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FA9_PIG
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   03-AUG-2022, entry version 166.
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   PeptideAtlas; P16293; -.
DR   PRIDE; P16293; -.
DR   eggNOG; ENOG502QUEV; Eukaryota.
DR   InParanoid; P16293; -.
DR   EvolutionaryTrace; P16293; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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; 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: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; 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
 
 
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