ID Q5NVS1_PONAB Unreviewed; 427 AA.
AC Q5NVS1;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Prothrombin {ECO:0000256|ARBA:ARBA00014840};
DE EC=3.4.21.5 {ECO:0000256|ARBA:ARBA00012174};
DE AltName: Full=Coagulation factor II {ECO:0000256|ARBA:ARBA00032835};
GN Name=DKFZp470K2111 {ECO:0000313|EMBL:CAI29592.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|EMBL:CAI29592.1};
RN [1] {ECO:0000313|EMBL:CAI29592.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:CAI29592.1};
RG The German cDNA Consortium;
RA Poustka A., Albert R., Moosmayer P., Schupp I., Wellenreuther R.,
RA Mewes H.W., Weil B., Amid C., Osanger A., Fobo G., Han M., Wiemann S.;
RL Submitted (NOV-2004) 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 -!- 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR925932; CAI29592.1; -; mRNA.
DR RefSeq; NP_001126851.1; NM_001133379.1.
DR AlphaFoldDB; Q5NVS1; -.
DR MEROPS; S01.217; -.
DR GeneID; 100173859; -.
DR KEGG; pon:100173859; -.
DR CTD; 2147; -.
DR OrthoDB; 211181at2759; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 2.
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; 1.
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; IPR018992; Thrombin_light_chain.
DR InterPro; IPR037111; Thrombin_light_chain_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
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 PRINTS; PR00001; GLABLOOD.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00130; KR; 2.
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; PS00134; TRYPSIN_HIS; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..427
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004261037"
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"
SQ SEQUENCE 427 AA; 47421 MW; C51F9FE3DD2C3304 CRC64;
MAHVRGLQLP GCLALAALCT LVHSQHVFLA PQQALSLLQR VRRANSVFLE EMRKGNLERE
CVEETCSYEE AFEALESSTA TDVFWAKYTA CETARTPRDK LAVCLEGNCA EGLGTNYRGH
VNITQSGIEC QLWRSRYPHK PEINSTTHPG ADLQENFCRN PDSSTTGPWC YTTDPTVRRQ
ECSIPVCGQD QVTVAMTPRS EGSGVNLSPP SEQCVPDRGQ QYQGHLAVTT HGLPCLAWAS
AQAKALSKHQ DFNSAVQLVE NFCRNPDGDE EGVWCYVAGK PGDFGYCDLN YCEEAMEEET
GGGLDEDPDR AIEGRTATSE YQTFFDPRTF GSGEADCGLR PLFEKKSLED KTERELLESY
IDGRIVEGSD AEIGMSPWQV MLFRKSPQEL LCGATLISDR WVLTAAHCHP APPTRHVYLS
FFPHLHQ
//
