ID H7BX99_MOUSE Unreviewed; 617 AA.
AC H7BX99;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=F2 {ECO:0000313|Ensembl:ENSMUSP00000106967.2,
GN ECO:0000313|MGI:MGI:88380};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000106967.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000106967.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000106967.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000106967.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000106967.2};
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 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; H7BX99; -.
DR SMR; H7BX99; -.
DR GlyCosmos; H7BX99; 3 sites, No reported glycans.
DR jPOST; H7BX99; -.
DR MaxQB; H7BX99; -.
DR PeptideAtlas; H7BX99; -.
DR ProteomicsDB; 347107; -.
DR Antibodypedia; 857; 1316 antibodies from 42 providers.
DR Ensembl; ENSMUST00000111335.2; ENSMUSP00000106967.2; ENSMUSG00000027249.16.
DR AGR; MGI:88380; -.
DR MGI; MGI:88380; F2.
DR VEuPathDB; HostDB:ENSMUSG00000027249; -.
DR GeneTree; ENSGT00940000154234; -.
DR ChiTaRS; F2; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027249; Expressed in left lobe of liver and 54 other cell types or tissues.
DR ExpressionAtlas; H7BX99; baseline and differential.
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; 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; 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; 2.
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 1: Evidence at protein level;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486, ECO:0000256|PIRNR:PIRNR001149};
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR001149}; 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|ARBA:ARBA00022696, 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 Proteomics identification {ECO:0007829|EPD:H7BX99,
KW ECO:0007829|MaxQB:H7BX99};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..617
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003608421"
FT DOMAIN 44..90
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 108..187
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 213..292
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 360..614
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 458
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 564
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT SITE 199..200
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
FT SITE 323..324
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
FT SITE 359..360
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-3"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-3"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-3"
FT DISULFID 61..66
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 91..104
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 109..187
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 130..170
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 158..182
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 214..292
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 235..275
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 263..287
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 332..478
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 387..403
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 532..546
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 560..590
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 617 AA; 70212 MW; 0124E20F4AE45164 CRC64;
MSHVRGLGLP GCLALAALVS LVHSQHVFLA PQQALSLLQR VRRANSGFLE ELRKGNLERE
CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET FMDCLEGRCA MDLGVNYLGT
VNVTHTGIQC QLWRSRYPHK PEINSTTHPG ADLKENFCRN PDSSTTGPWC YTTDPTVRRE
ECSVPVCQEG RTTVVMTPRS GGSKDNLSPP LGQCLTERGR LYQGNLAVTT LGSPCLPWNS
LPAKTLSKYQ DFDPEVKLVE NFCRNPDWDE EGAWCYVAGQ PGDFEYCNLN YCEEAVGEEN
YDVDESIAGR TTDAEFHTFF NEKTFGLGEA DCGLRPLFEK KSLKDTTEKE LLDSYIDGRI
VEGWDAEKGI APWQVMLFRK SPQELLCGAS LISDRWVLTA AHCILYPPWD KNFTENDLLV
RIGKHSRTRY ERNVEKISML EKIYVHPRYN WRENLDRDIA LLKLKKPVPF SDYIHPVCLP
DKQTVTSLLR AGYKGRVTGW GNLRETWTTN INEIQPSVLQ VVNLPIVERP VCKASTRIRI
TDNMFCAGFK VNDTKRGDAC EGDSGGPFVM KSPFNNRWYQ MGIVSWGEGC DRKGKYGFYT
HVFRLKRWIQ KVIDQFG
//
