C1QL3_MOUSE
ID C1QL3_MOUSE Reviewed; 255 AA.
AC Q9ESN4; A2AUR9; B0LXL6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Short=CTRP13;
DE AltName: Full=Gliacolin;
DE Flags: Precursor;
GN Name=C1ql3; Synonyms=C1ql, Ctrp13;
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].
RX PubMed=10862616; DOI=10.1074/jbc.m003026200;
RA Koide T., Aso A., Yorihuzi T., Nagata K.;
RT "Conformational requirements of collagenous peptides for recognition by the
RT chaperone protein HSP47.";
RL J. Biol. Chem. 275:27957-27963(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH
RP C1QL2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS
RP OF CYS-28 AND CYS-32.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Watanabe Y., Yorihuzi T., Yamazaki Y., Kubota H., Hosokawa N., Nagata K.;
RT "Molecular cloning of a new mouse C1q-like gene expressed in glia.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [7]
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 [8]
RP INTERACTION WITH C1QL4, 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).
CC -!- FUNCTION: May regulate the number of excitatory synapses that are
CC formed on hippocampus neurons. Has no effect on inhibitory synapses.
CC Plays a role in glucose homeostasis. Via AMPK signaling pathway,
CC stimulates glucose uptake in adipocytes, myotubes and hepatocytes and
CC enhances insulin-stimulated glucose uptake. In a hepatoma cell line,
CC reduces the expression of gluconeogenic enzymes G6PC1 and PCK1 and
CC hence decreases de novo glucose production.
CC {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:21378161}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with ADGRB3 (PubMed:21262840).
CC Forms heterooligomers with C1QL2 and C1QL4, when proteins are
CC coexpressed; this interaction does not occur after secretion.
CC {ECO:0000269|PubMed:21262840, ECO:0000269|PubMed:21378161,
CC ECO:0000269|PubMed:23449976}.
CC -!- INTERACTION:
CC Q9ESN4; Q9ESN4: C1ql3; NbExp=3; IntAct=EBI-15907894, EBI-15907894;
CC Q9ESN4; O60242: ADGRB3; Xeno; NbExp=4; IntAct=EBI-15907894, EBI-2682765;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21378161}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and white adipose tissue.
CC In gonadal fat pad, expressed at lower levels in adipocytes than in the
CC stromal vascular fraction (VSP), which contains preadipocytes,
CC fibroblasts, endothelial cells and occasional immune cells. Expression
CC exhibits sexually dimorphism, with higher levels in females than in
CC males (at protein level). Tends to be up-regulated in adipose tissue
CC from obese males, but not females. Expressed in glial cells.
CC {ECO:0000269|PubMed:21378161}.
CC -!- INDUCTION: In adipocytes, up-regulated by rosiglitazone, an insulin-
CC sensitizing drug. {ECO:0000269|PubMed:21378161}.
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DR EMBL; AB044560; BAB15806.1; -; mRNA.
DR EMBL; EU399230; ABY86415.1; -; mRNA.
DR EMBL; AB045983; BAB59006.1; -; Genomic_DNA.
DR EMBL; AL929209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08047.1; -; Genomic_DNA.
DR EMBL; BC024634; AAH24634.1; -; mRNA.
DR CCDS; CCDS15692.1; -.
DR RefSeq; NP_694795.1; NM_153155.2.
DR PDB; 4QQH; X-ray; 1.20 A; A=119-255.
DR PDB; 4QQL; X-ray; 2.39 A; A/B/C/D/E/F/G/H/I=119-255.
DR PDB; 4QQO; X-ray; 2.03 A; A=119-255.
DR PDB; 4QQP; X-ray; 1.46 A; A=119-255.
DR PDB; 5YBZ; X-ray; 1.71 A; A/C/D=125-255.
DR PDBsum; 4QQH; -.
DR PDBsum; 4QQL; -.
DR PDBsum; 4QQO; -.
DR PDBsum; 4QQP; -.
DR PDBsum; 5YBZ; -.
DR AlphaFoldDB; Q9ESN4; -.
DR SMR; Q9ESN4; -.
DR DIP; DIP-59699N; -.
DR IntAct; Q9ESN4; 1.
DR STRING; 10090.ENSMUSP00000056188; -.
DR PhosphoSitePlus; Q9ESN4; -.
DR MaxQB; Q9ESN4; -.
DR PaxDb; Q9ESN4; -.
DR PeptideAtlas; Q9ESN4; -.
DR PRIDE; Q9ESN4; -.
DR ProteomicsDB; 273726; -.
DR Antibodypedia; 56786; 80 antibodies from 20 providers.
DR DNASU; 227580; -.
DR Ensembl; ENSMUST00000061545; ENSMUSP00000056188; ENSMUSG00000049630.
DR GeneID; 227580; -.
DR KEGG; mmu:227580; -.
DR UCSC; uc008ijv.1; mouse.
DR CTD; 389941; -.
DR MGI; MGI:2387350; C1ql3.
DR VEuPathDB; HostDB:ENSMUSG00000049630; -.
DR eggNOG; ENOG502QSKV; Eukaryota.
DR GeneTree; ENSGT00940000161639; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; Q9ESN4; -.
DR OMA; CDPYGTR; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; Q9ESN4; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 227580; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9ESN4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ESN4; protein.
DR Bgee; ENSMUSG00000049630; Expressed in dentate gyrus of hippocampal formation granule cell and 89 other tissues.
DR ExpressionAtlas; Q9ESN4; baseline and differential.
DR Genevisible; Q9ESN4; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:MGI.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000003542"
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 MUTAGEN 28
FT /note="C->A: Does not affect heterooligomerization with
FT C1QL4; when associated with A-32."
FT /evidence="ECO:0000269|PubMed:21378161,
FT ECO:0000269|PubMed:23449976"
FT MUTAGEN 28
FT /note="C->S: Does not affect heterooligomerization with
FT C1QL2; when associated with S-32."
FT /evidence="ECO:0000269|PubMed:21378161,
FT ECO:0000269|PubMed:23449976"
FT MUTAGEN 32
FT /note="C->A: Does not affect heterooligomerization with
FT C1QL4; when associated with A-28."
FT /evidence="ECO:0000269|PubMed:21378161,
FT ECO:0000269|PubMed:23449976"
FT MUTAGEN 32
FT /note="C->S: Does not affect heterooligomerization with
FT C1QL2; when associated with S-28."
FT /evidence="ECO:0000269|PubMed:21378161,
FT ECO:0000269|PubMed:23449976"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4QQH"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4QQL"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 226..236
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4QQH"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:4QQH"
SQ SEQUENCE 255 AA; 26687 MW; 529FBAF4B2191BC1 CRC64;
MVLLLVILIP VLVSSAGTSA HYEMLGTCRM VCDPYGGTKA PSTAATPDRG LMQSLPTFIQ
GPKGEAGRPG KAGPRGPPGE PGPPGPVGPP GEKGEPGRQG LPGPPGAPGL NAAGAISAAT
YSTVPKIAFY AGLKRQHEGY EVLKFDDVVT NLGNHYDPTT GKFTCSIPGI YFFTYHVLMR
GGDGTSMWAD LCKNNQVRAS AIAQDADQNY DYASNSVVLH LEPGDEVYIK LDGGKAHGGN
NNKYSTFSGF IIYAD
