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Database: UniProt
Entry: Q5R537
LinkDB: Q5R537
Original site: Q5R537 
ID   THRB_PONAB              Reviewed;         623 AA.
AC   Q5R537;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Prothrombin;
DE            EC=3.4.21.5;
DE   AltName: Full=Coagulation factor II;
DE   Contains:
DE     RecName: Full=Activation peptide fragment 1;
DE   Contains:
DE     RecName: Full=Activation peptide fragment 2;
DE   Contains:
DE     RecName: Full=Thrombin light chain;
DE   Contains:
DE     RecName: Full=Thrombin heavy chain;
DE   Flags: Precursor;
GN   Name=F2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys,
CC       converts fibrinogen to fibrin and activates factors V, VII, VIII,
CC       XIII, and, in complex with thrombomodulin, protein C. Functions in
CC       blood homeostasis, inflammation and wound healing (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to
CC         form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
CC       chain; disulfide-linked. Forms a heterodimer with SERPINA5 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions,
CC       result from the carboxylation of glutamyl residues by a microsomal
CC       enzyme, the vitamin K-dependent carboxylase. The modified residues
CC       are necessary for the calcium-dependent interaction with a
CC       negatively charged phospholipid surface, which is essential for
CC       the conversion of prothrombin to thrombin (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Prothrombin is activated on the surface of a
CC       phospholipid membrane that binds the amino end of prothrombin and
CC       factors Va and Xa in Ca-dependent interactions; factor Xa removes
CC       the activation peptide and cleaves the remaining part into light
CC       and heavy chains. The activation process starts slowly because
CC       factor V itself has to be activated by the initial, small amounts
CC       of thrombin (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
CC       (fragment 1) of the prothrombin, prior to its activation by factor
CC       Xa. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; CR861038; CAH93129.1; -; mRNA.
DR   RefSeq; NP_001126851.1; NM_001133379.1.
DR   SMR; Q5R537; -.
DR   STRING; 9601.ENSPPYP00000003807; -.
DR   MEROPS; S01.217; -.
DR   PRIDE; Q5R537; -.
DR   GeneID; 100173859; -.
DR   KEGG; pon:100173859; -.
DR   CTD; 2147; -.
DR   eggNOG; ENOG410IKPN; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   InParanoid; Q5R537; -.
DR   KO; K01313; -.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:InterPro.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   CDD; cd00108; KR; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.20.10; -; 2.
DR   Gene3D; 4.10.140.10; -; 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; 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:SF10; PTHR24254:SF10; 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; PR01505; PROTHROMBIN.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00130; KR; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 2.
DR   SUPFAM; SSF57630; SSF57630; 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   2: Evidence at transcript level;
KW   Acute phase; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Kringle; Protease; Reference proteome; Repeat; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25     43       {ECO:0000250}.
FT                                /FTId=PRO_0000028171.
FT   CHAIN        44    623       Prothrombin.
FT                                /FTId=PRO_0000028172.
FT   PEPTIDE      44    199       Activation peptide fragment 1.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000028173.
FT   PEPTIDE     200    328       Activation peptide fragment 2.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000028174.
FT   CHAIN       329    364       Thrombin light chain. {ECO:0000250}.
FT                                /FTId=PRO_0000028175.
FT   CHAIN       365    622       Thrombin heavy chain. {ECO:0000250}.
FT                                /FTId=PRO_0000028176.
FT   DOMAIN       44     90       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN      108    187       Kringle 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      213    292       Kringle 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      365    619       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION      552    574       High affinity receptor-binding region
FT                                which also known as the TP508 peptide.
FT                                {ECO:0000250}.
FT   ACT_SITE    407    407       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    463    463       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    569    569       Charge relay system. {ECO:0000250}.
FT   SITE        199    200       Cleavage; by thrombin. {ECO:0000250}.
FT   SITE        328    329       Cleavage; by factor Xa. {ECO:0000250}.
FT   SITE        364    365       Cleavage; by factor Xa. {ECO:0000250}.
FT   MOD_RES      50     50       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      51     51       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      58     58       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      63     63       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      64     64       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      69     69       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      70     70       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      73     73       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00735,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     61     66       {ECO:0000250}.
FT   DISULFID     91    104       {ECO:0000250}.
FT   DISULFID    109    187       {ECO:0000250}.
FT   DISULFID    130    170       {ECO:0000250}.
FT   DISULFID    158    182       {ECO:0000250}.
FT   DISULFID    214    292       {ECO:0000250}.
FT   DISULFID    235    275       {ECO:0000250}.
FT   DISULFID    263    287       {ECO:0000250}.
FT   DISULFID    337    483       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    392    408       {ECO:0000250}.
FT   DISULFID    537    551       {ECO:0000250}.
FT   DISULFID    565    595       {ECO:0000250}.
SQ   SEQUENCE   623 AA;  70010 MW;  6E89738B07AA8F87 CRC64;
     MAHVRGLQLP GCLALAALCT LVHSQHVFLA PQQALSLLQR VRRANSVFLE EVRKGNLERE
     CVEETCSYEE AFEALESSTA TDVFWAKYTA CETARTPRDK LAACLEGNCA EGLGTNYRGH
     LNITQSGIQC QLWRSRYPHK PEINSTTHPG ADLQENFCRN PDSSTTGPWC YTTDPTVRRQ
     ECSIPVCGQD QVTVAMTPRS EGSGVNLSPP SEQCVPDRGQ QYQGRLAVTT HGLPCLAWAS
     AQAKALSKHQ DFNSAVQLVE NFCRNPDGDE EGVWCYVAGK PGDFGYCDLN YCEEAMEEET
     GGGLDEDPDR AIEGRTATSE YQTFFDPRTF GSGEADCGLR PLFEKKSLED KTERELLESY
     IDGRIVEGSD AEIGMSPWQV MLFRKSPQEL LCGATLISDR WVLTAAHCLL YPPWDKNFTE
     NDLLVRIGKH SRTRYERNIE KISMLEKIYI HPRYNWRENL DRDIALMKLK KPVAFSDYIH
     PVCLPDRETA ASLLQAGYKG RVTGWGNLKE TWTANVGKVQ PSVLQVVNLP IVERPVCKDS
     TRIRITDNMF CAGYKPDEGK RGDACEGDSG GPFVMKSPFN NCWYQMGIVS WGEGCDRDGK
     YGFYTHVFRL KKWIQKVIDQ FGE
//
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