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   27-MAR-2024, entry version 137.
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; 9606-ENSP00000298943; -.
DR   PeptideAtlas; 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; 95 antibodies from 20 providers.
DR   DNASU; 389941; -.
DR   Ensembl; ENST00000298943.4; ENSP00000298943.3; ENSG00000165985.11. [Q5VWW1-1]
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   AGR; HGNC:19359; -.
DR   CTD; 389941; -.
DR   DisGeNET; 389941; -.
DR   GeneCards; C1QL3; -.
DR   HGNC; HGNC:19359; C1QL3.
DR   HPA; ENSG00000165985; Group enriched (brain, retina).
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; GYEMLKF; -.
DR   OrthoDB; 4210331at2759; -.
DR   PhylomeDB; Q5VWW1; -.
DR   TreeFam; TF329591; -.
DR   PathwayCommons; Q5VWW1; -.
DR   SignaLink; Q5VWW1; -.
DR   BioGRID-ORCS; 389941; 7 hits in 1139 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 cell types or tissues.
DR   ExpressionAtlas; Q5VWW1; baseline and differential.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0097107; P:postsynaptic density assembly; 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   PANTHER; PTHR22923; CEREBELLIN-RELATED; 1.
DR   PANTHER; PTHR22923:SF96; COMPLEMENT C1Q-LIKE PROTEIN 3; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 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
//