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Q9NPY3 (C1QR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CD93
Synonyms:C1QR1, MXRA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Interacts with HCV core protein. Interacts with C1QBP; the association may represent a cell surface C1q receptor. Ref.5 Ref.8

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.

Post-translational modification

N- and O-glycosylated. Ref.7

Sequence similarities

Contains 1 C-type lectin domain.

Contains 5 EGF-like domains.

Caution

Has been sometimes referred to as a collectin receptor.

Ref.6 reported that C1q is not a ligand for C1QR1.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 652631Complement component C1q receptor
PRO_0000017367

Regions

Topological domain24 – 580557Extracellular Potential
Transmembrane581 – 60121Helical; Potential
Topological domain602 – 65251Cytoplasmic Potential
Domain32 – 174143C-type lectin
Domain260 – 30142EGF-like 1
Domain302 – 34443EGF-like 2
Domain345 – 38440EGF-like 3; calcium-binding Potential
Domain385 – 42642EGF-like 4; calcium-binding Potential
Domain427 – 46842EGF-like 5; calcium-binding Potential

Amino acid modifications

Modified residue6441Phosphotyrosine By similarity
Glycosylation3251N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 165 By similarity
Disulfide bond264 ↔ 275 By similarity
Disulfide bond271 ↔ 285 By similarity
Disulfide bond287 ↔ 300 By similarity
Disulfide bond306 ↔ 317 By similarity
Disulfide bond311 ↔ 328 By similarity
Disulfide bond330 ↔ 343 By similarity
Disulfide bond349 ↔ 358 By similarity
Disulfide bond354 ↔ 367 By similarity
Disulfide bond369 ↔ 383 By similarity
Disulfide bond389 ↔ 400 By similarity
Disulfide bond396 ↔ 409 By similarity
Disulfide bond411 ↔ 425 By similarity
Disulfide bond431 ↔ 443 By similarity
Disulfide bond439 ↔ 452 By similarity
Disulfide bond454 ↔ 467 By similarity

Natural variations

Natural variant2201A → V in a colorectal cancer sample; somatic mutation. Ref.9
VAR_036400
Natural variant3181V → A. Ref.2
VAR_013573
Natural variant5411P → S. Ref.1
Corresponds to variant rs3746731 [ dbSNP | Ensembl ].
VAR_050102

Experimental info

Sequence conflict221T → V AA sequence Ref.1
Sequence conflict361C → T AA sequence Ref.1
Sequence conflict38 – 392TA → RI AA sequence Ref.1
Sequence conflict1551S → N in AAB53110. Ref.1
Sequence conflict1861G → A AA sequence Ref.1
Sequence conflict4921S → A AA sequence Ref.1
Sequence conflict4961R → Q AA sequence Ref.1
Sequence conflict5041R → G AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NPY3 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: EECA0FEAC55FCAC2

FASTA65268,560
        10         20         30         40         50         60 
MATSMGLLLL LLLLLTQPGA GTGADTEAVV CVGTACYTAH SGKLSAAEAQ NHCNQNGGNL 

        70         80         90        100        110        120 
ATVKSKEEAQ HVQRVLAQLL RREAALTARM SKFWIGLQRE KGKCLDPSLP LKGFSWVGGG 

       130        140        150        160        170        180 
EDTPYSNWHK ELRNSCISKR CVSLLLDLSQ PLLPSRLPKW SEGPCGSPGS PGSNIEGFVC 

       190        200        210        220        230        240 
KFSFKGMCRP LALGGPGQVT YTTPFQTTSS SLEAVPFASA ANVACGEGDK DETQSHYFLC 

       250        260        270        280        290        300 
KEKAPDVFDW GSSGPLCVSP KYGCNFNNGG CHQDCFEGGD GSFLCGCRPG FRLLDDLVTC 

       310        320        330        340        350        360 
ASRNPCSSSP CRGGATCVLG PHGKNYTCRC PQGYQLDSSQ LDCVDVDECQ DSPCAQECVN 

       370        380        390        400        410        420 
TPGGFRCECW VGYEPGGPGE GACQDVDECA LGRSPCAQGC TNTDGSFHCS CEEGYVLAGE 

       430        440        450        460        470        480 
DGTQCQDVDE CVGPGGPLCD SLCFNTQGSF HCGCLPGWVL APNGVSCTMG PVSLGPPSGP 

       490        500        510        520        530        540 
PDEEDKGEKE GSTVPRAATA SPTRGPEGTP KATPTTSRPS LSSDAPITSA PLKMLAPSGS 

       550        560        570        580        590        600 
PGVWREPSIH HATAASGPQE PAGGDSSVAT QNNDGTDGQK LLLFYILGTV VAILLLLALA 

       610        620        630        640        650 
LGLLVYRKRR AKREEKKEKK PQNAADSYSW VPERAESRAM ENQYSPTPGT DC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-220.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94333 mRNA. Translation: AAB53110.1.
AL118508 Genomic DNA. Translation: CAC00597.1.
BC028075 mRNA. Translation: AAH28075.1.
CCDSCCDS13149.1.
RefSeqNP_036204.2. NM_012072.3.
UniGeneHs.97199.

3D structure databases

ProteinModelPortalQ9NPY3.
SMRQ9NPY3. Positions 33-183, 251-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116580. 9 interactions.
IntActQ9NPY3. 6 interactions.
MINTMINT-4539936.
STRING9606.ENSP00000246006.

PTM databases

PhosphoSiteQ9NPY3.

Polymorphism databases

DMDM21759074.

Proteomic databases

PaxDbQ9NPY3.
PeptideAtlasQ9NPY3.
PRIDEQ9NPY3.

Protocols and materials databases

DNASU22918.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246006; ENSP00000246006; ENSG00000125810.
GeneID22918.
KEGGhsa:22918.
UCSCuc002wsv.3. human.

Organism-specific databases

CTD22918.
GeneCardsGC20M023059.
HGNCHGNC:15855. CD93.
HPAHPA009300.
HPA012368.
MIM120577. gene.
neXtProtNX_Q9NPY3.
PharmGKBPA25627.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147482.
HOVERGENHBG050751.
InParanoidQ9NPY3.
KOK06702.
OMAVTCASRN.
OrthoDBEOG71K638.
PhylomeDBQ9NPY3.
TreeFamTF330714.

Gene expression databases

BgeeQ9NPY3.
CleanExHS_CD93.
GenevestigatorQ9NPY3.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. 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]
PfamPF12662. cEGF. 2 hits.
PF00059. Lectin_C. 1 hit.
[Graphical view]
PIRSFPIRSF001775. CD93/CD141. 1 hit.
SMARTSM00034. CLECT. 1 hit.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 3 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

GeneWikiCD93.
GenomeRNAi22918.
NextBio43613.
PROQ9NPY3.
SOURCESearch...

Entry information

Entry nameC1QR1_HUMAN
AccessionPrimary (citable) accession number: Q9NPY3
Secondary accession number(s): O00274
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 11, 2002
Last modified: July 9, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries