GenomeNet

Database: UniProt
Entry: Q7SZN0
LinkDB: Q7SZN0
Original site: Q7SZN0 
ID   FA5V_PSETE              Reviewed;        1460 AA.
AC   Q7SZN0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   26-NOV-2014, entry version 65.
DE   RecName: Full=Venom prothrombin activator pseutarin-C non-catalytic subunit;
DE            Short=PCNS;
DE            Short=vPA;
DE   AltName: Full=Venom coagulation factor Va-like protein;
DE   Contains:
DE     RecName: Full=Pseutarin-C non-catalytic subunit heavy chain;
DE   Contains:
DE     RecName: Full=Pseutarin-C non-catalytic subunit light chain;
DE   Flags: Precursor;
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
OC   Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-54; 58-124;
RP   141-160; 309-317; 331-340; 352-372; 378-392; 430-454; 477-499;
RP   507-530; 559-567; 821-840; 851-866; 868-886; 896-922; 926-949;
RP   968-996; 1037-1059; 1078-1089; 1119-1134; 1149-1175; 1266-1279;
RP   1327-1368; 1396-1405; 1413-1425; 1429-1435 AND 1443-1451, ABSENCE OF
RP   GLYCOSYLATION AT ASN-385 AND ASN-1397, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12730119; DOI=10.1182/blood-2002-12-3839;
RA   Rao V.S., Swarup S., Kini R.M.;
RT   "The nonenzymatic subunit of pseutarin C, a prothrombin activator from
RT   eastern brown snake (Pseudonaja textilis) venom, shows structural
RT   similarity to mammalian coagulation factor V.";
RL   Blood 102:1347-1354(2003).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=12362232; DOI=10.1267/th02100611;
RA   Rao V.S., Kini R.M.;
RT   "Pseutarin C, a prothrombin activator from Pseudonaja textilis venom:
RT   its structural and functional similarity to mammalian coagulation
RT   factor Xa-Va complex.";
RL   Thromb. Haemost. 88:611-619(2002).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=11522026;
RA   Manjunatha Kini R., Morita T., Rosing J.;
RT   "Classification and nomenclature of prothrombin activators isolated
RT   from snake venoms.";
RL   Thromb. Haemost. 86:710-711(2001).
RN   [4]
RP   TISSUE SPECIFICITY.
RC   TISSUE=Venom gland;
RX   PubMed=15735790; DOI=10.1267/THRO05030420;
RA   Minh Le T.N., Reza M.A., Swarup S., Kini R.M.;
RT   "Gene duplication of coagulation factor V and origin of venom
RT   prothrombin activator in Pseudonaja textilis snake.";
RL   Thromb. Haemost. 93:420-429(2005).
RN   [5]
RP   PHARMACEUTICAL.
RX   PubMed=21184772; DOI=10.1016/j.toxicon.2010.12.010;
RA   Earl S.T., Masci P.P., de Jersey J., Lavin M.F., Dixon J.;
RT   "Drug development from Australian elapid snake venoms and the Venomics
RT   pipeline of candidates for haemostasis: Textilinin-1 (Q8008),
RT   Haempatch (Q8009) and CoVase (V0801).";
RL   Toxicon 59:456-463(2012).
CC   -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC       system of prey. This non-catalytic subunit is functionally similar
CC       to blood coagulation factor V. It serves as a critical cofactor
CC       for the prothrombinase activity of the catalytic subunit, which is
CC       similar to the blood coagulation factor X.
CC       {ECO:0000269|PubMed:12362232}.
CC   -!- SUBUNIT: Heterodimer of a light and a heavy chains; non-disulfide-
CC       linked. The interaction between the two chains is calcium-
CC       dependent (By similarity). Found in its active form associated
CC       with pseutarin-C catalytic subunit (AC Q56VR3). {ECO:0000250,
CC       ECO:0000269|PubMed:12362232}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12362232,
CC       ECO:0000269|PubMed:12730119}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:12730119,
CC       ECO:0000269|PubMed:15735790}.
CC   -!- PTM: In physiological conditions, blood coagulation factor V and
CC       factor Va are inactivated by activated protein C (APC) through
CC       proteolytic degradation of the heavy chain. However, pseutarin-C
CC       non-catalytic subunit (factor V-like protein) retains its full
CC       activity even at high concentration of APC. This has two
CC       explanations: this protein has only one of the three cleavage
CC       sites present in factor V that are targeted by the APC for
CC       inactivation, and the binding with the catalytic subunit protect
CC       the cleavage site from inactivation.
CC   -!- PHARMACEUTICAL: Is under preclinical trial by the Australian
CC       biopharmaceutical company QRxPharma Ltd, its subsidiary Venomics
CC       Pty Ltd (VPL) and the University of Queensland (UQ) under the name
CC       CoVase (V0801). Tested as a procoagulant cofactor that may have
CC       application as a systemic anti-bleeding agent in the treatment of
CC       internal bleeding and non-compressible haemorrhage.
CC   -!- MISCELLANEOUS: In contrast to blood coagulation factors that
CC       circulate as inactive zymogen in plasma, venom prothrombin
CC       activators are always found in the active form in the venom.
CC       Hence, catalytic and non-catalytic subunits are found naturally in
CC       venom as stable complexes.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 F5/8 type A domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 F5/8 type C domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00081}.
CC   -!- SIMILARITY: Contains 6 plastocyanin-like domains. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY168281; AAO38805.1; -; mRNA.
DR   PDB; 4BXS; X-ray; 3.32 A; V=31-1460.
DR   PDBsum; 4BXS; -.
DR   ProteinModelPortal; Q7SZN0; -.
DR   SMR; Q7SZN0; 31-327, 1302-1460.
DR   HOVERGEN; HBG005631; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR   GO; GO:0035807; P:positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:GOC.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.40.420; -; 6.
DR   InterPro; IPR000421; Coagulation_fac_5/8-C_type_dom.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   Pfam; PF07732; Cu-oxidase_3; 3.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   SMART; SM00231; FA58C; 2.
DR   SUPFAM; SSF49503; SSF49503; 6.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   PROSITE; PS01285; FA58C_1; 2.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Metal-binding; Pharmaceutical;
KW   Phosphoprotein; Prothrombin activator; Repeat; Secreted; Signal;
KW   Toxin.
FT   SIGNAL        1     30       {ECO:0000269|PubMed:12730119}.
FT   CHAIN        31    772       Pseutarin-C non-catalytic subunit heavy
FT                                chain. {ECO:0000305}.
FT                                /FTId=PRO_5000089286.
FT   PROPEP      773    818       Activation peptide (connecting region).
FT                                /FTId=PRO_0000408521.
FT   CHAIN       819   1460       Pseutarin-C non-catalytic subunit light
FT                                chain.
FT                                /FTId=PRO_0000408522.
FT   DOMAIN       32    330       F5/8 type A 1.
FT   DOMAIN       32    196       Plastocyanin-like 1.
FT   DOMAIN      206    330       Plastocyanin-like 2.
FT   DOMAIN      351    685       F5/8 type A 2.
FT   DOMAIN      351    529       Plastocyanin-like 3.
FT   DOMAIN      539    685       Plastocyanin-like 4.
FT   DOMAIN      824   1143       F5/8 type A 3.
FT   DOMAIN      824    992       Plastocyanin-like 5.
FT   DOMAIN     1001   1143       Plastocyanin-like 6.
FT   DOMAIN     1147   1298       F5/8 type C 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN     1303   1457       F5/8 type C 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   REGION      693    818       B.
FT   COMPBIAS    695    699       Poly-Glu.
FT   METAL       142    142       Calcium. {ECO:0000250}.
FT   METAL       143    143       Calcium. {ECO:0000250}.
FT   SITE        385    385       Not glycosylated.
FT   SITE        537    538       Cleavage; by activated protein C.
FT                                {ECO:0000250}.
FT   SITE        772    773       Cleavage; by thrombin. {ECO:0000250}.
FT   SITE        818    819       Cleavage; by thrombin. {ECO:0000250}.
FT   SITE       1397   1397       Not glycosylated.
FT   CARBOHYD    156    156       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    242    242       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    471    471       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    944    944       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1001   1001       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1180   1180       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    170    196       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID    251    332       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID    503    529       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID    966    992       {ECO:0000305}.
FT   DISULFID   1147   1298       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   DISULFID   1303   1457       {ECO:0000255|PROSITE-ProRule:PRU00081}.
FT   CONFLICT     80     82       EPR -> KPQ (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    103    103       I -> Q (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    119    124       SAVYNK -> DAVKIG (in Ref. 1; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    146    146       P -> A (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       N -> E (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    350    363       IKNWEYFIAAEEIT -> AQLWEYHIAAQKED (in Ref.
FT                                1; AA sequence). {ECO:0000305}.
FT   CONFLICT    440    444       NLASR -> DLAVQ (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    522    523       LI -> IL (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    820    827       INRGNKRR -> QNTGNKLY (in Ref. 1; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    840    840       S -> I (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    876    876       G -> GK (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    902    902       K -> R (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    944    944       N -> F (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    981    995       IHSGLIGPILICQKG -> VEPGLIGPLYSIAEEAV (in
FT                                Ref. 1; AA sequence). {ECO:0000305}.
FT   CONFLICT   1041   1043       SLH -> NLG (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1055   1058       LQGL -> GK (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1166   1170       SGHVG -> AGHVQ (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1274   1274       I -> V (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1369   1369       I -> K (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1400   1404       WKPYL -> YKPYG (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1433   1434       LS -> SL (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       33     36       {ECO:0000244|PDB:4BXS}.
FT   STRAND       39     45       {ECO:0000244|PDB:4BXS}.
FT   STRAND       64     69       {ECO:0000244|PDB:4BXS}.
FT   HELIX        74     76       {ECO:0000244|PDB:4BXS}.
FT   STRAND       84     86       {ECO:0000244|PDB:4BXS}.
FT   STRAND      100    111       {ECO:0000244|PDB:4BXS}.
FT   STRAND      117    120       {ECO:0000244|PDB:4BXS}.
FT   TURN        124    126       {ECO:0000244|PDB:4BXS}.
FT   TURN        137    139       {ECO:0000244|PDB:4BXS}.
FT   TURN        141    143       {ECO:0000244|PDB:4BXS}.
FT   STRAND      150    155       {ECO:0000244|PDB:4BXS}.
FT   STRAND      159    162       {ECO:0000244|PDB:4BXS}.
FT   TURN        164    166       {ECO:0000244|PDB:4BXS}.
FT   STRAND      169    175       {ECO:0000244|PDB:4BXS}.
FT   TURN        178    180       {ECO:0000244|PDB:4BXS}.
FT   HELIX       181    185       {ECO:0000244|PDB:4BXS}.
FT   TURN        186    188       {ECO:0000244|PDB:4BXS}.
FT   STRAND      191    196       {ECO:0000244|PDB:4BXS}.
FT   STRAND      205    209       {ECO:0000244|PDB:4BXS}.
FT   STRAND      211    221       {ECO:0000244|PDB:4BXS}.
FT   TURN        223    225       {ECO:0000244|PDB:4BXS}.
FT   STRAND      226    228       {ECO:0000244|PDB:4BXS}.
FT   STRAND      234    237       {ECO:0000244|PDB:4BXS}.
FT   STRAND      248    251       {ECO:0000244|PDB:4BXS}.
FT   STRAND      256    263       {ECO:0000244|PDB:4BXS}.
FT   STRAND      272    274       {ECO:0000244|PDB:4BXS}.
FT   STRAND      287    289       {ECO:0000244|PDB:4BXS}.
FT   STRAND      295    300       {ECO:0000244|PDB:4BXS}.
FT   STRAND      307    313       {ECO:0000244|PDB:4BXS}.
FT   HELIX       316    320       {ECO:0000244|PDB:4BXS}.
FT   STRAND      325    330       {ECO:0000244|PDB:4BXS}.
FT   STRAND      355    366       {ECO:0000244|PDB:4BXS}.
FT   HELIX       378    381       {ECO:0000244|PDB:4BXS}.
FT   STRAND      392    404       {ECO:0000244|PDB:4BXS}.
FT   STRAND      409    411       {ECO:0000244|PDB:4BXS}.
FT   STRAND      413    415       {ECO:0000244|PDB:4BXS}.
FT   STRAND      417    419       {ECO:0000244|PDB:4BXS}.
FT   STRAND      426    428       {ECO:0000244|PDB:4BXS}.
FT   STRAND      433    440       {ECO:0000244|PDB:4BXS}.
FT   STRAND      442    444       {ECO:0000244|PDB:4BXS}.
FT   STRAND      449    453       {ECO:0000244|PDB:4BXS}.
FT   STRAND      475    478       {ECO:0000244|PDB:4BXS}.
FT   STRAND      483    489       {ECO:0000244|PDB:4BXS}.
FT   TURN        492    494       {ECO:0000244|PDB:4BXS}.
FT   STRAND      498    500       {ECO:0000244|PDB:4BXS}.
FT   STRAND      502    509       {ECO:0000244|PDB:4BXS}.
FT   HELIX       514    519       {ECO:0000244|PDB:4BXS}.
FT   STRAND      524    529       {ECO:0000244|PDB:4BXS}.
FT   HELIX       556    558       {ECO:0000244|PDB:4BXS}.
FT   HELIX       562    569       {ECO:0000244|PDB:4BXS}.
FT   HELIX       573    575       {ECO:0000244|PDB:4BXS}.
FT   HELIX       581    587       {ECO:0000244|PDB:4BXS}.
FT   STRAND      595    597       {ECO:0000244|PDB:4BXS}.
FT   STRAND      603    605       {ECO:0000244|PDB:4BXS}.
FT   STRAND      610    612       {ECO:0000244|PDB:4BXS}.
FT   STRAND      630    632       {ECO:0000244|PDB:4BXS}.
FT   STRAND      634    636       {ECO:0000244|PDB:4BXS}.
FT   STRAND      639    643       {ECO:0000244|PDB:4BXS}.
FT   STRAND      655    657       {ECO:0000244|PDB:4BXS}.
FT   STRAND      664    667       {ECO:0000244|PDB:4BXS}.
FT   HELIX       674    677       {ECO:0000244|PDB:4BXS}.
FT   STRAND      678    684       {ECO:0000244|PDB:4BXS}.
FT   HELIX       692    698       {ECO:0000244|PDB:4BXS}.
FT   STRAND      834    839       {ECO:0000244|PDB:4BXS}.
FT   STRAND      855    859       {ECO:0000244|PDB:4BXS}.
FT   STRAND      863    866       {ECO:0000244|PDB:4BXS}.
FT   STRAND      870    872       {ECO:0000244|PDB:4BXS}.
FT   HELIX       878    880       {ECO:0000244|PDB:4BXS}.
FT   STRAND      889    892       {ECO:0000244|PDB:4BXS}.
FT   STRAND      896    899       {ECO:0000244|PDB:4BXS}.
FT   STRAND      905    907       {ECO:0000244|PDB:4BXS}.
FT   STRAND      912    917       {ECO:0000244|PDB:4BXS}.
FT   HELIX       933    935       {ECO:0000244|PDB:4BXS}.
FT   TURN        936    938       {ECO:0000244|PDB:4BXS}.
FT   STRAND      949    952       {ECO:0000244|PDB:4BXS}.
FT   HELIX       955    957       {ECO:0000244|PDB:4BXS}.
FT   STRAND      966    972       {ECO:0000244|PDB:4BXS}.
FT   STRAND      974    976       {ECO:0000244|PDB:4BXS}.
FT   HELIX       977    981       {ECO:0000244|PDB:4BXS}.
FT   TURN        982    984       {ECO:0000244|PDB:4BXS}.
FT   STRAND      987    992       {ECO:0000244|PDB:4BXS}.
FT   STRAND      999   1002       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1004   1017       {ECO:0000244|PDB:4BXS}.
FT   TURN       1018   1020       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1021   1023       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1044   1048       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1051   1053       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1059   1064       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1066   1072       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1080   1084       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1100   1104       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1111   1113       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1120   1127       {ECO:0000244|PDB:4BXS}.
FT   HELIX      1129   1132       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1139   1143       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1152   1155       {ECO:0000244|PDB:4BXS}.
FT   TURN       1160   1162       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1163   1166       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1169   1171       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1183   1185       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1200   1215       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1226   1232       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1235   1237       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1254   1256       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1259   1262       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1265   1267       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1273   1288       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1293   1298       {ECO:0000244|PDB:4BXS}.
FT   TURN       1309   1311       {ECO:0000244|PDB:4BXS}.
FT   TURN       1316   1318       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1319   1322       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1343   1345       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1359   1362       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1368   1374       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1376   1378       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1383   1389       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1392   1394       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1396   1398       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1400   1402       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1408   1410       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1418   1421       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1426   1432       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1435   1438       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1441   1447       {ECO:0000244|PDB:4BXS}.
FT   STRAND     1452   1457       {ECO:0000244|PDB:4BXS}.
SQ   SEQUENCE   1460 AA;  165932 MW;  6AFB63E2D5D275A6 CRC64;
     MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYHIAA QLEDWDYNPQ PEELSRLSES
     DLTFKKIVYR EYELDFKQEE PRDALSGLLG PTLRGEVGDS LIIYFKNFAT QPVSIHPQSA
     VYNKWSEGSS YSDGTSDVER LDDAVPPGQS FKYVWNITAE IGPKKADPPC LTYAYYSHVN
     MVRDFNSGLI GALLICKEGS LNANGSQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF
     ANGTLPDVQA CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAD
     MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGNPDTLTR KLSFRELMKI KNWEYFIAAE
     EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR QYEDGNFTKP TYAIWPKERG
     ILGPVIKAKV RDTVTIVFKN LASRPYSIYV HGVSVSKDAE GAIYPSDPKE NITHGKAVEP
     GQVYTYKWTV LDTDEPTVKD SECITKLYHS AVDMTRDIAS GLIGPLLVCK HKALSVKGVQ
     NKADVEQHAV FAVFDENKSW YLEDNIKKYC SNPSAVKKDD PKFYKSNVMY TLNGYASDRT
     EVLRFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS GESATVTMDN
     LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED DGDIFADIFI PSEVVKKKEE
     VPVNFVPDPE SDALAKELGL IDDEGNPIIQ PRREQTEDDE EQLMKASMLG LRSFKGSVAE
     EELKHTALAL EEDAHASDPR IDSNSARNPD DIAGRYLRTI NRGNKRRYYI AAEEVLWDYS
     PIGKSQVRSR AAKTTFKKAI FRSYLDDTFQ TPSTGGEYEK HLGILGPIIR AEVDDVIEIQ
     FKNLASRPYS LHAHGLLYEK SSEGRSYDDK SPELFKKDDA IMPNGTYTYV WQVPPRSGPT
     DNTEKCKSWA YYSGVNPEKD IHSGLIGPIL ICQKGMIDKY NRTIDIREFV LFFMVFDEEK
     SWYFPKSDKS TCEEKLIGVQ SLHTFPAING IPYQLQGLTM YKDENVHWHL LNMGGPKDIH
     VVNFHGQTFT EEGREDNQLG VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF
     TVIDKDCKLP MGLASGIIQD SQISASGHVG YWEPKLARLN NTGKYNAWSI IKKEHEHPWI
     QIDLQRQVVI TGIQTQGTVQ LLQHSYTVEY FVTYSEDGQN WITFKGRHSE TQMHFEGNSD
     GTTVKENHID PPIIARYIRL HPTKFYNRPT FRIELLGCEV EGCSVPLGME SGAIKNSEIT
     ASSYKKTWWS SWEPSLARLN LEGGTNAWQP EVNNKDQWLQ IDLQHLTKIT SIITQGATSM
     TTSMYVKTFS IHYTDDNSTW KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII
     PKTWNQYIAL RIELFGCEVF
//
DBGET integrated database retrieval system