C1QR1_RAT
ID C1QR1_RAT Reviewed; 643 AA.
AC Q9ET61; Q9JIZ6;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Complement component C1q receptor;
DE AltName: Full=C1q/MBL/SPA receptor;
DE Short=C1qR(p);
DE Short=C1qRp;
DE AltName: Full=Cell surface antigen AA4;
DE AltName: Full=Complement component 1 q subcomponent receptor 1;
DE AltName: CD_antigen=CD93;
DE Flags: Precursor;
GN Name=Cd93; Synonyms=C1qr1, C1qrp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PVG; TISSUE=Natural killer cell;
RX PubMed=11093152;
RX DOI=10.1002/1521-4141(2000012)30:12<3355::aid-immu3355>3.0.co;2-1;
RA Lovik G., Vaage J.T., Dissen E., Szpirer C., Ryan J.C., Rolstad B.;
RT "Characterization and molecular cloning of rat C1qRp, a receptor on NK
RT cells.";
RL Eur. J. Immunol. 30:3355-3362(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=10934210; DOI=10.1074/jbc.m006229200;
RA Dean Y.D., McGreal E.P., Akatsu H., Gasque P.;
RT "Molecular and cellular properties of the rat AA4 antigen, a C-type lectin-
RT like receptor with structural homology to thrombomodulin.";
RL J. Biol. Chem. 275:34382-34392(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung and
CC heart. Expressed at lower level in brain, thymus, liver, spleen,
CC intestine, kidney, adrenal gland, muscle and testis. Expressed on
CC endothelial cells, platelets, undifferentiated monocytes and
CC circulating natural killer cells.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR EMBL; AF136537; AAG01572.1; -; mRNA.
DR EMBL; AF160978; AAF80402.1; -; mRNA.
DR RefSeq; NP_445835.1; NM_053383.1.
DR AlphaFoldDB; Q9ET61; -.
DR SMR; Q9ET61; -.
DR GlyGen; Q9ET61; 2 sites.
DR iPTMnet; Q9ET61; -.
DR PhosphoSitePlus; Q9ET61; -.
DR PaxDb; Q9ET61; -.
DR PRIDE; Q9ET61; -.
DR Ensembl; ENSRNOT00000076493; ENSRNOP00000089608; ENSRNOG00000024799.
DR GeneID; 84398; -.
DR KEGG; rno:84398; -.
DR UCSC; RGD:621251; rat.
DR CTD; 22918; -.
DR RGD; 621251; Cd93.
DR GeneTree; ENSGT00940000156996; -.
DR InParanoid; Q9ET61; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q9ET61; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9ET61; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISS: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; 4.
DR PROSITE; PS01187; EGF_CA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..643
FT /note="Complement component C1q receptor"
FT /id="PRO_0000017369"
FT TOPO_DOM 24..571
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..173
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 257..298
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 299..341
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 342..381
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 382..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 424..462
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 469..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 635
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O89103"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..164
FT /evidence="ECO:0000250"
FT DISULFID 261..272
FT /evidence="ECO:0000250"
FT DISULFID 268..282
FT /evidence="ECO:0000250"
FT DISULFID 284..297
FT /evidence="ECO:0000250"
FT DISULFID 303..314
FT /evidence="ECO:0000250"
FT DISULFID 308..325
FT /evidence="ECO:0000250"
FT DISULFID 327..340
FT /evidence="ECO:0000250"
FT DISULFID 346..355
FT /evidence="ECO:0000250"
FT DISULFID 351..364
FT /evidence="ECO:0000250"
FT DISULFID 366..380
FT /evidence="ECO:0000250"
FT DISULFID 386..397
FT /evidence="ECO:0000250"
FT DISULFID 393..406
FT /evidence="ECO:0000250"
FT DISULFID 408..422
FT /evidence="ECO:0000250"
FT DISULFID 428..437
FT /evidence="ECO:0000250"
FT DISULFID 433..446
FT /evidence="ECO:0000250"
FT DISULFID 448..461
FT /evidence="ECO:0000250"
FT CONFLICT 417
FT /note="E -> K (in Ref. 2; AAF80402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 68782 MW; 9AE4C933AD943DB6 CRC64;
MVTSTGLLLL LGLLGQLWAG AAADSEAVVC EGTACYTAHW GKLSAAEAQH RCNENGGNLA
TVKSEEEARH VQEALAQLLK TKAPSETKIG KFWIGLQREK GKCTYHDLPM KGFSWVGGGE
DTTYSNWYKA SKSSCISKRC VSLILDLSLK PHPSHLPKWH ESPCGTPDAP GNSIEGFLCK
FNFKGMCSPL ALGGPGQLTY TTPFQATTSS LKAVPFASVA NVVCGDEAES KTNYYLCKET
TAGVFHWGSS GPLCVSPKFG CSFNNGGCQQ DCFEGGDGSF RCGCRPGFRL LDDLVTCASR
NPCSSNPCTG GGMCHSVPLS ENYTCHCPRG YQLDSSQVHC VDIDECEDSP CDQECINTPG
GFHCECWVGY QSSGSKEEAC EDVDECTAAY SPCAQGCTNT DGSFYCSCKE GYIMSGEDST
QCEDIDECLG NPCDTLCINT DGSFRCGCPA GFELAPNGVS CTRGSMFSEL PARPPQKEDK
GDGKESTVPL TEMPGSLNGS KDVSNRAQTT DLSIQSDSST ASVPLEIEVS SEASDVWLDL
GTYLPTTSGH SQPTHEDSVP AHSDSDTDGQ KLLLFYILGT VVAISLLLAL ALGLLIYLKR
KAKKEEIKEK KAQNAADSYS WIPERAESRA PENQYSPTPG TDC
