(data stored in ACNUC19913 zone)

HOGENOM: MACMU13_137_PE9

ID   MACMU13_137_PE9                      STANDARD;      PRT;   462 AA.
AC   MACMU13_137_PE9; Q28506;
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; (MACMU13_137.PE9).
GN   Name=PROC;
OS   MACACA MULATTA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Cercopithecoidea; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MACMU13_137.PE9.
CC       Macaca mulatta chromosome 13 MMUL_1 partial sequence 133167979..1341660
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_MACMU
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:Macaca_mulatta;ENSMMUG00000023563;ENSMMUT00000033144;ENSMMUP00000031015.
DR   EMBL; D43754; - ;
DR   UniProtKB/Swiss-Prot; Q28506; -.
DR   EMBL; D43754; BAA07811.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q28506; -.
DR   SMR; Q28506; 1-161.
DR   STRING; Q28506; -.
DR   MEROPS; S01.218; -.
DR   eggNOG; prNOG07393; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q28506; -.
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; MACMU13_137.PE9; -.
KW   ENSMMUG000000235635old_1320000031; ENSMMUP000000310151old_1320000031;
KW   D43754;
KW   Blood coagulation; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Serine protease.
SQ   SEQUENCE   462 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWRLTGLLLF VATWGISSTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RPSSLERECV
     EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CSSLCCGHGT CIDGIGSFSC
     DCRSGWEGRF CQREVSFLNC SLDNGGCTHY CLEEVGWRRC SCAPGYKLGD DLLQCQPAVK
     FPCGRPWRRI EKKRSHLKRR DTEDQEDQVD PRLIDGKMTR RGDSPWQVVL LDSKKKLACG
     AVLIHPSWVL TAAHCMEESK KLLVRLGEYD LRRWEKWELD LDIEEVFIHP NYTKSTTDND
     IALLRLAQPA TLSQTIVPIC LPDSGLAERE LTQAGQETLV TGWGYHSSRE KEAKRNRTFI
     LNFIKIPVVP RNECSEVMSN MVSENMLCAG ILGDRQDACE GDSGGPMVAS FHGTWFLVGL
     VSWGEGCGLL HNYGVYTKVS RYLDWIHGHI RDKEALAKSR AP
//

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