ID G3PRY9_GASAC Unreviewed; 615 AA.
AC G3PRY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020375.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000020375.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000020375.1}
RP IDENTIFICATION.
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; G3PRY9; -.
DR MEROPS; S01.217; -.
DR Ensembl; ENSGACT00000020414.1; ENSGACP00000020375.1; ENSGACG00000015448.1.
DR GeneTree; ENSGT00940000164059; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000015448; Expressed in liver and 2 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; 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; 3.
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 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:UP000007635};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001149,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 41..87
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 107..187
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 207..287
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 108..187
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 129..170
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 158..182
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 208..287
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 229..269
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 257..282
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 615 AA; 69419 MW; 1C3FF2AE054EFA85 CRC64;
VSPLDTISRC VLLVSSTAVC WLSQIFLNSQ LATQLLPRSR RANQMFEEIK PGNLERECVE
EICDHEEARE VFEQTEKTEN FWTKYLVSDC KGTQMTRTQH NINIVRQCVE GSGVNYEGNI
NITQSGRKCQ PWSSSYPHPI FREFNASEPN SILLENFCRN PDSRPEGPWC FTKDPAVPKE
TCRVPTCGKG QDFVPPTVAP EPTRTAACLL NYGVDYVGDL SVTLGGHTCL QWSSREAKAL
SVDKDFIPEV GLPGNKCRNP DNDPEGPWCY VELSGNVTID YCDLELCEDL VTEDVLTTDT
EGQERSVLKP ARKTFFSPRT FGEGESVCGE RPLFEKLKKK DRNEAELLES YRQERIVGGD
DAEVASAPWQ VMLYKRSPQE LLCGASLISD QWIVTAAHCI LYPPWNKNFS ASDILVRLGK
HNRAAFERGI EKIVAISEII VHPKYNWKEN LNRDVALLHL RRPVGFTDAI HPICLPNRKV
ATALMTQGYK GRVTGWGNLK DTWNPSARNL PEVLQQIHLP IVDQDVCSSS TSVKVTDNMF
CAGYKPDDAK RGDACEGDSG GPFVMKYPAD DRWYQMGIVS WGEGCDKDGK YGFYTHLFRM
NRWMRKIIEK TGKDD
//
