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Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]

 THRB_BOVIN              Reviewed;         625 AA.
P00735; Q3MHK7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
25-OCT-2017, entry version 197.
RecName: Full=Prothrombin;
EC=3.4.21.5;
AltName: Full=Coagulation factor II;
Contains:
RecName: Full=Activation peptide fragment 1;
Contains:
RecName: Full=Activation peptide fragment 2;
Contains:
RecName: Full=Thrombin light chain;
Contains:
RecName: Full=Thrombin heavy chain;
Flags: Precursor;
Name=F2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3379642; DOI=10.1016/0022-2836(88)90331-2;
Irwin D.M., Robertson K.A., Macgillivray R.T.A.;
"Structure and evolution of the bovine prothrombin gene.";
J. Mol. Biol. 200:31-45(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6326805; DOI=10.1021/bi00303a007;
McGillivray R.T.A., Davie E.W.;
"Characterization of bovine prothrombin mRNA and its translation
product.";
Biochemistry 23:1626-1634(1984).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 44-625, DISULFIDE BONDS, GAMMA-CARBOXYGLUTAMATION
AT GLU-50; GLU-51; GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70;
GLU-73 AND GLU-76, AND GLYCOSYLATION AT ASN-120; ASN-144 AND ASN-419.
Magnusson S., Sottrup-Jensen L., Petersen T.E., Claeys H.;
(In) Hemker H.C., Veltkamp J.J. (eds.);
Boerhaave symposium on prothrombin and related coagulation factors,
pp.25-46, Leiden University Press, Leiden (1975).
[5]
GENE STRUCTURE.
PubMed=3000440; DOI=10.1021/bi00345a018;
Irwin D.M., Ahern K.G., Pearson G.D., McGillivray R.T.A.;
"Characterization of the bovine prothrombin gene.";
Biochemistry 24:6854-6861(1985).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
PubMed=3741841; DOI=10.1021/bi00362a001;
Park C.H., Tulinsky A.;
"Three-dimensional structure of the kringle sequence: structure of
prothrombin fragment 1.";
Biochemistry 25:3977-3982(1986).
[7]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
PubMed=1856869; DOI=10.1016/0022-2836(91)90025-2;
Seshadri T.-P., Tulinsky A., Skrzypczak-Jankun E., Park C.H.;
"Structure of bovine prothrombin fragment 1 refined at 2.25-A
resolution.";
J. Mol. Biol. 220:481-494(1991).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF ACTIVATION PEPTIDE 1 IN
COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-120 AND ASN-144.
PubMed=1547238; DOI=10.1021/bi00124a016;
Soriano-Garcia M., Padmanabhan K., de Vos A.M., Tulinsky A.;
"The Ca2+ ion and membrane binding structure of the Gla domain of Ca-
prothrombin fragment 1.";
Biochemistry 31:2554-2566(1992).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FIBRINOGEN.
PubMed=1560020;
Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.;
"The structure of residues 7-16 of the A alpha-chain of human
fibrinogen bound to bovine thrombin at 2.3-A resolution.";
J. Biol. Chem. 267:7911-7920(1992).
[10]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 318-625 IN COMPLEX WITH
HIRUDIN.
PubMed=1517214;
Vitali J., Martin P.D., Malkowski M.G., Robertson W.D., Lazar J.B.,
Winant R.C., Johnson P.H., Edwards B.F.P.;
"The structure of a complex of bovine alpha-thrombin and recombinant
hirudin at 2.8-A resolution.";
J. Biol. Chem. 267:17670-17678(1992).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=1518046; DOI=10.1016/0022-2836(92)91054-S;
Brandstetter H., Turk D., Hoeffken H.W., Grosse D., Stuerzebecher J.,
Martin P.D., Edwards B.F.P., Bode W.;
"Refined 2.3 A X-ray crystal structure of bovine thrombin complexes
formed with the benzamidine and arginine-based thrombin inhibitors
NAPAP, 4-TAPAP and MQPA. A starting point for improving
antithrombotics.";
J. Mol. Biol. 226:1085-1099(1992).
[12]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH ORNITHODORIN.
PubMed=8947023;
van de Locht A., Stubbs M.T., Bode W., Friedrich T., Bollschweiler C.,
Hoffken W., Huber R.;
"The ornithodorin-thrombin crystal structure, a key to the TAP
enigma?";
EMBO J. 15:6011-6017(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH TRIABIN.
PubMed=9342325; DOI=10.1073/pnas.94.22.11845;
Fuentes-Prior P., Noeske-Jungblut C., Donner P., Schleuning W.-D.,
Huber R., Bode W.;
"Structure of the thrombin complex with triabin, a lipocalin-like
exosite-binding inhibitor derived from a triatomine bug.";
Proc. Natl. Acad. Sci. U.S.A. 94:11845-11850(1997).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 44-190 IN COMPLEX WITH
CALCIUM AND LYSOPHOSPHATIDYLSERINE.
PubMed=12923575; DOI=10.1038/nsb971;
Huang M., Rigby A.C., Morelli X., Grant M.A., Huang G., Furie B.,
Seaton B., Furie B.C.;
"Structural basis of membrane binding by Gla domains of vitamin K-
dependent proteins.";
Nat. Struct. Biol. 10:751-756(2003).
-!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys,
converts fibrinogen to fibrin and activates factors V, VII, VIII,
XIII, and, in complex with thrombomodulin, protein C. Functions in
blood homeostasis, inflammation and wound healing (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in
fibrinogen to form fibrin and release fibrinopeptides A and B.
-!- ENZYME REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
chain; disulfide-linked. Forms a heterodimer with SERPINA5 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q4W8J9:coa (xeno); NbExp=2; IntAct=EBI-990806, EBI-990838;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions,
result from the carboxylation of glutamyl residues by a microsomal
enzyme, the vitamin K-dependent carboxylase. The modified residues
are necessary for the calcium-dependent interaction with a
negatively charged phospholipid surface, which is essential for
the conversion of prothrombin to thrombin. {ECO:0000269|Ref.4}.
-!- MISCELLANEOUS: Prothrombin is activated on the surface of a
phospholipid membrane that binds the amino end of prothrombin and
factors Va and Xa in Ca-dependent interactions; factor Xa removes
the activation peptide and cleaves the remaining part into light
and heavy chains. The activation process starts slowly because
factor V itself has to be activated by the initial, small amounts
of thrombin.
-!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
(fragment 1) of the prothrombin, prior to its activation by factor
Xa.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; V00135; CAA23451.1; -; mRNA.
EMBL; J00041; AAA30781.1; -; mRNA.
EMBL; BC105201; AAI05202.1; -; mRNA.
PIR; S02537; TBBO.
RefSeq; NP_776302.1; NM_173877.1.
RefSeq; XP_015330343.1; XM_015474857.1.
UniGene; Bt.29855; -.
PDB; 1A0H; X-ray; 3.20 A; A/D=208-366, B/E=367-625.
PDB; 1AVG; X-ray; 2.60 A; H=367-625, L=326-366.
PDB; 1BBR; X-ray; 2.30 A; E=517-625, H=367-515, J/L/M=318-366, K/N=367-625.
PDB; 1ETR; X-ray; 2.20 A; H=367-625, L=318-366.
PDB; 1ETS; X-ray; 2.30 A; H=367-625, L=318-366.
PDB; 1ETT; X-ray; 2.50 A; H=367-625, L=318-366.
PDB; 1HRT; X-ray; 2.80 A; H=367-625, L=318-366.
PDB; 1ID5; X-ray; 2.50 A; H=367-622, L=318-366.
PDB; 1MKW; X-ray; 2.30 A; H=367-625, K=318-625, L=318-366.
PDB; 1MKX; X-ray; 2.20 A; H=367-625, K=318-625, L=318-366.
PDB; 1NL1; X-ray; 1.90 A; A=44-190.
PDB; 1NL2; X-ray; 2.30 A; A=44-189.
PDB; 1TBQ; X-ray; 3.10 A; H/K=367-625, J/L=318-366.
PDB; 1TBR; X-ray; 2.60 A; H/K=367-625, J/L=318-366.
PDB; 1TOC; X-ray; 3.10 A; A/C/E/G=318-366, B/D/F/H=367-625.
PDB; 1UCY; X-ray; 2.20 A; E=517-625, H=367-516, J/L/M=318-366, K/N=367-625.
PDB; 1UVT; X-ray; 2.50 A; H=367-625, L=318-366.
PDB; 1UVU; X-ray; 2.80 A; H=367-625, L=318-366.
PDB; 1VIT; X-ray; 3.20 A; F=367-516, G=517-625, H=367-625, L/M=318-366.
PDB; 1YCP; X-ray; 2.50 A; H=367-625, J/L=318-366, K=367-516, M=517-625.
PDB; 2A1D; X-ray; 3.50 A; A/E=326-366, B/F=367-625.
PDB; 2HPP; X-ray; 3.30 A; P=214-292.
PDB; 2ODY; X-ray; 2.35 A; A/C=318-366, B/D=367-625.
PDB; 2PF1; X-ray; 2.80 A; A=44-199.
PDB; 2PF2; X-ray; 2.20 A; A=44-199.
PDB; 2SPT; X-ray; 2.50 A; A=44-188.
PDB; 3PMA; X-ray; 2.20 A; A/C=336-364, B/D=367-625.
PDB; 3PMB; X-ray; 2.90 A; A/C=336-364, B/D=367-625.
PDBsum; 1A0H; -.
PDBsum; 1AVG; -.
PDBsum; 1BBR; -.
PDBsum; 1ETR; -.
PDBsum; 1ETS; -.
PDBsum; 1ETT; -.
PDBsum; 1HRT; -.
PDBsum; 1ID5; -.
PDBsum; 1MKW; -.
PDBsum; 1MKX; -.
PDBsum; 1NL1; -.
PDBsum; 1NL2; -.
PDBsum; 1TBQ; -.
PDBsum; 1TBR; -.
PDBsum; 1TOC; -.
PDBsum; 1UCY; -.
PDBsum; 1UVT; -.
PDBsum; 1UVU; -.
PDBsum; 1VIT; -.
PDBsum; 1YCP; -.
PDBsum; 2A1D; -.
PDBsum; 2HPP; -.
PDBsum; 2ODY; -.
PDBsum; 2PF1; -.
PDBsum; 2PF2; -.
PDBsum; 2SPT; -.
PDBsum; 3PMA; -.
PDBsum; 3PMB; -.
ProteinModelPortal; P00735; -.
SMR; P00735; -.
DIP; DIP-6099N; -.
IntAct; P00735; 1.
MINT; MINT-1504393; -.
STRING; 9913.ENSBTAP00000009406; -.
BindingDB; P00735; -.
ChEMBL; CHEMBL4471; -.
Allergome; 1245; Bos d Thrombin.
MEROPS; S01.217; -.
iPTMnet; P00735; -.
UniCarbKB; P00735; -.
PaxDb; P00735; -.
PeptideAtlas; P00735; -.
PRIDE; P00735; -.
Ensembl; ENSBTAT00000009406; ENSBTAP00000009406; ENSBTAG00000007148.
GeneID; 280685; -.
KEGG; bta:280685; -.
CTD; 2147; -.
eggNOG; ENOG410IKPN; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000251824; -.
HOVERGEN; HBG108381; -.
InParanoid; P00735; -.
KO; K01313; -.
OMA; GIECQLW; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.5; 908.
Reactome; R-BTA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-BTA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-BTA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-BTA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
Reactome; R-BTA-375276; Peptide ligand-binding receptors.
Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-BTA-416476; G alpha (q) signalling events.
Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-BTA-76009; Platelet Aggregation (Plug Formation).
Reactome; R-BTA-977606; Regulation of Complement cascade.
EvolutionaryTrace; P00735; -.
PMAP-CutDB; P00735; -.
PRO; PR:P00735; -.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000007148; -.
GO; GO:0072562; C:blood microparticle; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0070051; F:fibrinogen binding; IPI:BHF-UCL.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0070053; F:thrombospondin receptor activity; IEA:Ensembl.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0051838; P:cytolysis by host of symbiont cells; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
GO; GO:0070945; P:neutrophil mediated killing of gram-negative bacterium; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; IEA:Ensembl.
GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0090218; P:positive regulation of lipid kinase activity; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:1900738; P:positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0051258; P:protein polymerization; IDA:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.140.10; -; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR003966; Prothrombin/thrombin.
InterPro; IPR018992; Thrombin_light_chain.
InterPro; IPR037111; Thrombin_light_chain_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24254:SF10; PTHR24254:SF10; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF09396; Thrombin_light; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001149; Thrombin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
PRINTS; PR01505; PROTHROMBIN.
SMART; SM00069; GLA; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
Glycoprotein; Hemostasis; Hydrolase; Kringle; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 43 {ECO:0000269|Ref.4}.
/FTId=PRO_0000028153.
CHAIN 44 625 Prothrombin.
/FTId=PRO_0000028154.
PEPTIDE 44 199 Activation peptide fragment 1.
/FTId=PRO_0000028155.
PEPTIDE 200 317 Activation peptide fragment 2.
/FTId=PRO_0000028156.
CHAIN 318 366 Thrombin light chain.
/FTId=PRO_0000028157.
CHAIN 367 625 Thrombin heavy chain.
/FTId=PRO_0000028158.
DOMAIN 44 90 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 109 187 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 214 292 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 367 621 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 554 576 High affinity receptor-binding region
which is also known as the TP508 peptide.
{ECO:0000250}.
ACT_SITE 409 409 Charge relay system.
ACT_SITE 465 465 Charge relay system.
ACT_SITE 571 571 Charge relay system.
SITE 199 200 Cleavage; by thrombin.
SITE 317 318 Cleavage; by factor Xa.
SITE 366 367 Cleavage; by factor Xa.
MOD_RES 50 50 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 51 51 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 58 58 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 60 60 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 63 63 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 64 64 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 69 69 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 70 70 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 73 73 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
MOD_RES 76 76 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|Ref.4}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1547238,
ECO:0000269|Ref.4}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1547238,
ECO:0000269|Ref.4}.
CARBOHYD 419 419 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.4}.
DISULFID 61 66
DISULFID 91 104
DISULFID 109 187
DISULFID 130 170
DISULFID 158 182
DISULFID 214 292
DISULFID 235 275
DISULFID 263 287
DISULFID 339 485 Interchain (between light and heavy
chains).
DISULFID 394 410
DISULFID 539 553
DISULFID 567 597
VARIANT 600 600 D -> N.
CONFLICT 231 231 S -> H (in Ref. 2; AAA30781).
{ECO:0000305}.
CONFLICT 249 249 D -> H (in Ref. 2; AAA30781).
{ECO:0000305}.
CONFLICT 288 288 D -> N (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 353 353 Q -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 355 355 E -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 358 358 L -> P (in Ref. 3; AAI05202).
{ECO:0000305}.
CONFLICT 549 550 DN -> ND (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 47 49 {ECO:0000244|PDB:1NL1}.
HELIX 50 52 {ECO:0000244|PDB:1NL1}.
HELIX 57 61 {ECO:0000244|PDB:1NL1}.
HELIX 68 74 {ECO:0000244|PDB:1NL1}.
HELIX 78 90 {ECO:0000244|PDB:1NL1}.
TURN 91 93 {ECO:0000244|PDB:1NL1}.
HELIX 98 106 {ECO:0000244|PDB:1NL1}.
STRAND 108 110 {ECO:0000244|PDB:1NL1}.
TURN 112 114 {ECO:0000244|PDB:2PF2}.
STRAND 125 127 {ECO:0000244|PDB:2PF2}.
STRAND 137 139 {ECO:0000244|PDB:1NL1}.
TURN 145 147 {ECO:0000244|PDB:1NL1}.
STRAND 149 151 {ECO:0000244|PDB:2PF1}.
STRAND 168 174 {ECO:0000244|PDB:1NL1}.
STRAND 179 181 {ECO:0000244|PDB:1NL1}.
STRAND 185 189 {ECO:0000244|PDB:2PF1}.
STRAND 192 194 {ECO:0000244|PDB:2PF1}.
HELIX 217 219 {ECO:0000244|PDB:1A0H}.
STRAND 238 240 {ECO:0000244|PDB:1A0H}.
HELIX 243 246 {ECO:0000244|PDB:1A0H}.
STRAND 248 250 {ECO:0000244|PDB:2HPP}.
STRAND 254 256 {ECO:0000244|PDB:2HPP}.
STRAND 274 276 {ECO:0000244|PDB:1A0H}.
STRAND 278 280 {ECO:0000244|PDB:1A0H}.
STRAND 284 286 {ECO:0000244|PDB:1A0H}.
STRAND 291 293 {ECO:0000244|PDB:1A0H}.
STRAND 310 313 {ECO:0000244|PDB:1A0H}.
STRAND 321 323 {ECO:0000244|PDB:1A0H}.
HELIX 329 332 {ECO:0000244|PDB:2ODY}.
TURN 337 340 {ECO:0000244|PDB:1ETR}.
TURN 343 345 {ECO:0000244|PDB:1ETR}.
HELIX 346 348 {ECO:0000244|PDB:1ETR}.
HELIX 355 362 {ECO:0000244|PDB:1ETR}.
STRAND 370 372 {ECO:0000244|PDB:1MKX}.
STRAND 375 377 {ECO:0000244|PDB:2A1D}.
STRAND 381 386 {ECO:0000244|PDB:1ETR}.
TURN 387 390 {ECO:0000244|PDB:1ETR}.
STRAND 391 400 {ECO:0000244|PDB:1ETR}.
STRAND 403 406 {ECO:0000244|PDB:1ETR}.
HELIX 408 410 {ECO:0000244|PDB:1ETR}.
HELIX 414 416 {ECO:0000244|PDB:1ETR}.
STRAND 424 430 {ECO:0000244|PDB:1ETR}.
STRAND 433 436 {ECO:0000244|PDB:1ETR}.
TURN 439 441 {ECO:0000244|PDB:1ETR}.
STRAND 443 445 {ECO:0000244|PDB:1ETR}.
STRAND 447 452 {ECO:0000244|PDB:1ETR}.
TURN 458 461 {ECO:0000244|PDB:1ETR}.
STRAND 467 473 {ECO:0000244|PDB:1ETR}.
HELIX 489 495 {ECO:0000244|PDB:1ETR}.
STRAND 501 506 {ECO:0000244|PDB:1ETR}.
STRAND 510 513 {ECO:0000244|PDB:1UCY}.
STRAND 516 518 {ECO:0000244|PDB:1ETR}.
STRAND 520 522 {ECO:0000244|PDB:1UCY}.
STRAND 527 533 {ECO:0000244|PDB:1ETR}.
HELIX 536 541 {ECO:0000244|PDB:1ETR}.
STRAND 543 545 {ECO:0000244|PDB:1ETT}.
STRAND 551 554 {ECO:0000244|PDB:1ETR}.
HELIX 558 560 {ECO:0000244|PDB:1ETR}.
TURN 568 572 {ECO:0000244|PDB:1ETR}.
STRAND 574 578 {ECO:0000244|PDB:1ETR}.
TURN 580 582 {ECO:0000244|PDB:1ETR}.
STRAND 585 591 {ECO:0000244|PDB:1ETR}.
STRAND 595 598 {ECO:0000244|PDB:1ETR}.
STRAND 604 608 {ECO:0000244|PDB:1ETR}.
TURN 609 612 {ECO:0000244|PDB:1ETR}.
HELIX 613 621 {ECO:0000244|PDB:1ETR}.
SEQUENCE 625 AA; 70506 MW; 95AFF17C23AD78F9 CRC64;
MARVRGPRLP GCLALAALFS LVHSQHVFLA HQQASSLLQR ARRANKGFLE EVRKGNLERE
CLEEPCSREE AFEALESLSA TDAFWAKYTA CESARNPREK LNECLEGNCA EGVGMNYRGN
VSVTRSGIEC QLWRSRYPHK PEINSTTHPG ADLRENFCRN PDGSITGPWC YTTSPTLRRE
ECSVPVCGQD RVTVEVIPRS GGSTTSQSPL LETCVPDRGR EYRGRLAVTT SGSRCLAWSS
EQAKALSKDQ DFNPAVPLAE NFCRNPDGDE EGAWCYVADQ PGDFEYCDLN YCEEPVDGDL
GDRLGEDPDP DAAIEGRTSE DHFQPFFNEK TFGAGEADCG LRPLFEKKQV QDQTEKELFE
SYIEGRIVEG QDAEVGLSPW QVMLFRKSPQ ELLCGASLIS DRWVLTAAHC LLYPPWDKNF
TVDDLLVRIG KHSRTRYERK VEKISMLDKI YIHPRYNWKE NLDRDIALLK LKRPIELSDY
IHPVCLPDKQ TAAKLLHAGF KGRVTGWGNR RETWTTSVAE VQPSVLQVVN LPLVERPVCK
ASTRIRITDN MFCAGYKPGE GKRGDACEGD SGGPFVMKSP YNNRWYQMGI VSWGEGCDRD
GKYGFYTHVF RLKKWIQKVI DRLGS


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