C1QL4_MOUSE
ID C1QL4_MOUSE Reviewed; 238 AA.
AC Q4ZJM9; B2RV40;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Complement C1q-like protein 4;
DE AltName: Full=C1q and tumor necrosis factor-related protein 11;
DE Short=C1q/TNF-related protein 11;
DE Short=C1qTNF11;
DE Short=CTRP11;
DE Flags: Precursor;
GN Name=C1ql4; Synonyms=C1qtnf11, Ctrp11;
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], FUNCTION IN ADIPOGENESIS, HOMOOLIGOMERIZATION,
RP INTERACTION WITH C1QL1; C1QL2 AND C1QL3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND MUTAGENESIS OF CYS-28 AND CYS-32.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 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).
CC -!- FUNCTION: May regulate the number of excitatory synapses that are
CC formed on hippocampus neurons. Has no effect on inhibitory synapses.
CC May inhibit adipocyte differentiation at an early stage of the process.
CC {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:23449976}.
CC -!- SUBUNIT: Forms homooligomers, predominantly dimers or trimers. Forms
CC heterooligomers with C1QL1, C1QL2 and C1QL3, when proteins are
CC coexpressed; this interaction does not occur after secretion
CC (PubMed:23449976). Interacts with ADGRB3 (PubMed:21262840).
CC {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:23449976}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23449976}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and adipose tissue,
CC brown adipose tissue expressing higher levels than subcutaneous and
CC visceral white adipose tissue. In gonadal fat pad, expressed at lower
CC levels in adipocytes than in the stromal vascular fraction (VSP), which
CC contains preadipocytes, fibroblasts, endothelial cells and occasional
CC immune cells. Expression exhibits sexually dimorphism, with higher
CC levels in females than in males. {ECO:0000269|PubMed:23449976}.
CC -!- INDUCTION: Down-regulated in fasted animals.
CC {ECO:0000269|PubMed:23449976}.
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DR EMBL; DQ002403; AAY21935.1; -; mRNA.
DR EMBL; CH466550; EDL04144.1; -; Genomic_DNA.
DR EMBL; BC147036; AAI47037.1; -; mRNA.
DR EMBL; BC147037; AAI47038.1; -; mRNA.
DR CCDS; CCDS27814.1; -.
DR RefSeq; NP_001019873.1; NM_001024702.1.
DR RefSeq; XP_006521038.1; XM_006520975.2.
DR AlphaFoldDB; Q4ZJM9; -.
DR SMR; Q4ZJM9; -.
DR BioGRID; 232112; 1.
DR STRING; 10090.ENSMUSP00000068402; -.
DR PhosphoSitePlus; Q4ZJM9; -.
DR PaxDb; Q4ZJM9; -.
DR PRIDE; Q4ZJM9; -.
DR ProteomicsDB; 273853; -.
DR Antibodypedia; 66308; 69 antibodies from 15 providers.
DR DNASU; 239659; -.
DR Ensembl; ENSMUST00000064462; ENSMUSP00000068402; ENSMUSG00000001076.
DR GeneID; 239659; -.
DR KEGG; mmu:239659; -.
DR UCSC; uc007xot.1; mouse.
DR CTD; 338761; -.
DR MGI; MGI:3579909; C1ql4.
DR VEuPathDB; HostDB:ENSMUSG00000001076; -.
DR eggNOG; ENOG502QSVI; Eukaryota.
DR GeneTree; ENSGT00940000155969; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; Q4ZJM9; -.
DR OMA; GPTHYEM; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; Q4ZJM9; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 239659; 6 hits in 74 CRISPR screens.
DR PRO; PR:Q4ZJM9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q4ZJM9; protein.
DR Bgee; ENSMUSG00000001076; Expressed in embryonic brain and 22 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IDA:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; 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 Collagen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..238
FT /note="Complement C1q-like protein 4"
FT /id="PRO_0000274339"
FT DOMAIN 53..96
FT /note="Collagen-like"
FT DOMAIN 105..238
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 37..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 28
FT /note="C->A: Does not affect homo-, nor
FT heterooligomerization with C1QL1, C1QL2 and C1QL3; when
FT associated with A-32. Increased secretion; when associated
FT with A-32. Does not impair inhibition of adipocyte
FT differentiation; when associated with A-32."
FT /evidence="ECO:0000269|PubMed:23449976"
FT MUTAGEN 32
FT /note="C->A: Does not affect homo-, nor
FT heterooligomerization with C1QL1, C1QL2 and C1QL3; when
FT associated with A-28. Increased secretion; when associated
FT with A-28. Does not impair inhibition of adipocyte
FT differentiation; when associated with A-28."
FT /evidence="ECO:0000269|PubMed:23449976"
SQ SEQUENCE 238 AA; 24928 MW; 72E7F6853E572056 CRC64;
MVLLLLVAIP LLVHSSRGPT HYEMLGRCRM VCDPHASRGQ GPDGAPASVP SLPPGAKGEV
GRRGKAGLRG PPGPPGPRGP PGEPGRPGPP GPPGPGPGGA APPAGYVPRI AFYAGLRRPH
EGYEVLRFDD VVTNVGNAYE AASGKFTCPM PGVYFFAYHV LMRGGDGTSM WADLMKNGQV
RASAIAQDAD QNYDYASNSV ILHLDVGDEV FIKLDGGKVH GGNTNKYSTF SGFIIYPD
