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Database: UniProt
Entry: P98139
LinkDB: P98139
Original site: P98139 
ID   FA7_RABIT               Reviewed;         444 AA.
AC   P98139; P79224;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   16-JAN-2019, entry version 144.
DE   RecName: Full=Coagulation factor VII;
DE            EC=3.4.21.21;
DE   AltName: Full=Serum prothrombin conversion accelerator;
DE   Contains:
DE     RecName: Full=Factor VII light chain;
DE   Contains:
DE     RecName: Full=Factor VII heavy chain;
DE   Flags: Precursor;
GN   Name=F7;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8383365; DOI=10.1016/0049-3848(93)90048-S;
RA   Brothers A.B., Clarke B.J., Sheffield W.P., Blajchman M.A.;
RT   "Complete nucleotide sequence of the cDNA encoding rabbit coagulation
RT   factor VII.";
RL   Thromb. Res. Suppl. 69:231-238(1993).
RN   [2]
RP   SEQUENCE REVISION TO 395.
RC   TISSUE=Liver;
RA   Ruiz S.R., Blajchman M.A., Clarke B.J.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation.
CC       Serine protease that circulates in the blood in a zymogen form.
CC       Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
CC       factor IXa, or thrombin by minor proteolysis. In the presence of
CC       tissue factor and calcium ions, factor VIIa then converts factor X
CC       to factor Xa by limited proteolysis. Factor VIIa will also convert
CC       factor IX to factor IXa in the presence of tissue factor and
CC       calcium (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC         factor Xa.; EC=3.4.21.21;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
CC       a disulfide bond. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC       {ECO:0000250}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine
CC       or threonine residue found in the consensus sequence C2-X(4,5)-
CC       [S/T]-C3 of EGF domains, where C2 and C3 are the second and third
CC       conserved cysteines. {ECO:0000250}.
CC   -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-91 by
CC       POGLUT1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U77477; AAB37326.1; -; mRNA.
DR   PIR; I46932; I46932.
DR   RefSeq; NP_001076148.1; NM_001082679.1.
DR   UniGene; Ocu.2617; -.
DR   ProteinModelPortal; P98139; -.
DR   SMR; P98139; -.
DR   STRING; 9986.ENSOCUP00000024648; -.
DR   BindingDB; P98139; -.
DR   ChEMBL; CHEMBL3351187; -.
DR   GeneID; 100009399; -.
DR   KEGG; ocu:100009399; -.
DR   CTD; 2155; -.
DR   eggNOG; ENOG410IIMB; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P98139; -.
DR   KO; K01320; -.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR033190; F7.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR44064:SF1; PTHR44064:SF1; 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; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
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.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   PROPEP       22     39       {ECO:0000255}.
FT                                /FTId=PRO_0000027735.
FT   CHAIN        40    191       Factor VII light chain.
FT                                /FTId=PRO_0000027736.
FT   CHAIN       192    444       Factor VII heavy chain.
FT                                /FTId=PRO_0000027737.
FT   DOMAIN       40     84       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       85    121       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      126    167       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      192    431       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    232    232       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    281    281       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    383    383       Charge relay system. {ECO:0000250}.
FT   BINDING     377    377       Substrate. {ECO:0000250}.
FT   SITE        191    192       Cleavage; by factor Xa, factor XIIa,
FT                                factor IXa, or thrombin. {ECO:0000250}.
FT   MOD_RES      45     45       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      46     46       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      53     53       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      55     55       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      58     58       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      59     59       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      64     64       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      65     65       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      68     68       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      74     74       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     102    102       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD     91     91       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250}.
FT   CARBOHYD     91     91       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250}.
FT   CARBOHYD     99     99       O-linked (Fuc) serine. {ECO:0000250}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    242    242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    306    306       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     56     61       {ECO:0000250}.
FT   DISULFID     89    100       {ECO:0000250}.
FT   DISULFID     94    109       {ECO:0000250}.
FT   DISULFID    111    120       {ECO:0000250}.
FT   DISULFID    130    141       {ECO:0000250}.
FT   DISULFID    137    151       {ECO:0000250}.
FT   DISULFID    153    166       {ECO:0000250}.
FT   DISULFID    174    301       {ECO:0000250}.
FT   DISULFID    198    203       {ECO:0000250}.
FT   DISULFID    217    233       {ECO:0000250}.
FT   DISULFID    349    368       {ECO:0000250}.
FT   DISULFID    379    407       {ECO:0000250}.
SQ   SEQUENCE   444 AA;  49011 MW;  0481ABC4FE5427F8 CRC64;
     MAPQARGLGL CSLLALQASL AAVFITQEEA HSVLRRQRRA NSFLEELRPG SLERECKEEL
     CSFEEAREVF QSTERTKQFW ITYNDGDQCA SNPCQNGGSC EDQIQSYICF CLADFEGRNC
     EKNKNDQLIC MYENGGCEQY CSDHVGSQRS CRCHEGYTLL PNGVSCTPTV DYPCGKVPAL
     EKRGASNPQG RIVGGKVCPK GECPWQAALM NGSTLLCGGS LLDTHWVVSA AHCFDKLSSL
     RNLTIVLGEH DLSEHEGDEQ VRHVAQLIMP DKYVPGKTDH DIALLRLLQP AALTNNVVPL
     CLPERNFSES TLATIRFSRV SGWGQLLYRG ALARELMAID VPRLMTQDCV EQSEHKPGSP
     EVTGNMFCAG YLDGSKDACK GDSGGPHATS YHGTWYLTGV VSWGEGCAAV GHVGVYTRVS
     RYTEWLSRLM RSKLHHGIQR HPFP
//
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