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Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR) (C1qR(p)) (C1qRp) (CDw93) (Complement component 1 q subcomponent receptor 1) (Matrix-remodeling-associated protein 4) (CD antigen CD93)

 C1QR1_HUMAN             Reviewed;         652 AA.
Q9NPY3; O00274;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 3.
20-JUN-2018, entry version 176.
RecName: Full=Complement component C1q receptor;
AltName: Full=C1q/MBL/SPA receptor;
Short=C1qR;
Short=C1qR(p);
Short=C1qRp;
AltName: Full=CDw93;
AltName: Full=Complement component 1 q subcomponent receptor 1;
AltName: Full=Matrix-remodeling-associated protein 4;
AltName: CD_antigen=CD93;
Flags: Precursor;
Name=CD93; Synonyms=C1QR1, MXRA4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
SER-541.
PubMed=9047234; DOI=10.1016/S1074-7613(00)80419-7;
Nepomuceno R.R., Henschen-Edman A.H., Burgess W.H., Tenner A.J.;
"cDNA cloning and primary structure analysis of C1qR(P), the human
C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro.";
Immunity 6:119-129(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-318.
PubMed=11781389;
Steinberger P., Szekeres A., Wille S., Stockl J., Selenko N.,
Prager E., Staffler G., Madic O., Stockinger H., Knapp W.;
"Identification of human CD93 as the phagocytic C1q receptor (C1qRp)
by expression cloning.";
J. Leukoc. Biol. 71:133-140(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukocyte;
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).
[5]
INTERACTION WITH C1QBP.
PubMed=9233640;
Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E.,
Eggleton P., Reid K.B., Peerschke E.I.;
"Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-
R, associate to form a complex.";
J. Immunol. 159:1429-1436(1997).
[6]
CHARACTERIZATION.
PubMed=11994479; DOI=10.4049/jimmunol.168.10.5222;
McGreal E.P., Ikewaki N., Akatsu H., Morgan B.P., Gasque P.;
"Human C1qRp is identical with CD93 and the mNI-11 antigen but does
not bind C1q.";
J. Immunol. 168:5222-5232(2002).
[7]
GLYCOSYLATION.
PubMed=10092817;
Nepomuceno R.R., Ruiz S., Park M., Tenner A.J.;
"C1qRP is a heavily O-glycosylated cell surface protein involved in
the regulation of phagocytic activity.";
J. Immunol. 162:3583-3589(1999).
[8]
INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
PubMed=11086025; DOI=10.1172/JCI10323;
Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J.,
Hahn Y.S.;
"Interaction between complement receptor gC1qR and hepatitis C virus
core protein inhibits T-lymphocyte proliferation.";
J. Clin. Invest. 106:1239-1249(2000).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
VARIANT [LARGE SCALE ANALYSIS] VAL-220.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
-!- SUBUNIT: Interacts with C1QBP; the association may represent a
cell surface C1q receptor. {ECO:0000269|PubMed:9233640}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis virus
C/HCV core protein. {ECO:0000269|PubMed:11086025}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Highly expressed in endothelial cells,
platelets, cells of myeloid origin, such as monocytes and
neutrophils. Not expressed in cells of lymphoid origin.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:10092817}.
-!- CAUTION: Has been sometimes referred to as a collectin receptor.
{ECO:0000305}.
-!- CAUTION: PubMed:11994479 reported that C1q is not a ligand for
C1QR1. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U94333; AAB53110.1; -; mRNA.
EMBL; AL118508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028075; AAH28075.1; -; mRNA.
CCDS; CCDS13149.1; -.
RefSeq; NP_036204.2; NM_012072.3.
UniGene; Hs.97199; -.
ProteinModelPortal; Q9NPY3; -.
SMR; Q9NPY3; -.
BioGrid; 116580; 21.
IntAct; Q9NPY3; 8.
STRING; 9606.ENSP00000246006; -.
iPTMnet; Q9NPY3; -.
PhosphoSitePlus; Q9NPY3; -.
BioMuta; CD93; -.
DMDM; 21759074; -.
PaxDb; Q9NPY3; -.
PeptideAtlas; Q9NPY3; -.
PRIDE; Q9NPY3; -.
ProteomicsDB; 82049; -.
TopDownProteomics; Q9NPY3; -.
DNASU; 22918; -.
Ensembl; ENST00000246006; ENSP00000246006; ENSG00000125810.
GeneID; 22918; -.
KEGG; hsa:22918; -.
UCSC; uc002wsv.4; human.
CTD; 22918; -.
DisGeNET; 22918; -.
EuPathDB; HostDB:ENSG00000125810.9; -.
GeneCards; CD93; -.
HGNC; HGNC:15855; CD93.
HPA; HPA009300; -.
HPA; HPA012368; -.
MIM; 120577; gene.
neXtProt; NX_Q9NPY3; -.
OpenTargets; ENSG00000125810; -.
PharmGKB; PA25627; -.
eggNOG; ENOG410IJQN; Eukaryota.
eggNOG; ENOG410ZKXP; LUCA.
GeneTree; ENSGT00920000148956; -.
HOVERGEN; HBG050751; -.
InParanoid; Q9NPY3; -.
KO; K06702; -.
OMA; HYFLCKE; -.
OrthoDB; EOG091G04OD; -.
PhylomeDB; Q9NPY3; -.
TreeFam; TF330714; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
GeneWiki; CD93; -.
GenomeRNAi; 22918; -.
PRO; PR:Q9NPY3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125810; -.
CleanEx; HS_CD93; -.
Genevisible; Q9NPY3; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
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; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006909; P:phagocytosis; NAS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; 3.
PROSITE; PS01187; EGF_CA; 3.
1: Evidence at protein level;
Cell adhesion; Complete proteome; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Host-virus interaction;
Lectin; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21
CHAIN 22 652 Complement component C1q receptor.
/FTId=PRO_0000017367.
TOPO_DOM 24 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 601 Helical. {ECO:0000255}.
TOPO_DOM 602 652 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 174 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 260 301 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 302 344 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 345 384 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 385 426 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 427 468 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET61}.
MOD_RES 644 644 Phosphotyrosine.
{ECO:0000250|UniProtKB:O89103}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 141 165 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 264 275 {ECO:0000250}.
DISULFID 271 285 {ECO:0000250}.
DISULFID 287 300 {ECO:0000250}.
DISULFID 306 317 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 311 328 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 330 343 {ECO:0000250}.
DISULFID 349 358 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 354 367 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 369 383 {ECO:0000250}.
DISULFID 389 400 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 396 409 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 411 425 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 431 443 {ECO:0000250}.
DISULFID 439 452 {ECO:0000250}.
DISULFID 454 467 {ECO:0000250}.
VARIANT 220 220 A -> V (in a colorectal cancer sample;
somatic mutation; dbSNP:rs138932459).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036400.
VARIANT 318 318 V -> A. {ECO:0000269|PubMed:11781389}.
/FTId=VAR_013573.
VARIANT 541 541 P -> S (in dbSNP:rs3746731).
{ECO:0000269|PubMed:9047234}.
/FTId=VAR_050102.
CONFLICT 22 22 T -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 36 36 C -> T (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 38 39 TA -> RI (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 155 155 S -> N (in Ref. 1; AAB53110).
{ECO:0000305}.
CONFLICT 186 186 G -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 492 492 S -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 496 496 R -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 504 504 R -> G (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 652 AA; 68560 MW; EECA0FEAC55FCAC2 CRC64;
MATSMGLLLL LLLLLTQPGA GTGADTEAVV CVGTACYTAH SGKLSAAEAQ NHCNQNGGNL
ATVKSKEEAQ HVQRVLAQLL RREAALTARM SKFWIGLQRE KGKCLDPSLP LKGFSWVGGG
EDTPYSNWHK ELRNSCISKR CVSLLLDLSQ PLLPSRLPKW SEGPCGSPGS PGSNIEGFVC
KFSFKGMCRP LALGGPGQVT YTTPFQTTSS SLEAVPFASA ANVACGEGDK DETQSHYFLC
KEKAPDVFDW GSSGPLCVSP KYGCNFNNGG CHQDCFEGGD GSFLCGCRPG FRLLDDLVTC
ASRNPCSSSP CRGGATCVLG PHGKNYTCRC PQGYQLDSSQ LDCVDVDECQ DSPCAQECVN
TPGGFRCECW VGYEPGGPGE GACQDVDECA LGRSPCAQGC TNTDGSFHCS CEEGYVLAGE
DGTQCQDVDE CVGPGGPLCD SLCFNTQGSF HCGCLPGWVL APNGVSCTMG PVSLGPPSGP
PDEEDKGEKE GSTVPRAATA SPTRGPEGTP KATPTTSRPS LSSDAPITSA PLKMLAPSGS
PGVWREPSIH HATAASGPQE PAGGDSSVAT QNNDGTDGQK LLLFYILGTV VAILLLLALA
LGLLVYRKRR AKREEKKEKK PQNAADSYSW VPERAESRAM ENQYSPTPGT DC


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