C1QL4_HUMAN
ID C1QL4_HUMAN Reviewed; 238 AA.
AC Q86Z23;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Flags: Precursor;
GN Name=C1QL4; Synonyms=CTRP11;
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 Kim N.-S., Shon H.-Y., Oh J.-H., Lee J.-Y., Kim J.-M., Hahn Y., Kim Y.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
RP TISSUE SPECIFICITY.
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 (By
CC similarity). May inhibit adipocyte differentiation at an early stage of
CC the process (By similarity). {ECO:0000250}.
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. Interacts
CC with ADGRB3. {ECO:0000250|UniProtKB:Q4ZJM9}.
CC -!- INTERACTION:
CC Q86Z23; P19397: CD53; NbExp=3; IntAct=EBI-12062109, EBI-6657396;
CC Q86Z23; Q9HA82: CERS4; NbExp=3; IntAct=EBI-12062109, EBI-2622997;
CC Q86Z23; Q969F0: FATE1; NbExp=3; IntAct=EBI-12062109, EBI-743099;
CC Q86Z23; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12062109, EBI-12142257;
CC Q86Z23; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-12062109, EBI-712073;
CC Q86Z23; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12062109, EBI-13345167;
CC Q86Z23; Q13651: IL10RA; NbExp=3; IntAct=EBI-12062109, EBI-1031656;
CC Q86Z23; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12062109, EBI-17490413;
CC Q86Z23; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12062109, EBI-11956541;
CC Q86Z23; Q9UBD6: RHCG; NbExp=3; IntAct=EBI-12062109, EBI-15853497;
CC Q86Z23; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-12062109, EBI-12823227;
CC Q86Z23; O43765: SGTA; NbExp=3; IntAct=EBI-12062109, EBI-347996;
CC Q86Z23; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12062109, EBI-744081;
CC Q86Z23; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-12062109, EBI-9978441;
CC Q86Z23; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12062109, EBI-17280858;
CC Q86Z23; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12062109, EBI-11724423;
CC Q86Z23; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12062109, EBI-12345267;
CC Q86Z23; P34981: TRHR; NbExp=3; IntAct=EBI-12062109, EBI-18055230;
CC Q86Z23; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12062109, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest expression levels in testis and adipose
CC tissue, lower levels in skeletal muscle and kidney.
CC {ECO:0000269|PubMed:23449976}.
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DR EMBL; AF466366; AAO33387.1; -; mRNA.
DR EMBL; BC110812; AAI10813.1; -; mRNA.
DR CCDS; CCDS31793.1; -.
DR RefSeq; NP_001008224.1; NM_001008223.1.
DR AlphaFoldDB; Q86Z23; -.
DR SMR; Q86Z23; -.
DR BioGRID; 130794; 91.
DR IntAct; Q86Z23; 48.
DR STRING; 9606.ENSP00000335285; -.
DR iPTMnet; Q86Z23; -.
DR PhosphoSitePlus; Q86Z23; -.
DR BioMuta; C1QL4; -.
DR DMDM; 74759547; -.
DR MassIVE; Q86Z23; -.
DR PaxDb; Q86Z23; -.
DR PeptideAtlas; Q86Z23; -.
DR PRIDE; Q86Z23; -.
DR ProteomicsDB; 70499; -.
DR Antibodypedia; 66308; 69 antibodies from 15 providers.
DR DNASU; 338761; -.
DR Ensembl; ENST00000334221.5; ENSP00000335285.3; ENSG00000186897.5.
DR GeneID; 338761; -.
DR KEGG; hsa:338761; -.
DR MANE-Select; ENST00000334221.5; ENSP00000335285.3; NM_001008223.2; NP_001008224.1.
DR UCSC; uc001rtz.2; human.
DR CTD; 338761; -.
DR DisGeNET; 338761; -.
DR GeneCards; C1QL4; -.
DR HGNC; HGNC:31416; C1QL4.
DR HPA; ENSG00000186897; Group enriched (brain, testis).
DR MIM; 615229; gene.
DR neXtProt; NX_Q86Z23; -.
DR OpenTargets; ENSG00000186897; -.
DR PharmGKB; PA142672536; -.
DR VEuPathDB; HostDB:ENSG00000186897; -.
DR eggNOG; ENOG502QSVI; Eukaryota.
DR GeneTree; ENSGT00940000155969; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; Q86Z23; -.
DR OMA; GPTHYEM; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; Q86Z23; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q86Z23; -.
DR SignaLink; Q86Z23; -.
DR BioGRID-ORCS; 338761; 4 hits in 1066 CRISPR screens.
DR GenomeRNAi; 338761; -.
DR Pharos; Q86Z23; Tdark.
DR PRO; PR:Q86Z23; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86Z23; protein.
DR Bgee; ENSG00000186897; Expressed in calcaneal tendon and 37 other tissues.
DR ExpressionAtlas; Q86Z23; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
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_0000274338"
FT DOMAIN 53..96
FT /note="Collagen-like"
FT DOMAIN 105..238
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 36..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 24909 MW; D89BD2793555AEF3 CRC64;
MVLLLLVAIP LLVHSSRGPA HYEMLGRCRM VCDPHGPRGP GPDGAPASVP PFPPGAKGEV
GRRGKAGLRG PPGPPGPRGP PGEPGRPGPP GPPGPGPGGV APAAGYVPRI AFYAGLRRPH
EGYEVLRFDD VVTNVGNAYE AASGKFTCPM PGVYFFAYHV LMRGGDGTSM WADLMKNGQV
RASAIAQDAD QNYDYASNSV ILHLDVGDEV FIKLDGGKVH GGNTNKYSTF SGFIIYPD
