(data stored in ACNUC19913 zone)

HOGENOM: FELCAGS_1392_PE1

ID   FELCAGS_1392_PE1                     STANDARD;      PRT;   456 AA.
AC   FELCAGS_1392_PE1; Q28412;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Vitamin K-dependent protein C; EC=3.4.21 69;AltName:
DE   Full=Anticoagulant protein C;AltName: Full=Autoprothrombin IIA;AltName:
DE   Full=Blood coagulation factor XIV;Flags: Fragment; (FELCAGS_1392.PE1).
GN   Name=PROC;
OS   FELIS CATUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FELCAGS_1392.PE1.
CC       Felis catus genescaffold GeneScaffold_1392 CAT full sequence 1..80740
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_FELCA
CC   -!- FUNCTION: Protein C is a vitamin K-dependent serine protease that
CC       regulates blood coagulation by inactivating factors Va and VIIIa
CC       in the presence of calcium ions and phospholipids.
CC   -!- CATALYTIC ACTIVITY: Degradation of blood coagulation factors Va
CC       and VIIIa.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Felis_catus;ENSFCAG00000009488;ENSFCAT00000009490;ENSFCAP00000008800.
DR   EMBL; D43750; - ;
DR   UniProtKB/Swiss-Prot; Q28412; -.
DR   EMBL; D43750; BAA07807.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q28412; -.
DR   SMR; Q28412; 1-157.
DR   MEROPS; S01.218; -.
DR   Ensembl; ENSFCAT00000009490; ENSFCAP00000008800; ENSFCAG00000009488.
DR   eggNOG; maNOG17466; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   OrthoDB; EOG43BMNX; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; PARTIAL.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   HOGENOMDNA; FELCAGS_1392.PE1; -.
KW   ENSFCAG000000094885old_1320000031; ENSFCAP000000088001old_1320000031;
KW   D43750;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Serine protease.
SQ   SEQUENCE   456 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWQLSSLFLL VTIWGTSATP APPDSVFSSR ELSHRVLRIR KRANTFLEEL RAGSLERECV
     EEICDLEEAQ EIFQNVDDTL AFWAKYIDED QCAAPPPDHP CDSPCCGHGN CIDGISAFRC
     DCDPGWEGRF CLYXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXK
     FPCGRPGRRM EKKRKTVKRD TSQADQIDPR LVNGKLSGWG ESPWQVILLD SKKKLACGAV
     LIHTSWVLTA AHCMEDSKKL MVRLGEYDLR RREKWELDLD IKEVLMHPNY SRSTSDNDIA
     LLRLAQPAIL SQTIVPICLP DSGLAERELT QAGQETVVTG WGHRSEAKRN RTFVLNFIKV
     PVVPQNECIN AMHNMISENM LCAGILGDSQ DACEGDSGGP MVASFRGTSF LVGLVSWGEG
     CGRLHNYGVY TKVSRYLDWI HSHIRAEEAS LEGQVP
//

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