C1QL3_HUMAN
ID C1QL3_HUMAN Reviewed; 255 AA.
AC Q5VWW1; A0PJY4; A0PJY5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Complement C1q-like protein 3;
DE AltName: Full=C1q and tumor necrosis factor-related protein 13;
DE Short=C1q/TNF-related protein 13;
DE Flags: Precursor;
GN Name=C1QL3; Synonyms=CTRP13;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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=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).
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). Plays a role in glucose homeostasis. Via AMPK signaling
CC pathway, stimulates glucose uptake in adipocytes, myotubes and
CC hepatocytes and enhances insulin-stimulated glucose uptake. In a
CC hepatoma cell line, reduces the expression of gluconeogenic enzymes
CC G6PC1 and PCK1 and hence decreases de novo glucose production (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with ADGRB3. Interacts with
CC C1QL2 and C1QL4, when proteins are coexpressed; this interaction does
CC not occur after secretion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5VWW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VWW1-2; Sequence=VSP_027130;
CC Name=3;
CC IsoId=Q5VWW1-3; Sequence=VSP_027130, VSP_027131;
CC -!- TISSUE SPECIFICITY: Highly expressed in adipose tissue, with expression
CC levels at least 2 orders of magnitude higher than in other tissues,
CC including brain and kidney. {ECO:0000269|PubMed:21378161}.
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DR EMBL; AL353576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127716; AAI27717.1; -; mRNA.
DR EMBL; BC127717; AAI27718.1; -; mRNA.
DR CCDS; CCDS31156.1; -. [Q5VWW1-1]
DR RefSeq; NP_001010908.1; NM_001010908.1. [Q5VWW1-1]
DR AlphaFoldDB; Q5VWW1; -.
DR SMR; Q5VWW1; -.
DR BioGRID; 133333; 11.
DR STRING; 9606.ENSP00000298943; -.
DR iPTMnet; Q5VWW1; -.
DR PhosphoSitePlus; Q5VWW1; -.
DR BioMuta; C1QL3; -.
DR DMDM; 74747449; -.
DR MassIVE; Q5VWW1; -.
DR PaxDb; Q5VWW1; -.
DR PeptideAtlas; Q5VWW1; -.
DR PRIDE; Q5VWW1; -.
DR ProteomicsDB; 65563; -. [Q5VWW1-1]
DR ProteomicsDB; 65564; -. [Q5VWW1-2]
DR ProteomicsDB; 65565; -. [Q5VWW1-3]
DR TopDownProteomics; Q5VWW1-3; -. [Q5VWW1-3]
DR Antibodypedia; 56786; 80 antibodies from 20 providers.
DR DNASU; 389941; -.
DR Ensembl; ENST00000298943.4; ENSP00000298943.3; ENSG00000165985.10. [Q5VWW1-1]
DR Ensembl; ENST00000619991.1; ENSP00000480149.1; ENSG00000165985.10. [Q5VWW1-3]
DR GeneID; 389941; -.
DR KEGG; hsa:389941; -.
DR MANE-Select; ENST00000298943.4; ENSP00000298943.3; NM_001010908.2; NP_001010908.1.
DR UCSC; uc001ioj.1; human. [Q5VWW1-1]
DR CTD; 389941; -.
DR DisGeNET; 389941; -.
DR GeneCards; C1QL3; -.
DR HGNC; HGNC:19359; C1QL3.
DR HPA; ENSG00000165985; Tissue enriched (brain).
DR MIM; 615227; gene.
DR neXtProt; NX_Q5VWW1; -.
DR OpenTargets; ENSG00000165985; -.
DR PharmGKB; PA134891919; -.
DR VEuPathDB; HostDB:ENSG00000165985; -.
DR eggNOG; ENOG502QSKV; Eukaryota.
DR GeneTree; ENSGT00940000161639; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; Q5VWW1; -.
DR OMA; CDPYGTR; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; Q5VWW1; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q5VWW1; -.
DR SignaLink; Q5VWW1; -.
DR BioGRID-ORCS; 389941; 7 hits in 1061 CRISPR screens.
DR GenomeRNAi; 389941; -.
DR Pharos; Q5VWW1; Tbio.
DR PRO; PR:Q5VWW1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VWW1; protein.
DR Bgee; ENSG00000165985; Expressed in superior frontal gyrus and 93 other tissues.
DR ExpressionAtlas; Q5VWW1; 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:0050807; P:regulation of synapse organization; IEA:Ensembl.
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; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..255
FT /note="Complement C1q-like protein 3"
FT /id="PRO_0000274337"
FT DOMAIN 61..111
FT /note="Collagen-like"
FT DOMAIN 122..255
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 39..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 63..86
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027130"
FT VAR_SEQ 87..104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027131"
SQ SEQUENCE 255 AA; 26719 MW; AEF2004E14DE07AC CRC64;
MVLLLVILIP VLVSSAGTSA HYEMLGTCRM VCDPYGGTKA PSTAATPDRG LMQSLPTFIQ
GPKGEAGRPG KAGPRGPPGE PGPPGPMGPP GEKGEPGRQG LPGPPGAPGL NAAGAISAAT
YSTVPKIAFY AGLKRQHEGY EVLKFDDVVT NLGNHYDPTT GKFTCSIPGI YFFTYHVLMR
GGDGTSMWAD LCKNNQVRAS AIAQDADQNY DYASNSVVLH LEPGDEVYIK LDGGKAHGGN
NNKYSTFSGF IIYAD
