C1QR1_HUMAN
ID C1QR1_HUMAN Reviewed; 652 AA.
AC Q9NPY3; O00274;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Complement component C1q receptor;
DE AltName: Full=C1q/MBL/SPA receptor;
DE Short=C1qR;
DE Short=C1qR(p);
DE Short=C1qRp;
DE AltName: Full=CDw93;
DE AltName: Full=Complement component 1 q subcomponent receptor 1;
DE AltName: Full=Matrix-remodeling-associated protein 4;
DE AltName: CD_antigen=CD93;
DE Flags: Precursor;
GN Name=CD93; Synonyms=C1QR1, MXRA4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT SER-541.
RX PubMed=9047234; DOI=10.1016/s1074-7613(00)80419-7;
RA Nepomuceno R.R., Henschen-Edman A.H., Burgess W.H., Tenner A.J.;
RT "cDNA cloning and primary structure analysis of C1qR(P), the human
RT C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro.";
RL Immunity 6:119-129(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-318.
RX PubMed=11781389;
RA Steinberger P., Szekeres A., Wille S., Stockl J., Selenko N., Prager E.,
RA Staffler G., Madic O., Stockinger H., Knapp W.;
RT "Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by
RT expression cloning.";
RL J. Leukoc. Biol. 71:133-140(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH C1QBP.
RX PubMed=9233640;
RA Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E., Eggleton P.,
RA Reid K.B., Peerschke E.I.;
RT "Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R,
RT associate to form a complex.";
RL J. Immunol. 159:1429-1436(1997).
RN [6]
RP CHARACTERIZATION.
RX PubMed=11994479; DOI=10.4049/jimmunol.168.10.5222;
RA McGreal E.P., Ikewaki N., Akatsu H., Morgan B.P., Gasque P.;
RT "Human C1qRp is identical with CD93 and the mNI-11 antigen but does not
RT bind C1q.";
RL J. Immunol. 168:5222-5232(2002).
RN [7]
RP GLYCOSYLATION.
RX PubMed=10092817;
RA Nepomuceno R.R., Ruiz S., Park M., Tenner A.J.;
RT "C1qRP is a heavily O-glycosylated cell surface protein involved in the
RT regulation of phagocytic activity.";
RL J. Immunol. 162:3583-3589(1999).
RN [8]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=11086025; DOI=10.1172/jci10323;
RA Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.;
RT "Interaction between complement receptor gC1qR and hepatitis C virus core
RT protein inhibits T-lymphocyte proliferation.";
RL J. Clin. Invest. 106:1239-1249(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-220.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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.
CC -!- SUBUNIT: Interacts with C1QBP; the association may represent a cell
CC surface C1q receptor. {ECO:0000269|PubMed:9233640}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis virus C/HCV
CC core protein. {ECO:0000269|PubMed:11086025}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in endothelial cells, platelets,
CC cells of myeloid origin, such as monocytes and neutrophils. Not
CC expressed in cells of lymphoid origin.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:10092817}.
CC -!- CAUTION: Has been sometimes referred to as a collectin receptor.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:11994479 reported that C1q is not a ligand for C1QR1.
CC {ECO:0000305}.
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DR EMBL; U94333; AAB53110.1; -; mRNA.
DR EMBL; AL118508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028075; AAH28075.1; -; mRNA.
DR CCDS; CCDS13149.1; -.
DR RefSeq; NP_036204.2; NM_012072.3.
DR AlphaFoldDB; Q9NPY3; -.
DR BioGRID; 116580; 29.
DR IntAct; Q9NPY3; 18.
DR STRING; 9606.ENSP00000246006; -.
DR GlyGen; Q9NPY3; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NPY3; -.
DR PhosphoSitePlus; Q9NPY3; -.
DR BioMuta; CD93; -.
DR DMDM; 21759074; -.
DR jPOST; Q9NPY3; -.
DR MassIVE; Q9NPY3; -.
DR PaxDb; Q9NPY3; -.
DR PeptideAtlas; Q9NPY3; -.
DR PRIDE; Q9NPY3; -.
DR ProteomicsDB; 82049; -.
DR TopDownProteomics; Q9NPY3; -.
DR ABCD; Q9NPY3; 1 sequenced antibody.
DR Antibodypedia; 2408; 586 antibodies from 33 providers.
DR DNASU; 22918; -.
DR Ensembl; ENST00000246006.5; ENSP00000246006.4; ENSG00000125810.10.
DR GeneID; 22918; -.
DR KEGG; hsa:22918; -.
DR MANE-Select; ENST00000246006.5; ENSP00000246006.4; NM_012072.4; NP_036204.2.
DR UCSC; uc002wsv.4; human.
DR CTD; 22918; -.
DR DisGeNET; 22918; -.
DR GeneCards; CD93; -.
DR HGNC; HGNC:15855; CD93.
DR HPA; ENSG00000125810; Tissue enhanced (placenta).
DR MIM; 120577; gene.
DR neXtProt; NX_Q9NPY3; -.
DR OpenTargets; ENSG00000125810; -.
DR PharmGKB; PA25627; -.
DR VEuPathDB; HostDB:ENSG00000125810; -.
DR eggNOG; ENOG502QUVB; Eukaryota.
DR GeneTree; ENSGT00940000156996; -.
DR HOGENOM; CLU_027075_1_0_1; -.
DR InParanoid; Q9NPY3; -.
DR OMA; MEPSTHH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q9NPY3; -.
DR TreeFam; TF330714; -.
DR PathwayCommons; Q9NPY3; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9NPY3; -.
DR BioGRID-ORCS; 22918; 17 hits in 1070 CRISPR screens.
DR GeneWiki; CD93; -.
DR GenomeRNAi; 22918; -.
DR Pharos; Q9NPY3; Tbio.
DR PRO; PR:Q9NPY3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NPY3; protein.
DR Bgee; ENSG00000125810; Expressed in visceral pleura and 193 other tissues.
DR Genevisible; Q9NPY3; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; NAS: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; 3.
DR PROSITE; PS01187; EGF_CA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Host-virus interaction; Lectin; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..652
FT /note="Complement component C1q receptor"
FT /id="PRO_0000017367"
FT TOPO_DOM 24..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..174
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 260..301
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 302..344
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 345..384
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 385..426
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 427..468
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 472..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET61"
FT MOD_RES 644
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O89103"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 264..275
FT /evidence="ECO:0000250"
FT DISULFID 271..285
FT /evidence="ECO:0000250"
FT DISULFID 287..300
FT /evidence="ECO:0000250"
FT DISULFID 306..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 311..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 330..343
FT /evidence="ECO:0000250"
FT DISULFID 349..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 354..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 369..383
FT /evidence="ECO:0000250"
FT DISULFID 389..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 396..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 411..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 431..443
FT /evidence="ECO:0000250"
FT DISULFID 439..452
FT /evidence="ECO:0000250"
FT DISULFID 454..467
FT /evidence="ECO:0000250"
FT VARIANT 220
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs138932459)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036400"
FT VARIANT 318
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:11781389"
FT /id="VAR_013573"
FT VARIANT 541
FT /note="P -> S (in dbSNP:rs3746731)"
FT /evidence="ECO:0000269|PubMed:9047234"
FT /id="VAR_050102"
FT CONFLICT 22
FT /note="T -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="C -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="TA -> RI (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="S -> N (in Ref. 1; AAB53110)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="G -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="S -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="R -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="R -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
