ID H3BHN3_LATCH Unreviewed; 618 AA.
AC H3BHN3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSLACP00000021404.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000021404.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000021404.1}
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 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; AFYH01005331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BHN3; -.
DR STRING; 7897.ENSLACP00000021404; -.
DR Ensembl; ENSLACT00000021545.1; ENSLACP00000021404.1; ENSLACG00000018806.2.
DR eggNOG; ENOG502QTSX; Eukaryota.
DR GeneTree; ENSGT00940000164059; -.
DR InParanoid; H3BHN3; -.
DR OMA; VMIFRKS; -.
DR TreeFam; TF327329; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000018806; Expressed in chordate pharynx and 1 other cell type or tissue.
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; 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; 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 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:UP000008672};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..618
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003581389"
FT DOMAIN 44..90
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 112..193
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 217..296
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 365..618
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 568
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT DISULFID 61..66
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 91..108
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 113..193
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 134..176
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 164..188
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 218..296
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 239..279
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 267..291
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 337..483
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 392..408
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 536..550
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 564..594
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 618 AA; 69926 MW; 106400B0853875A9 CRC64;
LVHSNVLQIK GMLPLAALLY LICTPPPVFL DSREAHLVLQ RHRRANQLFE EVKNGDLERE
CFEEVCSKEE AREVFEDTDA TEKFWTRYLD CDGTTSSRGR DKVKLEICLN VYCAEGNGAN
YLGDIAVTKS GKECQFWSSN FPHKINFNST LGPSLIRVKS KNYCRNPDGN PKGPWCFTRD
PMTRTEECAI PVCGENRTTS VHTPLLKPKV PASNAKDCIP DQGLDYQGKL AVTISGLKCM
AWNSPQVKEL SKDKNFMPEV KLVENFCRNP DGDDEGLWCF VDQDNKTFEY CPVTYCETTT
TTTNNNKKEE TLAGRTTTGE HKLFFNPKYF GQGENGCGLR PLFEEKNIED NGEKELLESY
IGGRIVGGED AQVGSSPWQV MLFKKSPQEL LCGASLISDE WVLTAAHCLL YPPWDKNFTS
SDILVRVGKH SRARYEMDAE RITAVDKIYI HPGYDWRTNL NRDIALLHLK RPISFSDRIR
PVCLPNKDVI QTLWFSGFLG RVTGWGLLKN TWSRKPGSLP GVLQQVSLPL VDQSVCRAST
SIPITKNMFC AGYHKDADRR GDACEGDSGG PFVMKNPNNN RWYQVGIVSW GEGCDQDGKY
GFYTHTFRMM RWIKKTIE
//
