ID A0A2I0MNE5_COLLI Unreviewed; 609 AA.
AC A0A2I0MNE5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|EMBL:PKK31196.1};
GN ORFNames=A306_00001919 {ECO:0000313|EMBL:PKK31196.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK31196.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK31196.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK31196.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK31196.1}.
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DR EMBL; AKCR02000005; PKK31196.1; -; Genomic_DNA.
DR RefSeq; XP_005502232.1; XM_005502175.1.
DR AlphaFoldDB; A0A2I0MNE5; -.
DR STRING; 8932.A0A2I0MNE5; -.
DR GeneID; 102087936; -.
DR KEGG; clv:102087936; -.
DR CTD; 2147; -.
DR InParanoid; A0A2I0MNE5; -.
DR OrthoDB; 211181at2759; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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; 4.10.740.10; Coagulation Factor IX; 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; IPR017857; Coagulation_fac-like_Gla_dom.
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:UP000053872};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..609
FT /note="Prothrombin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014132062"
FT DOMAIN 44..90
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 108..185
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 206..284
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 347..605
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 394
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 450
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1"
FT ACT_SITE 555
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..104
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 109..185
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 130..168
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 156..180
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 207..284
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4,
FT ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 228..268
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 256..279
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4,
FT ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 324..470
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 379..395
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 523..537
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
FT DISULFID 551..581
FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SQ SEQUENCE 609 AA; 68991 MW; CB5EF7025822F70F CRC64;
MAHNKTGVLR GLLLSSLLHL TLGHAGVFLE KGQALSLLKR PRRANKGFLE EMLKGNLERE
CLEETCNYEE AFEALESTVQ TEAFWSKYQV CQDIRKSRTA LDACLEGNCS LGLGENYRGT
ISYTKSGIEC QVWTSKYPHI PKYNATIYPN LIENYCRNPD NNSQGPWCYT RDPTVEREEC
PIPVCGEERT TVEFTPRVTP SAPVEPCEQE KGMLYTGTLS VTVSGAKCLP WNSEKAKEVL
HGKHIDPEVK LLENYCRNPD GDDEGVWCVT DEAPHFEYCD LQYCDSSLED GNEPSEGISG
RTTLPQEFKT FFDDQTFGSG EADCGTRPLF EKKKITDKSE KELLESYIGG RVVHGDDAEV
GSSPWQVMLY KKSPQELLCG ASLISDSWVL TAAHCLYYPP WDKNLTTNDI LVRIGKHMRA
KYEKNKERIA LLDKIIIHPK YNWKENMDRD IALMHLKRPV IFSDYIHPVC LPTKEVVQRL
MLAGYKGRVT GWGNLKETWA TSPSNLPTVL QQLNVPIVDQ DTCKASTKVK VTDNMFCAGY
SPEDSKRGDA CEGDSGGPFV MKNPDDNRWY QVGIVSWGEG CDRDGKYGFY THVFRLKKWM
RKVIEKHGR
//
