C1QR1_MOUSE
ID C1QR1_MOUSE Reviewed; 644 AA.
AC O89103; A2AVY5; Q3U2X0;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Complement component C1q receptor;
DE AltName: Full=C1q/MBL/SPA receptor;
DE Short=C1qR(p);
DE Short=C1qRp;
DE AltName: Full=Cell surface antigen AA4;
DE AltName: Full=Complement component 1 q subcomponent receptor 1;
DE AltName: Full=Lymphocyte antigen 68;
DE Short=Ly-68;
DE AltName: CD_antigen=CD93;
DE Flags: Precursor;
GN Name=Cd93; Synonyms=Aa4, C1qr1, C1qrp, Ly68;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11074255; DOI=10.1016/s0161-5890(00)00057-2;
RA Kim T.S., Park M., Nepomuceno R.R., Palmarini G., Winokur S., Cotman C.A.,
RA Bengtsson U., Tenner A.J.;
RT "Characterization of the murine homolog of C1qR(P): identical cellular
RT expression pattern, chromosomal location and functional activity of the
RT human and murine C1qR(P).";
RL Mol. Immunol. 37:377-389(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukemia;
RX PubMed=10403644; DOI=10.1016/s1074-7613(00)80068-0;
RA Petrenko O., Beavis A., Klaine M., Kittappa R., Godin I., Lemischka I.R.;
RT "The molecular characterization of the fetal stem cell marker AA4.";
RL Immunity 10:691-700(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Endothelial cell, and Spleen;
RX PubMed=10430665; DOI=10.1007/s003359901093;
RA Norsworthy P.J., Taylor P.R., Walport M.J., Botto M.;
RT "Cloning of the mouse homolog of the 126-kDa human C1q/MBL/SP-A receptor,
RT C1qRp.";
RL Mamm. Genome 10:789-793(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor (or element of a larger receptor complex) for C1q,
CC mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA).
CC May mediate the enhancement of phagocytosis in monocytes and
CC macrophages upon interaction with soluble defense collagens. May play a
CC role in intercellular adhesion. Marker for early multipotent
CC hematopoietic precursor cells. May play a role in cell-cell
CC interactions during hematopoietic and vascular development.
CC -!- SUBUNIT: Interacts with C1QBP; the association may represent a cell
CC surface C1q receptor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in lung, heart and bone marrow. Expressed
CC at lower level in ovary, whole embryo and fetal liver. Not detected in
CC brain, adult liver or thymus. Highly expressed in peritoneal cavity and
CC bone marrow macrophages. Not detected in epithelial cells.
CC -!- DEVELOPMENTAL STAGE: First detectable in day 9 embryos, in the
CC endocardium and vascular endothelium in the anterior part of the
CC embryo. Expression in endothelial cells, initially restricted to aorta,
CC omphalomesenteric and umbilical arteries, later extends to subcardinal
CC veins, intersomitic arteries and perineural vessels. On day 10,
CC detectable in the entire embryo.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF074856; AAC63274.1; -; Genomic_DNA.
DR EMBL; AF081789; AAC62649.1; -; mRNA.
DR EMBL; AF099939; AAD47906.1; -; Genomic_DNA.
DR EMBL; AF099938; AAD47906.1; JOINED; Genomic_DNA.
DR EMBL; AK079060; BAC37518.1; -; mRNA.
DR EMBL; AK155060; BAE33020.1; -; mRNA.
DR EMBL; AL935149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16839.1; -.
DR RefSeq; NP_034870.1; NM_010740.3.
DR AlphaFoldDB; O89103; -.
DR SMR; O89103; -.
DR STRING; 10090.ENSMUSP00000096876; -.
DR GlyGen; O89103; 2 sites.
DR iPTMnet; O89103; -.
DR PhosphoSitePlus; O89103; -.
DR CPTAC; non-CPTAC-3563; -.
DR EPD; O89103; -.
DR MaxQB; O89103; -.
DR PaxDb; O89103; -.
DR PeptideAtlas; O89103; -.
DR PRIDE; O89103; -.
DR ProteomicsDB; 273727; -.
DR Antibodypedia; 2408; 586 antibodies from 33 providers.
DR DNASU; 17064; -.
DR Ensembl; ENSMUST00000099269; ENSMUSP00000096876; ENSMUSG00000027435.
DR GeneID; 17064; -.
DR KEGG; mmu:17064; -.
DR UCSC; uc008mte.1; mouse.
DR CTD; 22918; -.
DR MGI; MGI:106664; Cd93.
DR VEuPathDB; HostDB:ENSMUSG00000027435; -.
DR eggNOG; ENOG502QUVB; Eukaryota.
DR GeneTree; ENSGT00940000156996; -.
DR HOGENOM; CLU_027075_1_0_1; -.
DR InParanoid; O89103; -.
DR OMA; MEPSTHH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O89103; -.
DR TreeFam; TF330714; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 17064; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cd93; mouse.
DR PRO; PR:O89103; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O89103; protein.
DR Bgee; ENSMUSG00000027435; Expressed in brain blood vessel and 224 other tissues.
DR Genevisible; O89103; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 5.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..644
FT /note="Complement component C1q receptor"
FT /id="PRO_0000017368"
FT TOPO_DOM 23..572
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..173
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 257..298
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 299..341
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 342..381
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 382..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 424..465
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 473..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET61"
FT MOD_RES 636
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..164
FT /evidence="ECO:0000250"
FT DISULFID 261..272
FT /evidence="ECO:0000250"
FT DISULFID 268..282
FT /evidence="ECO:0000250"
FT DISULFID 284..297
FT /evidence="ECO:0000250"
FT DISULFID 303..314
FT /evidence="ECO:0000250"
FT DISULFID 308..325
FT /evidence="ECO:0000250"
FT DISULFID 327..340
FT /evidence="ECO:0000250"
FT DISULFID 346..355
FT /evidence="ECO:0000250"
FT DISULFID 351..364
FT /evidence="ECO:0000250"
FT DISULFID 366..380
FT /evidence="ECO:0000250"
FT DISULFID 386..397
FT /evidence="ECO:0000250"
FT DISULFID 393..406
FT /evidence="ECO:0000250"
FT DISULFID 408..422
FT /evidence="ECO:0000250"
FT DISULFID 428..440
FT /evidence="ECO:0000250"
FT DISULFID 436..449
FT /evidence="ECO:0000250"
FT DISULFID 451..464
FT /evidence="ECO:0000250"
SQ SEQUENCE 644 AA; 69354 MW; EB4351648BF8635A CRC64;
MAISTGLFLL LGLLGQPWAG AAADSQAVVC EGTACYTAHW GKLSAAEAQH RCNENGGNLA
TVKSEEEARH VQQALTQLLK TKAPLEAKMG KFWIGLQREK GNCTYHDLPM RGFSWVGGGE
DTAYSNWYKA SKSSCIFKRC VSLILDLSLT PHPSHLPKWH ESPCGTPEAP GNSIEGFLCK
FNFKGMCRPL ALGGPGRVTY TTPFQATTSS LEAVPFASVA NVACGDEAKS ETHYFLCNEK
TPGIFHWGSS GPLCVSPKFG CSFNNGGCQQ DCFEGGDGSF RCGCRPGFRL LDDLVTCASR
NPCSSNPCTG GGMCHSVPLS ENYTCRCPSG YQLDSSQVHC VDIDECQDSP CAQDCVNTLG
SFHCECWVGY QPSGPKEEAC EDVDECAAAN SPCAQGCINT DGSFYCSCKE GYIVSGEDST
QCEDIDECSD ARGNPCDSLC FNTDGSFRCG CPPGWELAPN GVFCSRGTVF SELPARPPQK
EDNDDRKEST MPPTEMPSSP SGSKDVSNRA QTTGLFVQSD IPTASVPLEI EIPSEVSDVW
FELGTYLPTT SGHSKPTHED SVSAHSDTDG QNLLLFYILG TVVAISLLLV LALGILIYHK
RRAKKEEIKE KKPQNAADSY SWVPERAESQ APENQYSPTP GTDC
