UniProtKB - Q9ET61 (C1QR1_RAT)
Protein
Complement component C1q receptor
Gene
Cd93
Organism
Rattus norvegicus (Rat)
Status
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
- calcium ion binding Source: InterPro
- carbohydrate binding Source: UniProtKB-KW
- complement component C1q complex binding Source: RGD
GO - Biological processi
- cell-cell adhesion Source: UniProtKB
Keywordsi
Molecular function | Receptor |
Biological process | Cell adhesion |
Ligand | Lectin |
Enzyme and pathway databases
Reactomei | R-RNO-6798695, Neutrophil degranulation |
Names & Taxonomyi
Protein namesi | Recommended name: Complement component C1q receptorAlternative name(s): C1q/MBL/SPA receptor Short name: C1qR(p) Short name: C1qRp Cell surface antigen AA4 Complement component 1 q subcomponent receptor 1 CD_antigen: CD93 |
Gene namesi | Name:Cd93 Synonyms:C1qr1, C1qrp |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621251, Cd93 |
Subcellular locationi
Other locations
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- cell surface Source: RGD
- cytoplasmic vesicle Source: RGD
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 24 – 571 | ExtracellularSequence analysisAdd BLAST | 548 | |
Transmembranei | 572 – 592 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 593 – 643 | CytoplasmicSequence analysisAdd BLAST | 51 |
Keywords - Cellular componenti
MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | Sequence analysisAdd BLAST | 23 | |
ChainiPRO_0000017369 | 24 – 643 | Complement component C1q receptorAdd BLAST | 620 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 140 ↔ 164 | By similarity | ||
Disulfide bondi | 261 ↔ 272 | By similarity | ||
Disulfide bondi | 268 ↔ 282 | By similarity | ||
Disulfide bondi | 284 ↔ 297 | By similarity | ||
Disulfide bondi | 303 ↔ 314 | By similarity | ||
Disulfide bondi | 308 ↔ 325 | By similarity | ||
Glycosylationi | 322 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 327 ↔ 340 | By similarity | ||
Disulfide bondi | 346 ↔ 355 | By similarity | ||
Disulfide bondi | 351 ↔ 364 | By similarity | ||
Disulfide bondi | 366 ↔ 380 | By similarity | ||
Disulfide bondi | 386 ↔ 397 | By similarity | ||
Disulfide bondi | 393 ↔ 406 | By similarity | ||
Disulfide bondi | 408 ↔ 422 | By similarity | ||
Disulfide bondi | 428 ↔ 437 | By similarity | ||
Disulfide bondi | 433 ↔ 446 | By similarity | ||
Disulfide bondi | 448 ↔ 461 | By similarity | ||
Glycosylationi | 498 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 618 | PhosphoserineCombined sources | 1 | |
Modified residuei | 635 | PhosphotyrosineBy similarity | 1 |
Post-translational modificationi
N- and O-glycosylated.By similarity
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PaxDbi | Q9ET61 |
PRIDEi | Q9ET61 |
PTM databases
GlyGeni | Q9ET61, 2 sites |
iPTMneti | Q9ET61 |
PhosphoSitePlusi | Q9ET61 |
Expressioni
Tissue specificityi
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.
Interactioni
Subunit structurei
Interacts with C1QBP; the association may represent a cell surface C1q receptor.
By similarityGO - Molecular functioni
- complement component C1q complex binding Source: RGD
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 173 | C-type lectinPROSITE-ProRule annotationAdd BLAST | 143 | |
Domaini | 257 – 298 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 299 – 341 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 342 – 381 | EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 382 – 423 | EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 424 – 462 | EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 |
Keywords - Domaini
EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
InParanoidi | Q9ET61 |
OrthoDBi | 1174178at2759 |
PhylomeDBi | Q9ET61 |
Family and domain databases
Gene3Di | 3.10.100.10, 1 hit |
InterProi | View protein in InterPro IPR001304, C-type_lectin-like IPR016186, C-type_lectin-like/link_sf IPR026823, cEGF IPR016187, CTDL_fold IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF07645, EGF_CA, 2 hits PF00059, Lectin_C, 1 hit |
SMARTi | View protein in SMART SM00034, CLECT, 1 hit SM00181, EGF, 5 hits SM00179, EGF_CA, 5 hits |
SUPFAMi | SSF56436, SSF56436, 1 hit SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 3 hits PS50041, C_TYPE_LECTIN_2, 1 hit PS01186, EGF_2, 3 hits PS50026, EGF_3, 4 hits PS01187, EGF_CA, 3 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9ET61-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVTSTGLLLL LGLLGQLWAG AAADSEAVVC EGTACYTAHW GKLSAAEAQH
60 70 80 90 100
RCNENGGNLA TVKSEEEARH VQEALAQLLK TKAPSETKIG KFWIGLQREK
110 120 130 140 150
GKCTYHDLPM KGFSWVGGGE DTTYSNWYKA SKSSCISKRC VSLILDLSLK
160 170 180 190 200
PHPSHLPKWH ESPCGTPDAP GNSIEGFLCK FNFKGMCSPL ALGGPGQLTY
210 220 230 240 250
TTPFQATTSS LKAVPFASVA NVVCGDEAES KTNYYLCKET TAGVFHWGSS
260 270 280 290 300
GPLCVSPKFG CSFNNGGCQQ DCFEGGDGSF RCGCRPGFRL LDDLVTCASR
310 320 330 340 350
NPCSSNPCTG GGMCHSVPLS ENYTCHCPRG YQLDSSQVHC VDIDECEDSP
360 370 380 390 400
CDQECINTPG GFHCECWVGY QSSGSKEEAC EDVDECTAAY SPCAQGCTNT
410 420 430 440 450
DGSFYCSCKE GYIMSGEDST QCEDIDECLG NPCDTLCINT DGSFRCGCPA
460 470 480 490 500
GFELAPNGVS CTRGSMFSEL PARPPQKEDK GDGKESTVPL TEMPGSLNGS
510 520 530 540 550
KDVSNRAQTT DLSIQSDSST ASVPLEIEVS SEASDVWLDL GTYLPTTSGH
560 570 580 590 600
SQPTHEDSVP AHSDSDTDGQ KLLLFYILGT VVAISLLLAL ALGLLIYLKR
610 620 630 640
KAKKEEIKEK KAQNAADSYS WIPERAESRA PENQYSPTPG TDC
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 417 | E → K in AAF80402 (PubMed:10934210).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF136537 mRNA Translation: AAG01572.1 AF160978 mRNA Translation: AAF80402.1 |
RefSeqi | NP_445835.1, NM_053383.1 |
Genome annotation databases
GeneIDi | 84398 |
KEGGi | rno:84398 |
UCSCi | RGD:621251, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF136537 mRNA Translation: AAG01572.1 AF160978 mRNA Translation: AAF80402.1 |
RefSeqi | NP_445835.1, NM_053383.1 |
3D structure databases
SMRi | Q9ET61 |
ModBasei | Search... |
PTM databases
GlyGeni | Q9ET61, 2 sites |
iPTMneti | Q9ET61 |
PhosphoSitePlusi | Q9ET61 |
Proteomic databases
PaxDbi | Q9ET61 |
PRIDEi | Q9ET61 |
Genome annotation databases
GeneIDi | 84398 |
KEGGi | rno:84398 |
UCSCi | RGD:621251, rat |
Organism-specific databases
CTDi | 22918 |
RGDi | 621251, Cd93 |
Phylogenomic databases
InParanoidi | Q9ET61 |
OrthoDBi | 1174178at2759 |
PhylomeDBi | Q9ET61 |
Enzyme and pathway databases
Reactomei | R-RNO-6798695, Neutrophil degranulation |
Miscellaneous databases
PROi | PR:Q9ET61 |
Family and domain databases
Gene3Di | 3.10.100.10, 1 hit |
InterProi | View protein in InterPro IPR001304, C-type_lectin-like IPR016186, C-type_lectin-like/link_sf IPR026823, cEGF IPR016187, CTDL_fold IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF07645, EGF_CA, 2 hits PF00059, Lectin_C, 1 hit |
SMARTi | View protein in SMART SM00034, CLECT, 1 hit SM00181, EGF, 5 hits SM00179, EGF_CA, 5 hits |
SUPFAMi | SSF56436, SSF56436, 1 hit SSF57184, SSF57184, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 3 hits PS50041, C_TYPE_LECTIN_2, 1 hit PS01186, EGF_2, 3 hits PS50026, EGF_3, 4 hits PS01187, EGF_CA, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | C1QR1_RAT | |
Accessioni | Q9ET61Primary (citable) accession number: Q9ET61 Secondary accession number(s): Q9JIZ6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 20, 2002 |
Last sequence update: | March 1, 2001 | |
Last modified: | December 2, 2020 | |
This is version 133 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |