Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NPY3

- C1QR1_HUMAN

UniProt

Q9NPY3 - C1QR1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Complement component C1q receptor

Gene

CD93

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. carbohydrate binding Source: UniProtKB-KW
  3. complement component C1q binding Source: UniProtKB
  4. receptor activity Source: UniProtKB

GO - Biological processi

  1. macrophage activation Source: UniProtKB
  2. phagocytosis Source: UniProtKB
  3. single organismal cell-cell adhesion Source: UniProtKB
  4. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C1q receptor
Alternative name(s):
C1q/MBL/SPA receptor
Short name:
C1qR
Short name:
C1qR(p)
Short name:
C1qRp
CDw93
Complement component 1 q subcomponent receptor 1
Matrix-remodeling-associated protein 4
CD_antigen: CD93
Gene namesi
Name:CD93
Synonyms:C1QR1, MXRA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15855. CD93.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytoplasmic membrane-bounded vesicle Source: Ensembl
  3. integral component of membrane Source: UniProtKB
  4. plasma membrane Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 652631Complement component C1q receptorPRO_0000017367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 165By similarity
Disulfide bondi264 ↔ 275By similarity
Disulfide bondi271 ↔ 285By similarity
Disulfide bondi287 ↔ 300By similarity
Disulfide bondi306 ↔ 317By similarity
Disulfide bondi311 ↔ 328By similarity
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi330 ↔ 343By similarity
Disulfide bondi349 ↔ 358By similarity
Disulfide bondi354 ↔ 367By similarity
Disulfide bondi369 ↔ 383By similarity
Disulfide bondi389 ↔ 400By similarity
Disulfide bondi396 ↔ 409By similarity
Disulfide bondi411 ↔ 425By similarity
Disulfide bondi431 ↔ 443By similarity
Disulfide bondi439 ↔ 452By similarity
Disulfide bondi454 ↔ 467By similarity
Modified residuei644 – 6441PhosphotyrosineBy similarity

Post-translational modificationi

N- and O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9NPY3.
PeptideAtlasiQ9NPY3.
PRIDEiQ9NPY3.

PTM databases

PhosphoSiteiQ9NPY3.

Expressioni

Tissue specificityi

Highly expressed in endothelial cells, platelets, cells of myeloid origin, such as monocytes and neutrophils. Not expressed in cells of lymphoid origin.

Gene expression databases

BgeeiQ9NPY3.
CleanExiHS_CD93.
GenevestigatoriQ9NPY3.

Organism-specific databases

HPAiHPA009300.
HPA012368.

Interactioni

Subunit structurei

Interacts with HCV core protein. Interacts with C1QBP; the association may represent a cell surface C1q receptor.2 Publications

Protein-protein interaction databases

BioGridi116580. 10 interactions.
IntActiQ9NPY3. 8 interactions.
MINTiMINT-4539936.
STRINGi9606.ENSP00000246006.

Structurei

3D structure databases

ProteinModelPortaliQ9NPY3.
SMRiQ9NPY3. Positions 272-458.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 580557ExtracellularSequence AnalysisAdd
BLAST
Topological domaini602 – 65251CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei581 – 60121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 174143C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini260 – 30142EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini302 – 34443EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini345 – 38440EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini385 – 42642EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini427 – 46842EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 5 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG147482.
GeneTreeiENSGT00530000063403.
HOVERGENiHBG050751.
InParanoidiQ9NPY3.
KOiK06702.
OMAiVTCASRN.
OrthoDBiEOG71K638.
PhylomeDBiQ9NPY3.
TreeFamiTF330714.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR016316. CD93/CD141.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF12662. cEGF. 2 hits.
PF00059. Lectin_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 3 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NPY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSMGLLLL LLLLLTQPGA GTGADTEAVV CVGTACYTAH SGKLSAAEAQ
60 70 80 90 100
NHCNQNGGNL ATVKSKEEAQ HVQRVLAQLL RREAALTARM SKFWIGLQRE
110 120 130 140 150
KGKCLDPSLP LKGFSWVGGG EDTPYSNWHK ELRNSCISKR CVSLLLDLSQ
160 170 180 190 200
PLLPSRLPKW SEGPCGSPGS PGSNIEGFVC KFSFKGMCRP LALGGPGQVT
210 220 230 240 250
YTTPFQTTSS SLEAVPFASA ANVACGEGDK DETQSHYFLC KEKAPDVFDW
260 270 280 290 300
GSSGPLCVSP KYGCNFNNGG CHQDCFEGGD GSFLCGCRPG FRLLDDLVTC
310 320 330 340 350
ASRNPCSSSP CRGGATCVLG PHGKNYTCRC PQGYQLDSSQ LDCVDVDECQ
360 370 380 390 400
DSPCAQECVN TPGGFRCECW VGYEPGGPGE GACQDVDECA LGRSPCAQGC
410 420 430 440 450
TNTDGSFHCS CEEGYVLAGE DGTQCQDVDE CVGPGGPLCD SLCFNTQGSF
460 470 480 490 500
HCGCLPGWVL APNGVSCTMG PVSLGPPSGP PDEEDKGEKE GSTVPRAATA
510 520 530 540 550
SPTRGPEGTP KATPTTSRPS LSSDAPITSA PLKMLAPSGS PGVWREPSIH
560 570 580 590 600
HATAASGPQE PAGGDSSVAT QNNDGTDGQK LLLFYILGTV VAILLLLALA
610 620 630 640 650
LGLLVYRKRR AKREEKKEKK PQNAADSYSW VPERAESRAM ENQYSPTPGT

DC
Length:652
Mass (Da):68,560
Last modified:July 11, 2002 - v3
Checksum:iEECA0FEAC55FCAC2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → V AA sequence (PubMed:9047234)Curated
Sequence conflicti36 – 361C → T AA sequence (PubMed:9047234)Curated
Sequence conflicti38 – 392TA → RI AA sequence (PubMed:9047234)Curated
Sequence conflicti155 – 1551S → N in AAB53110. (PubMed:9047234)Curated
Sequence conflicti186 – 1861G → A AA sequence (PubMed:9047234)Curated
Sequence conflicti492 – 4921S → A AA sequence (PubMed:9047234)Curated
Sequence conflicti496 – 4961R → Q AA sequence (PubMed:9047234)Curated
Sequence conflicti504 – 5041R → G AA sequence (PubMed:9047234)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti220 – 2201A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036400
Natural varianti318 – 3181V → A.1 Publication
VAR_013573
Natural varianti541 – 5411P → S.1 Publication
Corresponds to variant rs3746731 [ dbSNP | Ensembl ].
VAR_050102

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U94333 mRNA. Translation: AAB53110.1.
AL118508 Genomic DNA. Translation: CAC00597.1.
BC028075 mRNA. Translation: AAH28075.1.
CCDSiCCDS13149.1.
RefSeqiNP_036204.2. NM_012072.3.
UniGeneiHs.97199.

Genome annotation databases

EnsembliENST00000246006; ENSP00000246006; ENSG00000125810.
GeneIDi22918.
KEGGihsa:22918.
UCSCiuc002wsv.3. human.

Polymorphism databases

DMDMi21759074.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U94333 mRNA. Translation: AAB53110.1 .
AL118508 Genomic DNA. Translation: CAC00597.1 .
BC028075 mRNA. Translation: AAH28075.1 .
CCDSi CCDS13149.1.
RefSeqi NP_036204.2. NM_012072.3.
UniGenei Hs.97199.

3D structure databases

ProteinModelPortali Q9NPY3.
SMRi Q9NPY3. Positions 272-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116580. 10 interactions.
IntActi Q9NPY3. 8 interactions.
MINTi MINT-4539936.
STRINGi 9606.ENSP00000246006.

PTM databases

PhosphoSitei Q9NPY3.

Polymorphism databases

DMDMi 21759074.

Proteomic databases

PaxDbi Q9NPY3.
PeptideAtlasi Q9NPY3.
PRIDEi Q9NPY3.

Protocols and materials databases

DNASUi 22918.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000246006 ; ENSP00000246006 ; ENSG00000125810 .
GeneIDi 22918.
KEGGi hsa:22918.
UCSCi uc002wsv.3. human.

Organism-specific databases

CTDi 22918.
GeneCardsi GC20M023059.
HGNCi HGNC:15855. CD93.
HPAi HPA009300.
HPA012368.
MIMi 120577. gene.
neXtProti NX_Q9NPY3.
PharmGKBi PA25627.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG147482.
GeneTreei ENSGT00530000063403.
HOVERGENi HBG050751.
InParanoidi Q9NPY3.
KOi K06702.
OMAi VTCASRN.
OrthoDBi EOG71K638.
PhylomeDBi Q9NPY3.
TreeFami TF330714.

Miscellaneous databases

GeneWikii CD93.
GenomeRNAii 22918.
NextBioi 43613.
PROi Q9NPY3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NPY3.
CleanExi HS_CD93.
Genevestigatori Q9NPY3.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR016316. CD93/CD141.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view ]
Pfami PF12662. cEGF. 2 hits.
PF00059. Lectin_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001775. CD93/CD141. 1 hit.
SMARTi SM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 3 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro."
    Nepomuceno R.R., Henschen-Edman A.H., Burgess W.H., Tenner A.J.
    Immunity 6:119-129(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT SER-541.
  2. "Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning."
    Steinberger P., Szekeres A., Wille S., Stockl J., Selenko N., Prager E., Staffler G., Madic O., Stockinger H., Knapp W.
    J. Leukoc. Biol. 71:133-140(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-318.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Leukocyte.
  5. "Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R, associate to form a complex."
    Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E., Eggleton P., Reid K.B., Peerschke E.I.
    J. Immunol. 159:1429-1436(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  6. "Human C1qRp is identical with CD93 and the mNI-11 antigen but does not bind C1q."
    McGreal E.P., Ikewaki N., Akatsu H., Morgan B.P., Gasque P.
    J. Immunol. 168:5222-5232(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity."
    Nepomuceno R.R., Ruiz S., Park M., Tenner A.J.
    J. Immunol. 162:3583-3589(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  8. "Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation."
    Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.
    J. Clin. Invest. 106:1239-1249(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV CORE PROTEIN.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-220.

Entry informationi

Entry nameiC1QR1_HUMAN
AccessioniPrimary (citable) accession number: Q9NPY3
Secondary accession number(s): O00274
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 11, 2002
Last modified: October 29, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Has been sometimes referred to as a collectin receptor.Curated
PubMed:11994479 reported that C1q is not a ligand for C1QR1.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3