C1QRF_MOUSE
ID C1QRF_MOUSE Reviewed; 258 AA.
AC O88992; A2AH89;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=C1q-related factor;
DE AltName: Full=C1q and tumor necrosis factor-related protein 14;
DE Short=C1q/TNF-related protein 14;
DE Short=CTRP14;
DE AltName: Full=Complement component 1 Q subcomponent-like 1;
DE Flags: Precursor;
GN Name=C1ql1; Synonyms=C1qrf, Crf, Ctrp14;
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=9878755; DOI=10.1016/s0169-328x(98)00278-2;
RA Berube N.G., Swanson X.H., Bertram M.J., Kittle J.D., Didenko V.,
RA Baskin D.S., Smith J.R., Pereira-Smith O.M.;
RT "Cloning and characterization of CRF, a novel C1q-related factor, expressed
RT in areas of the brain involved in motor function.";
RL Brain Res. Mol. Brain Res. 63:233-240(1999).
RN [2]
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 [3]
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 [4]
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 [5]
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 {ECO:0000269|PubMed:21262840}.
CC -!- SUBUNIT: Interacts with ADGRB3 (PubMed:21262840). Forms heterooligomers
CC with C1QL4, when proteins are coexpressed; this interaction does not
CC occur after secretion (PubMed:23449976). {ECO:0000269|PubMed:21262840,
CC ECO:0000269|PubMed:23449976}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in brainstem. More abundant in areas of
CC the nervous system involved in motor function, such as the Purkinje
CC cells of the cerebellum, the accessory olivary nucleus, the pons and
CC the red nucleus.
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DR EMBL; AF095155; AAC64187.1; -; mRNA.
DR EMBL; AL731670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34162.1; -; Genomic_DNA.
DR CCDS; CCDS25509.1; -.
DR RefSeq; NP_035925.2; NM_011795.2.
DR PDB; 4D7Y; X-ray; 1.44 A; A=125-258.
DR PDB; 4QQ2; X-ray; 1.80 A; A/B/C=122-258.
DR PDBsum; 4D7Y; -.
DR PDBsum; 4QQ2; -.
DR AlphaFoldDB; O88992; -.
DR SMR; O88992; -.
DR DIP; DIP-61402N; -.
DR STRING; 10090.ENSMUSP00000050469; -.
DR PhosphoSitePlus; O88992; -.
DR PaxDb; O88992; -.
DR PeptideAtlas; O88992; -.
DR PRIDE; O88992; -.
DR ProteomicsDB; 273854; -.
DR Antibodypedia; 29941; 66 antibodies from 16 providers.
DR DNASU; 23829; -.
DR Ensembl; ENSMUST00000057849; ENSMUSP00000050469; ENSMUSG00000045532.
DR GeneID; 23829; -.
DR KEGG; mmu:23829; -.
DR UCSC; uc007lsz.2; mouse.
DR CTD; 10882; -.
DR MGI; MGI:1344400; C1ql1.
DR VEuPathDB; HostDB:ENSMUSG00000045532; -.
DR eggNOG; ENOG502QSKV; Eukaryota.
DR GeneTree; ENSGT00940000162478; -.
DR HOGENOM; CLU_001074_3_1_1; -.
DR InParanoid; O88992; -.
DR OMA; FTCAIPG; -.
DR OrthoDB; 1320954at2759; -.
DR PhylomeDB; O88992; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 23829; 1 hit in 73 CRISPR screens.
DR PRO; PR:O88992; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88992; protein.
DR Bgee; ENSMUSG00000045532; Expressed in retinal neural layer and 88 other tissues.
DR ExpressionAtlas; O88992; baseline and differential.
DR Genevisible; O88992; MM.
DR GO; GO:0044301; C:climbing fiber; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0099558; P:maintenance of synapse structure; IMP:MGI.
DR GO; GO:0061743; P:motor learning; IGI:MGI.
DR GO; GO:0016322; P:neuron remodeling; IMP: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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..258
FT /note="C1q-related factor"
FT /id="PRO_0000003528"
FT DOMAIN 67..115
FT /note="Collagen-like"
FT DOMAIN 125..258
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 39..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..109
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: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:23449976"
FT CONFLICT 52
FT /note="L -> V (in Ref. 1; AAC64187)"
FT /evidence="ECO:0000305"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4D7Y"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:4D7Y"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4QQ2"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:4D7Y"
SQ SEQUENCE 258 AA; 26500 MW; 3C769203069B2137 CRC64;
MLLVLVVLIP VLVSSGGPDG HYEMLGTCRM VCDPYPARGP GAGARSDGGD ALSEQSGAPP
PSTLVQGPQG KPGRTGKPGP PGPPGDRGPP GPVGPPGEKG EPGKPGPPGL PGSGGSGAIS
TATYTTVPRV AFYAGLKNPH EGYEVLKFDD VVTNLGNNYD AASGKFTCNI PGTYFFTYHV
LMRGGDGTSM WADLCKNGQV RASAIAQDAD QNYDYASNSV ILHLDAGDEV FIKLDGGKAH
GGNSNKYSTF SGFIIYSD
