EPCR_MOUSE
ID EPCR_MOUSE Reviewed; 242 AA.
AC Q64695; Q4FK76; Q9WV33;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Endothelial protein C receptor;
DE AltName: Full=Activated protein C receptor;
DE Short=APC receptor;
DE AltName: Full=Centrocyclin;
DE AltName: Full=Centrosomal protein CCD41;
DE AltName: Full=Endothelial cell protein C receptor;
DE AltName: CD_antigen=CD201;
DE Flags: Precursor;
GN Name=Procr; Synonyms=Epcr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8449997; DOI=10.1242/jcs.104.1.19;
RA Rothbarth K., Petzelt C., Lu X., Todorov I.T., Joswigt G.H., Pepperkok R.,
RA Ansorge W., Werner D.;
RT "cDNA-derived molecular characteristics and antibodies to a new centrosome-
RT associated and G2/M phase-prevalent protein.";
RL J. Cell Sci. 104:19-30(1993).
RN [2]
RP SEQUENCE REVISION TO 18-47.
RA Werner D.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hemangioendothelioma;
RX PubMed=7890676; DOI=10.1074/jbc.270.10.5571;
RA Fukudome K., Esmon C.T.;
RT "Molecular cloning and expression of murine and bovine endothelial cell
RT protein C/activated protein C receptor (EPCR). The structural and
RT functional conservation in human, bovine, and murine EPCR.";
RL J. Biol. Chem. 270:5571-5577(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10235444;
RA Liang Z., Rosen E.D., Castellino F.J.;
RT "Nucleotide structure and characterization of the murine gene encoding the
RT endothelial cell protein C receptor.";
RL Thromb. Haemost. 81:585-588(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds activated protein C. Enhances protein C activation by
CC the thrombin-thrombomodulin complex; plays a role in the protein C
CC pathway controlling blood coagulation.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells.
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DR EMBL; X63748; CAA45281.2; -; mRNA.
DR EMBL; L39017; AAC42049.1; -; mRNA.
DR EMBL; AF162695; AAD43351.1; -; Genomic_DNA.
DR EMBL; AK143719; BAE25514.1; -; mRNA.
DR EMBL; AK167302; BAE39407.1; -; mRNA.
DR EMBL; CT010175; CAJ18383.1; -; mRNA.
DR EMBL; AL929233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06143.1; -; Genomic_DNA.
DR CCDS; CCDS16954.1; -.
DR PIR; A55945; A55945.
DR PIR; S18948; S18948.
DR RefSeq; NP_035301.2; NM_011171.2.
DR AlphaFoldDB; Q64695; -.
DR SMR; Q64695; -.
DR STRING; 10090.ENSMUSP00000029140; -.
DR GlyGen; Q64695; 5 sites.
DR iPTMnet; Q64695; -.
DR PhosphoSitePlus; Q64695; -.
DR SwissPalm; Q64695; -.
DR EPD; Q64695; -.
DR MaxQB; Q64695; -.
DR PaxDb; Q64695; -.
DR PeptideAtlas; Q64695; -.
DR PRIDE; Q64695; -.
DR ProteomicsDB; 275529; -.
DR Antibodypedia; 11183; 695 antibodies from 39 providers.
DR DNASU; 19124; -.
DR Ensembl; ENSMUST00000029140; ENSMUSP00000029140; ENSMUSG00000027611.
DR GeneID; 19124; -.
DR KEGG; mmu:19124; -.
DR UCSC; uc008nlh.2; mouse.
DR CTD; 10544; -.
DR MGI; MGI:104596; Procr.
DR VEuPathDB; HostDB:ENSMUSG00000027611; -.
DR eggNOG; ENOG502S3SK; Eukaryota.
DR GeneTree; ENSGT00390000001159; -.
DR HOGENOM; CLU_1151498_0_0_1; -.
DR InParanoid; Q64695; -.
DR OMA; QDPESWA; -.
DR PhylomeDB; Q64695; -.
DR TreeFam; TF335868; -.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 19124; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Procr; mouse.
DR PRO; PR:Q64695; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64695; protein.
DR Bgee; ENSMUSG00000027611; Expressed in decidua and 190 other tissues.
DR ExpressionAtlas; Q64695; baseline and differential.
DR Genevisible; Q64695; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0050819; P:negative regulation of coagulation; ISO:MGI.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR015669; Endothetial_C_recpt.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR PANTHER; PTHR15349; PTHR15349; 1.
DR Pfam; PF16497; MHC_I_3; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..242
FT /note="Endothelial protein C receptor"
FT /id="PRO_0000021192"
FT TOPO_DOM 18..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..190
FT /evidence="ECO:0000250"
FT DISULFID 223..236
FT /evidence="ECO:0000250"
FT CONFLICT 7
FT /note="P -> L (in Ref. 1; CAA45281)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="N -> H (in Ref. 1; CAA45281, 3; AAC42049 and 4;
FT AAD43351)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="RC -> GLLII (in Ref. 1; CAA45281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 27189 MW; 7215B7F51C81B50A CRC64;
MLTKFLPLLL LLLPGCALCN SDGSQSLHML QISYFQDNHH VRHQGNASLG KLLTHTLEGP
SQNVTILQLQ PWQDPESWER TESGLQIYLT QFESLVKLVY RERKENVFFP LTVSCSLGCE
LPEEEEEGSE PHVFFDVAVN GSAFVSFRPK TAVWVSGSQE PSKAANFTLK QLNAYNRTRY
ELQEFLQDTC VEFLENHITT QNMKGSQTGR SYTSLVLGIL MGCFIIAGVA VGIFMCTSGR
RC
