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Complement C1q-like protein 3 (C1q and tumor necrosis factor-related protein 13) (C1q/TNF-related protein 13) (CTRP13) (Gliacolin)

 C1QL3_MOUSE             Reviewed;         255 AA.
Q9ESN4; A2AUR9; B0LXL6;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 123.
RecName: Full=Complement C1q-like protein 3;
AltName: Full=C1q and tumor necrosis factor-related protein 13;
Short=C1q/TNF-related protein 13;
Short=CTRP13;
AltName: Full=Gliacolin;
Flags: Precursor;
Name=C1ql3; Synonyms=C1ql, Ctrp13;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10862616; DOI=10.1074/jbc.M003026200;
Koide T., Aso A., Yorihuzi T., Nagata K.;
"Conformational requirements of collagenous peptides for recognition
by the chaperone protein HSP47.";
J. Biol. Chem. 275:27957-27963(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMOOLIGOMERIZATION, INTERACTION
WITH C1QL2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
MUTAGENESIS OF CYS-28 AND CYS-32.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=21378161; DOI=10.1074/jbc.M110.201087;
Wei Z., Peterson J.M., Wong G.W.;
"Metabolic regulation by C1q/TNF-related protein-13 (CTRP13):
activation OF AMP-activated protein kinase and suppression of fatty
acid-induced JNK signaling.";
J. Biol. Chem. 286:15652-15665(2011).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Watanabe Y., Yorihuzi T., Yamazaki Y., Kubota H., Hosokawa N.,
Nagata K.;
"Molecular cloning of a new mouse C1q-like gene expressed in glia.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND INTERACTION WITH ADGRB3.
PubMed=21262840; DOI=10.1073/pnas.1019577108;
Bolliger M.F., Martinelli D.C., Sudhof T.C.;
"The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity
receptor for C1q-like proteins.";
Proc. Natl. Acad. Sci. U.S.A. 108:2534-2539(2011).
[8]
INTERACTION WITH C1QL4, AND MUTAGENESIS OF CYS-28 AND CYS-32.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=23449976; DOI=10.1074/jbc.M113.458711;
Wei Z., Seldin M.M., Natarajan N., Djemal D.C., Peterson J.M.,
Wong G.W.;
"C1q/tumor necrosis factor-related protein 11 (CTRP11), a novel
adipose stroma-derived regulator of adipogenesis.";
J. Biol. Chem. 288:10214-10229(2013).
-!- FUNCTION: May regulate the number of excitatory synapses that are
formed on hippocampus neurons. Has no effect on inhibitory
synapses. Plays a role in glucose homeostasis. Via AMPK signaling
pathway, stimulates glucose uptake in adipocytes, myotubes and
hepatocytes and enhances insulin-stimulated glucose uptake. In a
hepatoma cell line, reduces the expression of gluconeogenic
enzymes G6PC and PCK1 and hence decreases de novo glucose
production. {ECO:0000269|PubMed:21262840,
ECO:0000269|PubMed:21378161}.
-!- SUBUNIT: Forms homooligomers. Interacts with ADGRB3
(PubMed:21262840). Forms heterooligomers with C1QL2 and C1QL4,
when proteins are coexpressed; this interaction does not occur
after secretion. {ECO:0000269|PubMed:21262840,
ECO:0000269|PubMed:21378161, ECO:0000269|PubMed:23449976}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-15907894, EBI-15907894;
O60242:ADGRB3 (xeno); NbExp=4; IntAct=EBI-15907894, EBI-2682765;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21378161}.
-!- TISSUE SPECIFICITY: Highly expressed in brain and white adipose
tissue. In gonadal fat pad, expressed at lower levels in
adipocytes than in the stromal vascular fraction (VSP), which
contains preadipocytes, fibroblasts, endothelial cells and
occasional immune cells. Expression exhibits sexually dimorphism,
with higher levels in females than in males (at protein level).
Tends to be up-regulated in adipose tissue from obese males, but
not females. Expressed in glial cells.
{ECO:0000269|PubMed:21378161}.
-!- INDUCTION: In adipocytes, up-regulated by rosiglitazone, an
insulin-sensitizing drug. {ECO:0000269|PubMed:21378161}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB044560; BAB15806.1; -; mRNA.
EMBL; EU399230; ABY86415.1; -; mRNA.
EMBL; AB045983; BAB59006.1; -; Genomic_DNA.
EMBL; AL929209; CAM23728.1; -; Genomic_DNA.
EMBL; CH466542; EDL08047.1; -; Genomic_DNA.
EMBL; BC024634; AAH24634.1; -; mRNA.
CCDS; CCDS15692.1; -.
RefSeq; NP_694795.1; NM_153155.2.
UniGene; Mm.229322; -.
UniGene; Mm.477072; -.
PDB; 4QQH; X-ray; 1.20 A; A=119-255.
PDB; 4QQL; X-ray; 2.39 A; A/B/C/D/E/F/G/H/I=119-255.
PDB; 4QQO; X-ray; 2.03 A; A=119-255.
PDB; 4QQP; X-ray; 1.46 A; A=119-255.
PDB; 5YBZ; X-ray; 1.71 A; A/C/D=125-255.
PDBsum; 4QQH; -.
PDBsum; 4QQL; -.
PDBsum; 4QQO; -.
PDBsum; 4QQP; -.
PDBsum; 5YBZ; -.
ProteinModelPortal; Q9ESN4; -.
SMR; Q9ESN4; -.
DIP; DIP-59699N; -.
IntAct; Q9ESN4; 1.
STRING; 10090.ENSMUSP00000056188; -.
PhosphoSitePlus; Q9ESN4; -.
MaxQB; Q9ESN4; -.
PaxDb; Q9ESN4; -.
PeptideAtlas; Q9ESN4; -.
PRIDE; Q9ESN4; -.
Ensembl; ENSMUST00000061545; ENSMUSP00000056188; ENSMUSG00000049630.
GeneID; 227580; -.
KEGG; mmu:227580; -.
UCSC; uc008ijv.1; mouse.
CTD; 389941; -.
MGI; MGI:2387350; C1ql3.
eggNOG; ENOG410IFA6; Eukaryota.
eggNOG; ENOG4111FAZ; LUCA.
GeneTree; ENSGT00940000161639; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; Q9ESN4; -.
OMA; DPYGTKS; -.
OrthoDB; EOG091G0UOF; -.
PhylomeDB; Q9ESN4; -.
TreeFam; TF329591; -.
PRO; PR:Q9ESN4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000049630; Expressed in 105 organ(s), highest expression level in lumbar subsegment of spinal cord.
CleanEx; MM_C1QL3; -.
Genevisible; Q9ESN4; MM.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050807; P:regulation of synapse organization; IDA:MGI.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR001073; C1q_dom.
InterPro; IPR008160; Collagen.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00386; C1q; 1.
Pfam; PF01391; Collagen; 1.
PRINTS; PR00007; COMPLEMNTC1Q.
SMART; SM00110; C1Q; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50871; C1Q; 1.
1: Evidence at protein level;
3D-structure; Collagen; Complete proteome; Reference proteome;
Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 255 Complement C1q-like protein 3.
/FTId=PRO_0000003542.
DOMAIN 61 111 Collagen-like.
DOMAIN 122 255 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
MUTAGEN 28 28 C->A: Does not affect
heterooligomerization with C1QL4; when
associated with A-32.
{ECO:0000269|PubMed:21378161,
ECO:0000269|PubMed:23449976}.
MUTAGEN 28 28 C->S: Does not affect
heterooligomerization with C1QL2; when
associated with S-32.
{ECO:0000269|PubMed:21378161,
ECO:0000269|PubMed:23449976}.
MUTAGEN 32 32 C->A: Does not affect
heterooligomerization with C1QL4; when
associated with A-28.
{ECO:0000269|PubMed:21378161,
ECO:0000269|PubMed:23449976}.
MUTAGEN 32 32 C->S: Does not affect
heterooligomerization with C1QL2; when
associated with S-28.
{ECO:0000269|PubMed:21378161,
ECO:0000269|PubMed:23449976}.
STRAND 128 132 {ECO:0000244|PDB:4QQH}.
STRAND 137 142 {ECO:0000244|PDB:4QQH}.
STRAND 147 152 {ECO:0000244|PDB:4QQH}.
TURN 158 160 {ECO:0000244|PDB:4QQH}.
STRAND 162 164 {ECO:0000244|PDB:4QQL}.
STRAND 169 179 {ECO:0000244|PDB:4QQH}.
STRAND 181 183 {ECO:0000244|PDB:4QQH}.
STRAND 185 193 {ECO:0000244|PDB:4QQH}.
STRAND 196 204 {ECO:0000244|PDB:4QQH}.
STRAND 212 221 {ECO:0000244|PDB:4QQH}.
STRAND 226 236 {ECO:0000244|PDB:4QQH}.
STRAND 240 242 {ECO:0000244|PDB:4QQH}.
STRAND 245 254 {ECO:0000244|PDB:4QQH}.
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


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