C1QL2_MOUSE
ID C1QL2_MOUSE Reviewed; 287 AA.
AC Q8CFR0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Complement C1q-like protein 2;
DE AltName: Full=C1q and tumor necrosis factor-related protein 10;
DE Short=C1q/TNF-related protein 10;
DE Short=C1qTNF10;
DE Short=CTRP10;
DE Flags: Precursor;
GN Name=C1ql2; Synonyms=C1qtnf10, Ctrp10;
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], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND MUTAGENESIS OF CYS-29 AND CYS-33.
RC STRAIN=C57BL/6J;
RX PubMed=18783346; DOI=10.1042/bj20081240;
RA Wong G.W., Krawczyk S.A., Kitidis-Mitrokostas C., Revett T., Gimeno R.,
RA Lodish H.F.;
RT "Molecular, biochemical and functional characterizations of C1q/TNF family
RT members: adipose-tissue-selective expression patterns, regulation by PPAR-
RT gamma agonist, cysteine-mediated oligomerizations, combinatorial
RT associations and metabolic functions.";
RL Biochem. J. 416:161-177(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 MRNA].
RC TISSUE=Eye;
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 [4]
RP INTERACTION WITH C1QL3.
RX PubMed=21378161; DOI=10.1074/jbc.m110.201087;
RA Wei Z., Peterson J.M., Wong G.W.;
RT "Metabolic regulation by C1q/TNF-related protein-13 (CTRP13): activation OF
RT AMP-activated protein kinase and suppression of fatty acid-induced JNK
RT signaling.";
RL J. Biol. Chem. 286:15652-15665(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH ADGRB3.
RX PubMed=21262840; DOI=10.1073/pnas.1019577108;
RA Bolliger M.F., Martinelli D.C., Sudhof T.C.;
RT "The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity
RT receptor for C1q-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2534-2539(2011).
RN [6]
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 [7]
RP INTERACTION WITH C1QL4, AND MUTAGENESIS OF CYS-29 AND CYS-33.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=23449976; DOI=10.1074/jbc.m113.458711;
RA Wei Z., Seldin M.M., Natarajan N., Djemal D.C., Peterson J.M., Wong G.W.;
RT "C1q/tumor necrosis factor-related protein 11 (CTRP11), a novel adipose
RT stroma-derived regulator of adipogenesis.";
RL J. Biol. Chem. 288:10214-10229(2013).
CC -!- FUNCTION: May regulate the number of excitatory synapses that are
CC formed on hippocampus neurons. Has no effect on inhibitory synapses.
CC {ECO:0000269|PubMed:21262840}.
CC -!- SUBUNIT: Forms homotrimers which can further assemble to form higher-
CC order oligomeric complexes. Interacts with ADGRB3. May interact with
CC ERFE. Forms heterooligomers with C1QL3 and C1QL4, when proteins are
CC coexpressed; this interaction does not occur after secretion.
CC {ECO:0000269|PubMed:18783346, ECO:0000269|PubMed:21262840,
CC ECO:0000269|PubMed:21378161, ECO:0000269|PubMed:22351773,
CC ECO:0000269|PubMed:23449976}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18783346}.
CC -!- TISSUE SPECIFICITY: Highest expression in eye, followed by placenta and
CC brain, intermediate expression in adipose tissue and lowest expression
CC in lymph node and testis. {ECO:0000269|PubMed:18783346}.
CC -!- PTM: Glycosylated, but not with N-linked glycans.
CC {ECO:0000269|PubMed:18783346}.
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; DQ002402; AAY21934.1; -; mRNA.
DR EMBL; AK144471; BAE25906.1; -; mRNA.
DR EMBL; BC040774; AAH40774.1; -; mRNA.
DR CCDS; CCDS15233.1; -.
DR RefSeq; NP_997116.1; NM_207233.1.
DR PDB; 4QPY; X-ray; 2.38 A; A/B/C=152-287.
DR PDBsum; 4QPY; -.
DR AlphaFoldDB; Q8CFR0; -.
DR SMR; Q8CFR0; -.
DR DIP; DIP-59698N; -.
DR IntAct; Q8CFR0; 2.
DR STRING; 10090.ENSMUSP00000037257; -.
DR MaxQB; Q8CFR0; -.
DR PaxDb; Q8CFR0; -.
DR PeptideAtlas; Q8CFR0; -.
DR PRIDE; Q8CFR0; -.
DR ProteomicsDB; 273804; -.
DR Antibodypedia; 58204; 105 antibodies from 21 providers.
DR DNASU; 226359; -.
DR Ensembl; ENSMUST00000037286; ENSMUSP00000037257; ENSMUSG00000036907.
DR GeneID; 226359; -.
DR KEGG; mmu:226359; -.
DR UCSC; uc007cjk.1; mouse.
DR CTD; 165257; -.
DR MGI; MGI:3032521; C1ql2.
DR VEuPathDB; HostDB:ENSMUSG00000036907; -.
DR eggNOG; ENOG502QUZ7; Eukaryota.
DR GeneTree; ENSGT00940000156913; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; Q8CFR0; -.
DR OMA; TGAHYEM; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; Q8CFR0; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 226359; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8CFR0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CFR0; protein.
DR Bgee; ENSMUSG00000036907; Expressed in dentate gyrus of hippocampal formation granule cell and 43 other tissues.
DR ExpressionAtlas; Q8CFR0; baseline and differential.
DR Genevisible; Q8CFR0; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
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 3D-structure; Collagen; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..287
FT /note="Complement C1q-like protein 2"
FT /id="PRO_0000274336"
FT DOMAIN 76..118
FT /note="Collagen-like"
FT DOMAIN 154..287
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 65..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 29
FT /note="C->A: No effect on homotrimer formation, but loss of
FT higher-order oligomeric complexes; when associated with A-
FT 33. Does not affect heterooligomerization with C1QL4; when
FT associated with A-33."
FT /evidence="ECO:0000269|PubMed:18783346,
FT ECO:0000269|PubMed:23449976"
FT MUTAGEN 33
FT /note="C->A: No effect on homotrimer formation, but loss of
FT higher-order oligomeric complexes; when associated with A-
FT 29. Does not affect heterooligomerization with C1QL4; when
FT associated with A-29."
FT /evidence="ECO:0000269|PubMed:18783346,
FT ECO:0000269|PubMed:23449976"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4QPY"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 201..212
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4QPY"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:4QPY"
SQ SEQUENCE 287 AA; 29292 MW; 8FF89EC1C7420415 CRC64;
MALGLLIAVP LLLQAAPPGA AHYEMLGTCR MICDPYSVAP AGGPAGAKAP PPGPSTAALE
VMQDLSANPP PPFIQGPKGD PGRPGKPGPR GPPGEPGPPG PRGPPGEKGD SGRPGLPGLQ
LTTSAAGGVG VVSGGTGGGG DTEGEVTSAL SAAFSGPKIA FYVGLKSPHE GYEVLKFDDV
VTNLGNHYDP TTGKFSCQVR GIYFFTYHIL MRGGDGTSMW ADLCKNGQVR ASAIAQDADQ
NYDYASNSVV LHLDSGDEVY VKLDGGKAHG GNNNKYSTFS GFLLYPD
