(data stored in ACNUC19913 zone)

HOGENOM: RAT16_PE860

ID   RAT16_PE860                          STANDARD;      PRT;   482 AA.
AC   RAT16_PE860; Q63207;
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=Coagulation factor X; EC=3.4.21 6;AltName: Full=Stuart
DE   factor;Contains: RecName: Full=Factor X light chain;Contains: RecName:
DE   Full=Factor X heavy chain;Contains: RecName: Full=Activated factor Xa
DE   heavy chain;Flags: Precursor; (RAT16.PE860).
GN   Name=F10;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT16.PE860.
CC       Rattus norvegicus chromosome 16 RGSC3.4  sequence 1..90238779
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA10_RAT
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then
CC       Arg-|-Ile bonds in prothrombin to form thrombin.
CC   -!- SUBUNIT: The two chains are formed from a single-chain precursor
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated (By similarity).
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway)
CC       (By similarity).
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   -!- 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:Rattus_norvegicus;ENSRNOG00000033444;ENSRNOT00000026677;ENSRNOP00000026677.
DR   EMBL; BC088151; - ;
DR   EMBL; D21215; - ;
DR   EMBL; X79807; - ;
DR   UniProtKB/Swiss-Prot; Q63207; -.
DR   EMBL; X79807; CAA56202.1; -; mRNA.
DR   EMBL; BC088151; AAH88151.1; -; mRNA.
DR   IPI; IPI00206786; -.
DR   PIR; S49075; EXRT.
DR   RefSeq; NP_058839.1; NM_017143.2.
DR   UniGene; Rn.21393; -.
DR   ProteinModelPortal; Q63207; -.
DR   SMR; Q63207; 42-86, 88-174, 232-473.
DR   STRING; Q63207; -.
DR   MEROPS; S01.216; -.
DR   PRIDE; Q63207; -.
DR   Ensembl; ENSRNOT00000026677; ENSRNOP00000026677; ENSRNOG00000033444.
DR   GeneID; 29243; -.
DR   KEGG; rno:29243; -.
DR   NMPDR; fig|10116.3.peg.12776; -.
DR   UCSC; NM_017143; rat.
DR   CTD; 2159; -.
DR   RGD; 61850; F10.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q63207; -.
DR   OrthoDB; EOG447FTB; -.
DR   PhylomeDB; Q63207; -.
DR   NextBio; 608522; -.
DR   ArrayExpress; Q63207; -.
DR   Genevestigator; Q63207; -.
DR   GermOnline; ENSRNOG00000033444; Rattus norvegicus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:RGD.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
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; PF00008; EGF; 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; 1.
DR   SMART; SM00179; EGF_CA; 1.
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; RAT16.PE860; -.
KW   ENSRNOG00000033444820036002503210000011;
KW   F10; F10m1Mcwi; F10m2Mcwi; FA10_RAT;
KW   BC088151; D21215; X79807;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal; Zymogen.
SQ   SEQUENCE   482 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MESPVRLSLL YVVLASLLLP GRSVFINRER ANNVLQRIRR ANSFFEEIKK GNLERECVEE
     ICSFEEAREV FEDNEKTTEF WNKYEDGDQC ESSPCQNQGE CRDGLGSYTC TCTEGFEGKN
     CELFVRKLCS LDNGDCDQFC REEQNSVVCS CAKGYFLGND GKSCLSTAPF PCGKTNKGRA
     KRSVALNTSN SEPDPEDLMP DADILYPTES PSELLNLNKT EPEANSDDVI RIVGGQECKR
     GECPWQALLF SDEETDGFCG GTILNEFYIL TAAHCLHQAK RFKVRVGDLN TEQEDGGEMV
     HEVDMIIKHN KFQRDTYDFD IAMLRLKTPI TFRENVAPAC LPQKDWAEAT LMTQKTGIVS
     GFGRTHEKGR QSKVLKMMEV PYVDRNTCRL STSFSITQNM FCAGYDAKQE DACQGDSGGP
     HVTRFKDTYF VTGIVSWGEG CARKGKYGIY TKVTAFLKWI DRSMKARVGP TSETPRLTHP
     PY
//

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