GenomeNet

Database: UniProt
Entry: P16293
LinkDB: P16293
Original site: P16293 
ID   FA9_PIG                 Reviewed;         409 AA.
AC   P16293; Q28994;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAY-2019, entry version 157.
DE   RecName: Full=Coagulation factor IX;
DE            EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740};
DE   AltName: Full=Christmas factor;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa light chain;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa heavy chain;
DE   Flags: Precursor; Fragment;
GN   Name=F9;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-146.
RC   TISSUE=Liver;
RA   Lollar P.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 139-409.
RX   PubMed=2303254; DOI=10.1016/0888-7543(90)90458-7;
RA   Sarkar G., Koeberl D.D., Sommer S.S.;
RT   "Direct sequencing of the activation peptide and the catalytic domain
RT   of the factor IX gene in six species.";
RL   Genomics 6:133-143(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-245.
RC   STRAIN=Meishan, and Wild boar;
RX   PubMed=8856916;
RA   Signer E.N., Armour J.A.L., Jeffreys A.J.;
RT   "Detection of an MboI RFLP at the porcine clotting factor IX locus and
RT   verification of sex linkage.";
RL   Anim. Genet. 27:130-130(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-12.
RX   PubMed=3322404; DOI=10.1021/bi00398a015;
RA   Lollar P., Parker C.G., Kajenski P.J., Litwiller R.D., Fass D.N.;
RT   "Degradation of coagulation proteins by an enzyme from Malayan pit
RT   viper (Akistrodon rhodostoma) venom.";
RL   Biochemistry 26:7627-7636(1987).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
RP   DISULFIDE BOND, AND SUBUNIT.
RX   PubMed=7568220; DOI=10.1073/pnas.92.21.9796;
RA   Brandstetter H., Bauer M., Huber R., Lollar P., Bode W.;
RT   "X-ray structure of clotting factor IXa: active site and module
RT   structure related to Xase activity and hemophilia B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:9796-9800(1995).
CC   -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
CC       participates in the intrinsic pathway of blood coagulation by
CC       converting factor X to its active form in the presence of Ca(2+)
CC       ions, phospholipids, and factor VIIIa.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC         factor Xa.; EC=3.4.21.22;
CC         Evidence={ECO:0000250|UniProtKB:P00740};
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked. Interacts with SERPINC1.
CC       {ECO:0000269|PubMed:7568220}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
CC   -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
CC       residues in the Gla domain. Calcium can also bind, with stronger
CC       affinity, to another site beyond the Gla domain. Under
CC       physiological ion concentrations, Ca(2+) is displaced by Mg(2+)
CC       from some of the gammaglutamate residues in the N-terminal Gla
CC       domain. This leads to a subtle conformation change that may affect
CC       the interaction with its binding protein.
CC       {ECO:0000250|UniProtKB:P00741}.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide. The propeptide can also be removed by snake venom
CC       protease. {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; U51135; AAA96318.1; -; mRNA.
DR   EMBL; M26235; AAA31031.1; -; mRNA.
DR   EMBL; X92427; CAA63155.1; -; Genomic_DNA.
DR   EMBL; X92593; CAA63337.1; -; Genomic_DNA.
DR   PIR; I46580; I46580.
DR   PDB; 1PFX; X-ray; 3.00 A; C=183-409, L=8-147.
DR   PDB; 1X7A; X-ray; 2.90 A; C=183-409, L=1-147.
DR   PDBsum; 1PFX; -.
DR   PDBsum; 1X7A; -.
DR   SMR; P16293; -.
DR   STRING; 9823.ENSSSCP00000013514; -.
DR   MEROPS; S01.214; -.
DR   PeptideAtlas; P16293; -.
DR   PRIDE; P16293; -.
DR   InParanoid; P16293; -.
DR   EvolutionaryTrace; P16293; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR035694; Coagulation_factor_IX.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Magnesium; Metal-binding; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Sulfation;
KW   Zymogen.
FT   CHAIN         1    409       Coagulation factor IX.
FT                                /FTId=PRO_0000027770.
FT   CHAIN         1    147       Coagulation factor IXa light chain.
FT                                /FTId=PRO_0000027771.
FT   PROPEP      148    182       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000027772.
FT   CHAIN       183    409       Coagulation factor IXa heavy chain.
FT                                /FTId=PRO_0000027773.
FT   DOMAIN        1     47       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       48     84       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN       85    126       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      183    409       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    223    223       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    271    271       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    367    367       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         1      1       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         2      2       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         7      7       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         7      7       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         8      8       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL         8      8       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        16     16       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        18     18       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        18     18       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        18     18       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        21     21       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        22     22       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        27     27       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        28     28       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        28     28       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        31     31       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        31     31       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        37     37       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        41     41       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        48     48       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        49     49       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        51     51       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        65     65       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        66     66       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       237    237       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       239    239       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       242    242       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       244    244       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       247    247       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        147    148       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        182    183       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES       7      7       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES       8      8       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      16     16       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      18     18       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      21     21       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      22     22       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      27     27       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      28     28       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      31     31       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      34     34       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      37     37       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      41     41       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      65     65       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES      69     69       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     157    157       Sulfotyrosine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     160    160       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     161    161       Phosphothreonine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    161    161       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    171    171       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    262    262       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     19     24       {ECO:0000269|PubMed:7568220}.
FT   DISULFID     52     63       {ECO:0000269|PubMed:7568220}.
FT   DISULFID     57     72       {ECO:0000269|PubMed:7568220}.
FT   DISULFID     74     83       {ECO:0000269|PubMed:7568220}.
FT   DISULFID     89    100       {ECO:0000269|PubMed:7568220}.
FT   DISULFID     96    110       {ECO:0000269|PubMed:7568220}.
FT   DISULFID    112    125       {ECO:0000269|PubMed:7568220}.
FT   DISULFID    133    291       Interchain (between light and heavy
FT                                chains). {ECO:0000269|PubMed:7568220}.
FT   DISULFID    208    224       {ECO:0000269|PubMed:7568220}.
FT   DISULFID    338    352       {ECO:0000269|PubMed:7568220}.
FT   DISULFID    363    391       {ECO:0000269|PubMed:7568220}.
FT   NON_TER       1      1
FT   STRAND        4      6       {ECO:0000244|PDB:1PFX}.
FT   HELIX        15     18       {ECO:0000244|PDB:1PFX}.
FT   TURN         19     23       {ECO:0000244|PDB:1PFX}.
FT   HELIX        26     33       {ECO:0000244|PDB:1PFX}.
FT   HELIX        37     44       {ECO:0000244|PDB:1PFX}.
FT   TURN         51     54       {ECO:0000244|PDB:1PFX}.
FT   STRAND       62     65       {ECO:0000244|PDB:1X7A}.
FT   STRAND       70     73       {ECO:0000244|PDB:1X7A}.
FT   STRAND       76     80       {ECO:0000244|PDB:1X7A}.
FT   TURN         81     83       {ECO:0000244|PDB:1X7A}.
FT   HELIX        92     94       {ECO:0000244|PDB:1X7A}.
FT   STRAND       97     99       {ECO:0000244|PDB:1X7A}.
FT   STRAND      104    106       {ECO:0000244|PDB:1X7A}.
FT   STRAND      116    118       {ECO:0000244|PDB:1X7A}.
FT   STRAND      122    127       {ECO:0000244|PDB:1X7A}.
FT   STRAND      129    131       {ECO:0000244|PDB:1X7A}.
FT   TURN        138    143       {ECO:0000244|PDB:1X7A}.
FT   STRAND      197    201       {ECO:0000244|PDB:1X7A}.
FT   STRAND      208    214       {ECO:0000244|PDB:1X7A}.
FT   STRAND      217    220       {ECO:0000244|PDB:1X7A}.
FT   HELIX       222    224       {ECO:0000244|PDB:1PFX}.
FT   STRAND      232    234       {ECO:0000244|PDB:1X7A}.
FT   STRAND      252    257       {ECO:0000244|PDB:1X7A}.
FT   STRAND      263    265       {ECO:0000244|PDB:1X7A}.
FT   STRAND      273    279       {ECO:0000244|PDB:1X7A}.
FT   STRAND      285    287       {ECO:0000244|PDB:1X7A}.
FT   HELIX       295    302       {ECO:0000244|PDB:1X7A}.
FT   STRAND      305    312       {ECO:0000244|PDB:1X7A}.
FT   STRAND      314    319       {ECO:0000244|PDB:1X7A}.
FT   STRAND      326    333       {ECO:0000244|PDB:1X7A}.
FT   HELIX       335    339       {ECO:0000244|PDB:1X7A}.
FT   STRAND      348    354       {ECO:0000244|PDB:1X7A}.
FT   STRAND      356    359       {ECO:0000244|PDB:1X7A}.
FT   TURN        364    368       {ECO:0000244|PDB:1X7A}.
FT   STRAND      370    377       {ECO:0000244|PDB:1X7A}.
FT   STRAND      379    387       {ECO:0000244|PDB:1X7A}.
FT   STRAND      389    392       {ECO:0000244|PDB:1X7A}.
FT   STRAND      398    401       {ECO:0000244|PDB:1X7A}.
FT   HELIX       403    409       {ECO:0000244|PDB:1X7A}.
SQ   SEQUENCE   409 AA;  45516 MW;  6AFEAE92E2515488 CRC64;
     YNSGKLEESF VRGNLERECI EEKCSFEEAR EVFENTEKTN EFWKQYVDGD QCEPNPCLNG
     GLCKDDINSY ECWCQVGFEG KNCELDATCN IKNGRCKQFC KTGADSKVLC SCTTGYRLAP
     DQKSCKPAVP FPCGRVSVSH SPTTLTRAEI IFSNMDYENS TEVEPILDSL TESNQSSDDF
     IRIVGGENAK PGQFPWQVLL NGKIDAFCGG SIINEKWVVT AAHCIEPGVK ITVVAGEYNT
     EETEPTEQRR NVIRAIPHHS YNATVNKYSH DIALLELDEP LTLNSYVTPI CIADKEYTNI
     FLKFGSGYVS GWGRVFNRGR SATILQYLKV PLVDRATCLR STKVTIYSNM FCAGFHEGGK
     DSCLGDSGGP HVTEVEGTSF LTGIISWGEE CAVKGKYGIY TKVSRYVNW
//
DBGET integrated database retrieval system