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Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR(p)) (C1qRp) (Cell surface antigen AA4) (Complement component 1 q subcomponent receptor 1) (Lymphocyte antigen 68) (Ly-68) (CD antigen CD93)

 C1QR1_MOUSE             Reviewed;         644 AA.
O89103; A2AVY5; Q3U2X0;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 164.
RecName: Full=Complement component C1q receptor;
AltName: Full=C1q/MBL/SPA receptor;
Short=C1qR(p);
Short=C1qRp;
AltName: Full=Cell surface antigen AA4;
AltName: Full=Complement component 1 q subcomponent receptor 1;
AltName: Full=Lymphocyte antigen 68;
Short=Ly-68;
AltName: CD_antigen=CD93;
Flags: Precursor;
Name=Cd93; Synonyms=Aa4, C1qr1, C1qrp, Ly68;
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 [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=11074255; DOI=10.1016/S0161-5890(00)00057-2;
Kim T.S., Park M., Nepomuceno R.R., Palmarini G., Winokur S.,
Cotman C.A., Bengtsson U., Tenner A.J.;
"Characterization of the murine homolog of C1qR(P): identical cellular
expression pattern, chromosomal location and functional activity of
the human and murine C1qR(P).";
Mol. Immunol. 37:377-389(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukemia;
PubMed=10403644; DOI=10.1016/S1074-7613(00)80068-0;
Petrenko O., Beavis A., Klaine M., Kittappa R., Godin I.,
Lemischka I.R.;
"The molecular characterization of the fetal stem cell marker AA4.";
Immunity 10:691-700(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv; TISSUE=Endothelial cell, and Spleen;
PubMed=10430665; DOI=10.1007/s003359901093;
Norsworthy P.J., Taylor P.R., Walport M.J., Botto M.;
"Cloning of the mouse homolog of the 126-kDa human C1q/MBL/SP-A
receptor, C1qRp.";
Mamm. Genome 10:789-793(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-636, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Receptor (or element of a larger receptor complex) for
C1q, mannose-binding lectin (MBL2) and pulmonary surfactant
protein A (SPA). May mediate the enhancement of phagocytosis in
monocytes and macrophages upon interaction with soluble defense
collagens. May play a role in intercellular adhesion. Marker for
early multipotent hematopoietic precursor cells. May play a role
in cell-cell interactions during hematopoietic and vascular
development.
-!- SUBUNIT: Interacts with C1QBP; the association may represent a
cell surface C1q receptor. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed in lung, heart and bone marrow.
Expressed at lower level in ovary, whole embryo and fetal liver.
Not detected in brain, adult liver or thymus. Highly expressed in
peritoneal cavity and bone marrow macrophages. Not detected in
epithelial cells.
-!- DEVELOPMENTAL STAGE: First detectable in day 9 embryos, in the
endocardium and vascular endothelium in the anterior part of the
embryo. Expression in endothelial cells, initially restricted to
aorta, omphalomesenteric and umbilical arteries, later extends to
subcardinal veins, intersomitic arteries and perineural vessels.
On day 10, detectable in the entire embryo.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF074856; AAC63274.1; -; Genomic_DNA.
EMBL; AF081789; AAC62649.1; -; mRNA.
EMBL; AF099939; AAD47906.1; -; Genomic_DNA.
EMBL; AF099938; AAD47906.1; JOINED; Genomic_DNA.
EMBL; AK079060; BAC37518.1; -; mRNA.
EMBL; AK155060; BAE33020.1; -; mRNA.
EMBL; AL935149; CAM26726.1; -; Genomic_DNA.
CCDS; CCDS16839.1; -.
RefSeq; NP_034870.1; NM_010740.3.
UniGene; Mm.681; -.
ProteinModelPortal; O89103; -.
SMR; O89103; -.
IntAct; O89103; 1.
MINT; O89103; -.
STRING; 10090.ENSMUSP00000096876; -.
iPTMnet; O89103; -.
PhosphoSitePlus; O89103; -.
EPD; O89103; -.
MaxQB; O89103; -.
PaxDb; O89103; -.
PeptideAtlas; O89103; -.
PRIDE; O89103; -.
Ensembl; ENSMUST00000099269; ENSMUSP00000096876; ENSMUSG00000027435.
GeneID; 17064; -.
KEGG; mmu:17064; -.
UCSC; uc008mte.1; mouse.
CTD; 22918; -.
MGI; MGI:106664; Cd93.
eggNOG; ENOG410IJQN; Eukaryota.
eggNOG; ENOG410ZKXP; LUCA.
GeneTree; ENSGT00920000148956; -.
HOGENOM; HOG000232038; -.
HOVERGEN; HBG050751; -.
InParanoid; O89103; -.
KO; K06702; -.
OMA; HYFLCKE; -.
OrthoDB; EOG091G04OD; -.
PhylomeDB; O89103; -.
TreeFam; TF330714; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:O89103; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027435; Expressed in 248 organ(s), highest expression level in brain blood vessel.
CleanEx; MM_CD93; -.
Genevisible; O89103; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0001849; F:complement component C1q binding; ISO:MGI.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR026823; cEGF.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
Pfam; PF12662; cEGF; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 5.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 3.
1: Evidence at protein level;
Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Lectin; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 644 Complement component C1q receptor.
/FTId=PRO_0000017368.
TOPO_DOM 23 572 Extracellular. {ECO:0000255}.
TRANSMEM 573 593 Helical. {ECO:0000255}.
TOPO_DOM 594 644 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 173 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 257 298 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 299 341 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 342 381 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 382 423 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 424 465 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
MOD_RES 619 619 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET61}.
MOD_RES 636 636 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 164 {ECO:0000250}.
DISULFID 261 272 {ECO:0000250}.
DISULFID 268 282 {ECO:0000250}.
DISULFID 284 297 {ECO:0000250}.
DISULFID 303 314 {ECO:0000250}.
DISULFID 308 325 {ECO:0000250}.
DISULFID 327 340 {ECO:0000250}.
DISULFID 346 355 {ECO:0000250}.
DISULFID 351 364 {ECO:0000250}.
DISULFID 366 380 {ECO:0000250}.
DISULFID 386 397 {ECO:0000250}.
DISULFID 393 406 {ECO:0000250}.
DISULFID 408 422 {ECO:0000250}.
DISULFID 428 440 {ECO:0000250}.
DISULFID 436 449 {ECO:0000250}.
DISULFID 451 464 {ECO:0000250}.
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


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