ID   EPCR_BOVIN              Reviewed;         241 AA.
AC   Q28105; Q1LZD2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Endothelial protein C receptor;
DE   AltName: Full=Activated protein C receptor;
DE            Short=APC receptor;
DE   AltName: Full=Endothelial cell protein C receptor;
DE   AltName: CD_antigen=CD201;
DE   Flags: Precursor;
GN   Name=PROCR; Synonyms=EPCR;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L39065; AAA87356.1; -; mRNA.
DR   EMBL; BC116074; AAI16075.1; -; mRNA.
DR   PIR; B55945; B55945.
DR   RefSeq; NP_776862.1; NM_174437.1.
DR   AlphaFoldDB; Q28105; -.
DR   SMR; Q28105; -.
DR   STRING; 9913.ENSBTAP00000010911; -.
DR   PaxDb; Q28105; -.
DR   Ensembl; ENSBTAT00000010911; ENSBTAP00000010911; ENSBTAG00000008291.
DR   GeneID; 282005; -.
DR   KEGG; bta:282005; -.
DR   CTD; 10544; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008291; -.
DR   VGNC; VGNC:33359; PROCR.
DR   eggNOG; ENOG502S3SK; Eukaryota.
DR   GeneTree; ENSGT00390000001159; -.
DR   HOGENOM; CLU_1151498_0_0_1; -.
DR   InParanoid; Q28105; -.
DR   OMA; QDPESWA; -.
DR   OrthoDB; 1203534at2759; -.
DR   TreeFam; TF335868; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000008291; Expressed in ureter and 101 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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   2: Evidence at transcript 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..241
FT                   /note="Endothelial protein C receptor"
FT                   /id="PRO_0000021190"
FT   TOPO_DOM        18..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        221..234
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   241 AA;  27010 MW;  B5129082F86FEE70 CRC64;
     MLTTLLPLLP LLLPGWALCS QEASDGPWDL HMTQVSYFRN PSQVWHRGNA TLGGVLTHVL
     EGPGRNVSIQ QLQPLQEPDS WALTKIYLNR YLEEFVGLVQ VVHQERGVTF PLIIRCFLGC
     ELPPEGSEAR VFFEVAVNGS SFVNFQPKTA SWVAEPHAPS RVVTYTVDQL NKYNRTRYEL
     REFLQDTCVQ YIQKHITTNN LKGSQTGRSY TSLVLGVLVG CFIVTGVAVG IFLCTGGRRR
     C