ID A0A3B3IJN6_ORYLA Unreviewed; 617 AA.
AC A0A3B3IJN6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Prothrombin {ECO:0000256|ARBA:ARBA00014840, ECO:0000256|PIRNR:PIRNR001149};
DE EC=3.4.21.5 {ECO:0000256|ARBA:ARBA00012174, ECO:0000256|PIRNR:PIRNR001149};
DE AltName: Full=Coagulation factor II {ECO:0000256|ARBA:ARBA00032835, ECO:0000256|PIRNR:PIRNR001149};
GN Name=LOC101170246 {ECO:0000313|Ensembl:ENSORLP00000044059.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000044059.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000044059.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000044059.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000044059.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000044059.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts
CC fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in
CC complex with thrombomodulin, protein C. Functions in blood homeostasis,
CC inflammation and wound healing. {ECO:0000256|ARBA:ARBA00025390,
CC ECO:0000256|PIRNR:PIRNR001149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
CC fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001621,
CC ECO:0000256|PIRNR:PIRNR001149};
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000256|ARBA:ARBA00008850}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001149}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; A0A3B3IJN6; -.
DR Ensembl; ENSORLT00000035693.1; ENSORLP00000044059.1; ENSORLG00000019844.2.
DR GeneTree; ENSGT00940000164059; -.
DR Proteomes; UP000001038; Chromosome 2.
DR Bgee; ENSORLG00000019844; Expressed in liver and 13 other cell types or tissues.
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:UniProtKB-EC.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 4.10.140.10; Thrombin light chain domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR003966; Prothrombin/thrombin.
DR InterPro; IPR018992; Thrombin_light_chain.
DR InterPro; IPR037111; Thrombin_light_chain_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24254; PROTHROMBIN; 1.
DR PANTHER; PTHR24254:SF10; PROTHROMBIN; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF09396; Thrombin_light; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001149; Thrombin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR01505; PROTHROMBIN.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486, ECO:0000256|PIRNR:PIRNR001149};
KW Blood coagulation {ECO:0000256|PIRNR:PIRNR001149};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001149-4};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Hemostasis {ECO:0000256|PIRNR:PIRNR001149};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001149};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001149};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001149,
KW ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..617
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017211264"
FT DOMAIN 41..87
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 110..190
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 208..288
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 357..610
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT DISULFID 58..63
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 88..106
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 111..190
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 132..173
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 161..185
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 209..288
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 230..270
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 258..283
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 329..475
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 384..400
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 528..542
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 617 AA; 70295 MW; 57E58F65E39A1DAB CRC64;
MVEPTLRTSA VVLLLILHNC AANHVFLKGQ QASQVLVRNP RANQMFEELK PGNLERECFE
EICDHEEARE VFEQTDKTEI FWAKYLDCEG TVKHRTTKTI GLIRDCVEGH CVSGNGHNYN
GNIHITKSGR VCQHWSHSFP HPIFREFNAS EPNSILQENF CRNPDKRSEG PWCFTKDPSV
QKETCRVPKC GEKFVPPTVA PEVVKTTICL PNYGVDYTGD LSVTLGGHTC IQWSSPQAKA
LSKDKEFIPE VQLTGNKCRN PDNDPEGPWC YVHISGNITV DYCDLDLCED PLLAQEQETE
TEGRERSVLA PAKKLFFNPR TFGEGESSCG LRPLFELKSK KDAKEQELLD SYREQRIVGG
DDAEVASAPW QVMLYKRSPQ ELLCGASLIS DQWIVTAAHC VLYPPWNKNL TTEDILVRLG
KHNRAKFERG VEKIVAIDEI IVHPKYDWKQ NLNRDVALLH LRRPITFSDE IYPICLPNKQ
VARNLMMQGY KGRVTGWGNL KESWNPAARN LPTVLQQIHL PIVDQEICRQ STSVRVTDNM
FCAGFKPDDS QRGDACEGDS GGPFVMKHPG ENRWYQIGIV WWRQGYDRNG IYGFYTHLFR
MGRWIKKVIE KSGADDE
//
