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Complement component C1q receptor (C1q/MBL/SPA receptor) (C1qR(p)) (C1qRp) (Cell surface antigen AA4) (Complement component 1 q subcomponent receptor 1) (CD antigen CD93)

 C1QR1_RAT               Reviewed;         643 AA.
Q9ET61; Q9JIZ6;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 123.
RecName: Full=Complement component C1q receptor;
AltName: Full=C1q/MBL/SPA receptor;
Short=C1qR(p);
Short=C1qRp;
AltName: Full=Cell surface antigen AA4;
AltName: Full=Complement component 1 q subcomponent receptor 1;
AltName: CD_antigen=CD93;
Flags: Precursor;
Name=Cd93; Synonyms=C1qr1, C1qrp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=PVG; TISSUE=Natural killer cell;
PubMed=11093152;
DOI=10.1002/1521-4141(2000012)30:12<3355::AID-IMMU3355>3.0.CO;2-1;
Lovik G., Vaage J.T., Dissen E., Szpirer C., Ryan J.C., Rolstad B.;
"Characterization and molecular cloning of rat C1qRp, a receptor on NK
cells.";
Eur. J. Immunol. 30:3355-3362(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Lung;
PubMed=10934210; DOI=10.1074/jbc.M006229200;
Dean Y.D., McGreal E.P., Akatsu H., Gasque P.;
"Molecular and cellular properties of the rat AA4 antigen, a C-type
lectin-like receptor with structural homology to thrombomodulin.";
J. Biol. Chem. 275:34382-34392(2000).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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: Interacts with C1QBP; the association may represent a
cell surface C1q receptor. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung and
heart. Expressed at lower level in brain, thymus, liver, spleen,
intestine, kidney, adrenal gland, muscle and testis. Expressed on
endothelial cells, platelets, undifferentiated monocytes and
circulating natural killer cells.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
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EMBL; AF136537; AAG01572.1; -; mRNA.
EMBL; AF160978; AAF80402.1; -; mRNA.
RefSeq; NP_445835.1; NM_053383.1.
UniGene; Rn.162695; -.
ProteinModelPortal; Q9ET61; -.
SMR; Q9ET61; -.
STRING; 10116.ENSRNOP00000034001; -.
iPTMnet; Q9ET61; -.
PhosphoSitePlus; Q9ET61; -.
PaxDb; Q9ET61; -.
PRIDE; Q9ET61; -.
GeneID; 84398; -.
KEGG; rno:84398; -.
UCSC; RGD:621251; rat.
CTD; 22918; -.
RGD; 621251; Cd93.
eggNOG; ENOG410IJQN; Eukaryota.
eggNOG; ENOG410ZKXP; LUCA.
HOVERGEN; HBG050751; -.
InParanoid; Q9ET61; -.
KO; K06702; -.
PhylomeDB; Q9ET61; -.
PRO; PR:Q9ET61; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR026823; cEGF.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
Pfam; PF12662; cEGF; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 5.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 3.
1: Evidence at protein level;
Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Lectin; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 643 Complement component C1q receptor.
/FTId=PRO_0000017369.
TOPO_DOM 24 571 Extracellular. {ECO:0000255}.
TRANSMEM 572 592 Helical. {ECO:0000255}.
TOPO_DOM 593 643 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 173 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 257 298 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 299 341 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 342 381 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 382 423 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 424 462 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
MOD_RES 618 618 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 635 635 Phosphotyrosine.
{ECO:0000250|UniProtKB:O89103}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 164 {ECO:0000250}.
DISULFID 261 272 {ECO:0000250}.
DISULFID 268 282 {ECO:0000250}.
DISULFID 284 297 {ECO:0000250}.
DISULFID 303 314 {ECO:0000250}.
DISULFID 308 325 {ECO:0000250}.
DISULFID 327 340 {ECO:0000250}.
DISULFID 346 355 {ECO:0000250}.
DISULFID 351 364 {ECO:0000250}.
DISULFID 366 380 {ECO:0000250}.
DISULFID 386 397 {ECO:0000250}.
DISULFID 393 406 {ECO:0000250}.
DISULFID 408 422 {ECO:0000250}.
DISULFID 428 437 {ECO:0000250}.
DISULFID 433 446 {ECO:0000250}.
DISULFID 448 461 {ECO:0000250}.
CONFLICT 417 417 E -> K (in Ref. 2; AAF80402).
{ECO:0000305}.
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


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