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-NOV-2023, entry version 170.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; 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 of
RT 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 viper
RT (Akistrodon rhodostoma) venom.";
RL Biochemistry 26:7627-7636(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR, DISULFIDE
RP 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 structure
RT 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+) ions,
CC phospholipids, and factor VIIIa. {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; Evidence={ECO:0000250|UniProtKB:P00740};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC linked. Interacts with SERPINC1. {ECO:0000269|PubMed:7568220}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
CC -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues
CC in the Gla domain. Calcium can also bind, with stronger affinity, to
CC another site beyond the Gla domain. Under physiological ion
CC concentrations, Ca(2+) is displaced by Mg(2+) from some of the
CC gammaglutamate residues in the N-terminal Gla domain. This leads to a
CC subtle conformation change that may affect the interaction with its
CC binding protein. {ECO:0000250|UniProtKB:P00741}.
CC -!- PTM: Activated by factor XIa, which excises the activation peptide. The
CC propeptide can also be removed by snake venom protease.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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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 AlphaFoldDB; P16293; -.
DR SMR; P16293; -.
DR STRING; 9823.ENSSSCP00000013514; -.
DR MEROPS; S01.214; -.
DR GlyCosmos; P16293; 4 sites, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000013514; -.
DR PeptideAtlas; P16293; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR InParanoid; P16293; -.
DR EvolutionaryTrace; P16293; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; 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:UniProtKB-EC.
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; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF31; COAGULATION FACTOR IX; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00010; EGFBLOOD.
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; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydrolase; Hydroxylation; Magnesium; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Sulfation; Zymogen.
FT CHAIN 1..409
FT /note="Coagulation factor IX"
FT /id="PRO_0000027770"
FT CHAIN 1..147
FT /note="Coagulation factor IXa light chain"
FT /id="PRO_0000027771"
FT PROPEP 148..182
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027772"
FT CHAIN 183..409
FT /note="Coagulation factor IXa heavy chain"
FT /id="PRO_0000027773"
FT DOMAIN 1..47
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 48..84
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 85..126
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 183..409
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 1
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 2
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 8
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 8
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 147..148
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 182..183
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 7
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 8
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 16
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 18
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 22
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 27
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 28
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 31
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 34
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 37
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 41
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P00741,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 157
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 161
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 161
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 171
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..24
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 52..63
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 57..72
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 74..83
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 89..100
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 96..110
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 112..125
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 133..291
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 208..224
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 338..352
FT /evidence="ECO:0000269|PubMed:7568220"
FT DISULFID 363..391
FT /evidence="ECO:0000269|PubMed:7568220"
FT NON_TER 1
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1PFX"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1PFX"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:1PFX"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1PFX"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:1PFX"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1PFX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1X7A"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1X7A"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1X7A"
FT TURN 138..143
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1X7A"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1PFX"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1X7A"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1X7A"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1X7A"
FT TURN 364..368
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1X7A"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1X7A"
FT HELIX 403..409
FT /evidence="ECO:0007829|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
//
