ID A0A2K6L8F3_RHIBE Unreviewed; 567 AA.
AC A0A2K6L8F3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=F2 {ECO:0000313|Ensembl:ENSRBIP00000019814.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000019814.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000019814.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000019814.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- 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 RefSeq; XP_017717472.1; XM_017861983.1.
DR AlphaFoldDB; A0A2K6L8F3; -.
DR Ensembl; ENSRBIT00000043692.1; ENSRBIP00000019814.1; ENSRBIG00000033898.1.
DR GeneID; 108521952; -.
DR KEGG; rbb:108521952; -.
DR CTD; 2147; -.
DR GeneTree; ENSGT00940000154234; -.
DR OMA; VMIFRKS; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000233180; Unplaced.
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: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:InterPro.
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; 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; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR PRINTS; PR00018; KRINGLE.
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; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486};
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 ECO:0000256|PIRSR:PIRSR001149-4};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
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 Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..567
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014412061"
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 389..563
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT SITE 199..200
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
FT SITE 328..329
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
FT SITE 364..365
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-2"
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 337..427
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 481..495
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 509..539
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 567 AA; 63602 MW; 24E4B7B802C8B087 CRC64;
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQALSLLQR VRRANSIFLE EVLKGNLERE
CVEETCSYEE AFEALESPTA TDAFWAKYTA CETARTSRDT LAACLEGNCA EGLGMNYRGH
VNITWSGTEC QLWRSRYPHK PEINSTTHPG ADLQENFCRN PDGSTTGPWC YTTDPTVRRE
ECSIPVCGQN QVTVAMTPRS RGASENLSPP SEQCVPDRGR QYQGSLAVTT HGLPCLAWAS
AQAKALSKHQ DFNSAVQLVE NFCRNPDGDE EGVWCYVAGK PGDFEYCDLN YCEEAVDEET
GDGLGEDPDR AIEGRTATSE YQTFFDPRTF GLGEADCGLR PLFEKKSLED KTEGELLESY
IDGRIVEGWD AEIGMSPWYE RNIEKISMLE KIHIHPRYNW RENLDRDIAL MKLKKPVTFS
DYIHPVCLPD RETAASLFQA GYKGRVTGWG NLKETWTANV GKVQPSVLQV VNLPIVERSV
CKDSTRIRIT DNMFCAGYKP DEGKRGDACE GDSGGPFVMK NPFNKRWYQM GIVSWGEGCD
RDGKYGFYTH VFRLKKWIKK VTDEFGD
//
