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Q9NPY3

- C1QR1_HUMAN

UniProt

Q9NPY3 - C1QR1_HUMAN

Protein

Complement component C1q receptor

Gene

CD93

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (11 Jul 2002)
      Previous versions | rss
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    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: InterPro
    3. complement component C1q binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. 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

    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

    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. 9 interactions.
    IntActiQ9NPY3. 8 interactions.
    MINTiMINT-4539936.
    STRINGi9606.ENSP00000246006.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPY3.
    SMRiQ9NPY3. Positions 33-183, 251-458.
    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.
    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

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    MATSMGLLLL LLLLLTQPGA GTGADTEAVV CVGTACYTAH SGKLSAAEAQ    50
    NHCNQNGGNL ATVKSKEEAQ HVQRVLAQLL RREAALTARM SKFWIGLQRE 100
    KGKCLDPSLP LKGFSWVGGG EDTPYSNWHK ELRNSCISKR CVSLLLDLSQ 150
    PLLPSRLPKW SEGPCGSPGS PGSNIEGFVC KFSFKGMCRP LALGGPGQVT 200
    YTTPFQTTSS SLEAVPFASA ANVACGEGDK DETQSHYFLC KEKAPDVFDW 250
    GSSGPLCVSP KYGCNFNNGG CHQDCFEGGD GSFLCGCRPG FRLLDDLVTC 300
    ASRNPCSSSP CRGGATCVLG PHGKNYTCRC PQGYQLDSSQ LDCVDVDECQ 350
    DSPCAQECVN TPGGFRCECW VGYEPGGPGE GACQDVDECA LGRSPCAQGC 400
    TNTDGSFHCS CEEGYVLAGE DGTQCQDVDE CVGPGGPLCD SLCFNTQGSF 450
    HCGCLPGWVL APNGVSCTMG PVSLGPPSGP PDEEDKGEKE GSTVPRAATA 500
    SPTRGPEGTP KATPTTSRPS LSSDAPITSA PLKMLAPSGS PGVWREPSIH 550
    HATAASGPQE PAGGDSSVAT QNNDGTDGQK LLLFYILGTV VAILLLLALA 600
    LGLLVYRKRR AKREEKKEKK PQNAADSYSW VPERAESRAM ENQYSPTPGT 650
    DC 652
    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 33-183, 251-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116580. 9 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.
    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

    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 1, 2014
    This is version 139 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