ID D9U8F9_PLEAT Unreviewed; 616 AA.
AC D9U8F9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=thrombin {ECO:0000313|EMBL:CBD77420.1};
OS Plecoglossus altivelis (Ayu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Stomiati; Osmeriformes;
OC Plecoglossus.
OX NCBI_TaxID=61084 {ECO:0000313|EMBL:CBD77420.1};
RN [1] {ECO:0000313|EMBL:CBD77420.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:CBD77420.1};
RA Shi Y.H., Yang H.Y., Lu X.J., Chen J.;
RT "Molecular cloning and sequence analysis of thrombin gene in Plecoglossus
RT altivelis.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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 EMBL; FN547920; CBD77420.1; -; mRNA.
DR AlphaFoldDB; D9U8F9; -.
DR SMR; D9U8F9; -.
DR MEROPS; S01.217; -.
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: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; 4.10.740.10; Coagulation Factor IX; 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; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
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 2: Evidence at transcript level;
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 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..616
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003129334"
FT DOMAIN 41..87
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 110..187
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 210..289
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 356..609
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 398
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 454
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 559
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..187
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 132..170
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 158..182
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 211..289
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 232..272
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 260..284
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 328..474
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 383..399
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 527..541
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 555..585
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 616 AA; 69985 MW; 56632239FE4ECDE0 CRC64;
MANLTPSLLL TLLLSGLQIT LCDDVFLDNK KASQVFVRAR RANSLFEEVK PGNLERECIE
EICDHEEARE VFERTDLTTA FWLTYQDCKG TSLKRTTDNI QMVKKCVDGK CVVGTGLNYK
GNVSYTSSGK QCQYWRSNFP HLVEFNATVD KSLQENFCRN PDSSSKGPWC YTRDPTVKRE
HCTVPICGKV FVPAPPPPVQ NVNMYAQKKD CLSNNGVDYV GTLSTTLQAR TCLSWSDPSV
QARIKDKSFI PEVKLEKNHC RNPDEDPEGP WCFVKNNGTT IEYCDLELCD NPIDEYQDST
GGKERTVLSG PRKTFFSPRS FGNGEQVCGE RPMFEKVNKK DAKEQELLDS YRGSRIVKGL
DAEVASAPWQ VMLYKRSPQE LLCGASLISD EWILTAAHCI LYPPWNKNFT INDILVRLGK
HNRAKFERGI EKIVAIDEII VHPKYNWKEN LNRDIALLHL RQPIQFTDEI HPICMPSKKV
ANTLMFSGYK GRVTGWGNLK ETWSSNNKNL PTVLQQIHLP IVEQDTCRQS TSIRVTDNMF
CAGYKPDDTT RGDACEGDSG GPFVMKNPED NRWYQIGIVS WGEGCDRDGK YGFYTHLFRM
RKWMSKVIDK SGGDDD
//
