MGI; MGI:1916433; C1qtnf2.
DR VEuPathDB; HostDB:ENSMUSG00000046491; -.
DR eggNOG; ENOG502QT1U; Eukaryota.
DR GeneTree; ENSGT00940000159591; -.
DR HOGENOM; CLU_001074_0_3_1; -.
DR InParanoid; Q9D8U4; -.
DR OMA; AMIPWVL; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q9D8U4; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 69183; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D8U4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D8U4; protein.
DR Bgee; ENSMUSG00000046491; Expressed in head bone and 147 other tissues.
DR ExpressionAtlas; Q9D8U4; baseline and differential.
DR Genevisible; Q9D8U4; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0046321; P:positive regulation of fatty acid oxidation; IDA:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; IDA:MGI.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP: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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..294
FT /note="Complement C1q tumor necrosis factor-related protein
FT 2"
FT /id="PRO_0000320083"
FT DOMAIN 48..150
FT /note="Collagen-like"
FT DOMAIN 154..290
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 42..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 30865 MW; 6D3905AE7C19E6FA CRC64;
MTIFKKVTTM ISWVLLACAL PCAADPMLGA FARRDFQKGG PQLVCSLPGP QGPPGPPGAP
GSSGVVGRMG FPGKDGQDGQ DGDRGDSGEE GPPGRTGNRG KQGPKGKAGA IGRAGPRGPK
GVSGTPGKHG TPGKKGPKGK KGEPGLPGPC SCGSSRAKSA FSVAVTKSYP RERLPIKFDK
ILMNEGGHYN ASSGKFVCSV PGIYYFTYDI TLANKHLAIG LVHNGQYRIR TFDANTGNHD
VASGSTILAL KEGDEVWLQI FYSEQNGLFY DPYWTDSLFT GFLIYADQGD PNEV
