(data stored in ACNUC19913 zone)

HOGENOM: RABIT7_62_PE7

ID   RABIT7_62_PE7                        STANDARD;      PRT;   464 AA.
AC   RABIT7_62_PE7; Q28661;
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;Contains: RecName: Full=Vitamin
DE   K-dependent protein C light chain;Contains: RecName: Full=Vitamin
DE   K-dependent protein C heavy chain;Contains: RecName: Full=Activation
DE   peptide;Flags: Precursor; Fragment; (RABIT7_62.PE7).
GN   Name=PROC;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT7_62.PE7.
CC       Oryctolagus cuniculus chromosome 7 oryCun2 partial sequence
CC       58486702..59424744 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_RABIT
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   -!- SUBUNIT: Synthesized as a single chain precursor, which is cleaved
CC       into a light chain and a heavy chain held together by a disulfide
CC       bond. The enzyme is then activated by thrombin, which cleaves a
CC       tetradecapeptide from the amino end of the heavy chain; this
CC       reaction, which occurs at the surface of endothelial cells, is
CC       strongly promoted by thrombomodulin.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu
CC       residues allows the modified protein to bind calcium.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains
CC       (By similarity).
CC   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to
CC       another site, beyond the GLA domain. This GLA-independent binding
CC       site is necessary for the recognition of the thrombin-
CC       thrombomodulin complex.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000015846;ENSOCUT00000015843;ENSOCUP00000013608.
DR   EMBL; U49933; - ;
DR   UniProtKB/Swiss-Prot; Q28661; -.
DR   EMBL; U49933; AAA92956.1; -; mRNA.
DR   UniGene; Ocu.2057; -.
DR   ProteinModelPortal; Q28661; -.
DR   SMR; Q28661; 38-82, 85-179, 209-446.
DR   MEROPS; S01.218; -.
DR   Ensembl; ENSOCUT00000015843; ENSOCUP00000013608; ENSOCUG00000015846.
DR   eggNOG; maNOG17466; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   OrthoDB; EOG43BMNX; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   HOGENOMDNA; RABIT7_62.PE7; -.
KW   ENSOCUG00000015846820036002503210000011;
KW   PROC_RABIT; U49933;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat;
KW   Serine protease; Signal; Zymogen.
SQ   SEQUENCE   464 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWQLAGLLLF VATWGTSSTP APPDSVFTSR EHAHHVLRIR KRANSFLEEL RPSSLERECV
     EEVCDLEEAK EIFQSVDDTL AFWYKYVDGD QCAALPSEHP CSSQCCGHGT CADSIGGFSC
     QCHGGWEGSF CQYEVRFSNC SVDNGGCAHY CLEEEAGRSC SCAPGYELAD DHLQCEPAVR
     FPCGRLGWKR IEKKRGNVKR DLEQVDEMDE VDPRLIDGKL TRRGDSPWQV ILLDSKKKLA
     CGAVLIHVSW VLTAAHCMEE PKKLFVRLGE YDLRRKERWE LDLNIQEVLI HPNYSRSTTD
     NDIALLRLAQ PATLSQTIVP ICLPDNGLAE RELMQAGQET VVTGWGYHSS REKEAKRNRT
     FILNFITVPV APQNECEQVM SNIISENMLC AGILGDRRDA CDGDSGGPMV ASFRGTWFLV
     GLVSWGEGCG DLNNYGVYTK VSRYLDWIHS HIEEKEAAPE SPAP
//

If you have problems or comments...

PBIL Back to PBIL home page