GenomeNet

Database: UniProt
Entry: Q0QF01
LinkDB: Q0QF01
Original site: Q0QF01 
ID   SDHA_PIG                Reviewed;         664 AA.
AC   Q0QF01; A0SNV1;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   07-NOV-2018, entry version 75.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000305|PubMed:15989954};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=SDHA;
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], PROTEIN SEQUENCE OF 43-47, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Heart;
RX   PubMed=17480203; DOI=10.1111/j.1742-4658.2007.05698.x;
RA   Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F.,
RA   Rao Z.;
RT   "Preliminary molecular characterization and crystallization of
RT   mitochondrial respiratory complex II from porcine heart.";
RL   FEBS J. 274:1524-1529(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-599.
RC   TISSUE=Liver;
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 165-663.
RX   PubMed=17697375; DOI=10.1186/1471-2199-8-67;
RA   Nygard A.B., Jorgensen C.B., Cirera S., Fredholm M.;
RT   "Selection of reference genes for gene expression studies in pig
RT   tissues using SYBR green qPCR.";
RL   BMC Mol. Biol. 8:67-67(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND
RP   SUBSTRATE ANALOG 3-NITROPROPIONATE, FUNCTION, CATALYTIC ACTIVITY,
RP   PATHWAY, COFACTOR, AND SUBUNIT.
RX   PubMed=15989954; DOI=10.1016/j.cell.2005.05.025;
RA   Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.;
RT   "Crystal structure of mitochondrial respiratory membrane protein
RT   complex II.";
RL   Cell 121:1043-1057(2005).
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q) (Probable). Can act as a
CC       tumor suppressor (By similarity). {ECO:0000250|UniProtKB:P31040,
CC       ECO:0000305|PubMed:15989954}.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {ECO:0000305|PubMed:15989954}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:15989954};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC       {ECO:0000305|PubMed:15989954}.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
CC       cytochrome b560 composed of SDHC and SDHD (PubMed:15989954,
CC       PubMed:17480203). Interacts with SDHAF2/SDH5; interaction is
CC       required for FAD attachment (By similarity). Interacts with TRAP1
CC       (By similarity). {ECO:0000250|UniProtKB:P31040,
CC       ECO:0000269|PubMed:15989954, ECO:0000269|PubMed:17480203}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:17480203}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:17480203}; Matrix side
CC       {ECO:0000269|PubMed:17480203}.
CC   -!- PTM: Phosphorylation at Tyr-215 is important for efficient
CC       electron transfer in complex II and the prevention of ROS
CC       generation. {ECO:0000250|UniProtKB:P31040}.
CC   -!- PTM: Acetylated. Deacetylated by SIRT3.
CC       {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI29191.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DQ402993; ABD77326.1; -; mRNA.
DR   EMBL; DQ845177; ABI29191.1; ALT_INIT; mRNA.
DR   UniGene; Ssc.24988; -.
DR   PDB; 1ZOY; X-ray; 2.40 A; A=43-664.
DR   PDB; 1ZP0; X-ray; 3.50 A; A=43-664.
DR   PDB; 3ABV; X-ray; 3.24 A; A=43-664.
DR   PDB; 3AE1; X-ray; 3.14 A; A=43-664.
DR   PDB; 3AE2; X-ray; 3.10 A; A=43-664.
DR   PDB; 3AE3; X-ray; 3.35 A; A=43-664.
DR   PDB; 3AE4; X-ray; 2.91 A; A=43-664.
DR   PDB; 3AE5; X-ray; 3.41 A; A=43-664.
DR   PDB; 3AE6; X-ray; 3.40 A; A=43-664.
DR   PDB; 3AE7; X-ray; 3.62 A; A=43-664.
DR   PDB; 3AE8; X-ray; 3.40 A; A=43-664.
DR   PDB; 3AE9; X-ray; 3.31 A; A=43-664.
DR   PDB; 3AEA; X-ray; 3.39 A; A=43-664.
DR   PDB; 3AEB; X-ray; 3.00 A; A=43-664.
DR   PDB; 3AEC; X-ray; 3.61 A; A=43-664.
DR   PDB; 3AED; X-ray; 3.52 A; A=43-664.
DR   PDB; 3AEE; X-ray; 3.22 A; A=43-664.
DR   PDB; 3AEF; X-ray; 2.80 A; A=43-664.
DR   PDB; 3AEG; X-ray; 3.27 A; A=43-664.
DR   PDB; 3SFD; X-ray; 2.61 A; A=43-664.
DR   PDB; 3SFE; X-ray; 2.81 A; A=43-664.
DR   PDB; 4YTP; X-ray; 3.10 A; A=1-664.
DR   PDB; 4YXD; X-ray; 3.00 A; A=1-664.
DR   PDBsum; 1ZOY; -.
DR   PDBsum; 1ZP0; -.
DR   PDBsum; 3ABV; -.
DR   PDBsum; 3AE1; -.
DR   PDBsum; 3AE2; -.
DR   PDBsum; 3AE3; -.
DR   PDBsum; 3AE4; -.
DR   PDBsum; 3AE5; -.
DR   PDBsum; 3AE6; -.
DR   PDBsum; 3AE7; -.
DR   PDBsum; 3AE8; -.
DR   PDBsum; 3AE9; -.
DR   PDBsum; 3AEA; -.
DR   PDBsum; 3AEB; -.
DR   PDBsum; 3AEC; -.
DR   PDBsum; 3AED; -.
DR   PDBsum; 3AEE; -.
DR   PDBsum; 3AEF; -.
DR   PDBsum; 3AEG; -.
DR   PDBsum; 3SFD; -.
DR   PDBsum; 3SFE; -.
DR   PDBsum; 4YTP; -.
DR   PDBsum; 4YXD; -.
DR   ProteinModelPortal; Q0QF01; -.
DR   SMR; Q0QF01; -.
DR   PeptideAtlas; Q0QF01; -.
DR   PRIDE; Q0QF01; -.
DR   Ensembl; ENSSSCT00000031591; ENSSSCP00000026945; ENSSSCG00000020686.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q0QF01; -.
DR   Reactome; R-SSC-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   EvolutionaryTrace; Q0QF01; -.
DR   Proteomes; UP000008227; Chromosome 16.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:0055114; P:oxidation-reduction process; IC:UniProtKB.
DR   GO; GO:0022904; P:respiratory electron transport chain; IC:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT       1     42       Mitochondrion.
FT                                {ECO:0000269|PubMed:17480203}.
FT   CHAIN        43    664       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000391718.
FT   NP_BIND      68     73       FAD. {ECO:0000269|PubMed:15989954}.
FT   NP_BIND      91    106       FAD. {ECO:0000269|PubMed:15989954}.
FT   NP_BIND     456    457       FAD. {ECO:0000269|PubMed:15989954}.
FT   ACT_SITE    340    340       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     275    275       FAD. {ECO:0000269|PubMed:15989954}.
FT   BINDING     296    296       Substrate. {ECO:0000269|PubMed:15989954}.
FT   BINDING     308    308       Substrate. {ECO:0000269|PubMed:15989954}.
FT   BINDING     407    407       Substrate. {ECO:0000269|PubMed:15989954}.
FT   BINDING     440    440       FAD. {ECO:0000269|PubMed:15989954}.
FT   BINDING     451    451       Substrate. {ECO:0000269|PubMed:15989954}.
FT   MOD_RES      99     99       Tele-8alpha-FAD histidine.
FT                                {ECO:0000269|PubMed:15989954}.
FT   MOD_RES     167    167       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     179    179       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     179    179       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     182    182       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     215    215       Phosphotyrosine; by SRC.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     335    335       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     335    335       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     480    480       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     485    485       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     485    485       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     498    498       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     498    498       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     517    517       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     538    538       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     538    538       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     550    550       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     598    598       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     608    608       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     615    615       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     624    624       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     633    633       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     636    636       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     647    647       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   CONFLICT    165    171       DGKIYQR -> LQESARG (in Ref. 3; ABI29191).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       L -> S (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    235    235       I -> T (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    358    358       G -> N (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    453    453       G -> E (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    509    509       S -> W (in Ref. 2; ABD77326).
FT                                {ECO:0000305}.
FT   CONFLICT    566    566       L -> P (in Ref. 2; ABD77326).
FT                                {ECO:0000305}.
FT   STRAND       57     61       {ECO:0000244|PDB:1ZOY}.
FT   STRAND       63     67       {ECO:0000244|PDB:1ZOY}.
FT   HELIX        71     82       {ECO:0000244|PDB:1ZOY}.
FT   STRAND       87     93       {ECO:0000244|PDB:1ZOY}.
FT   HELIX        95     97       {ECO:0000244|PDB:1ZOY}.
FT   HELIX        99    102       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      113    115       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       119    129       {ECO:0000244|PDB:1ZOY}.
FT   TURN        130    132       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       136    156       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      166    168       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      170    178       {ECO:0000244|PDB:1ZOY}.
FT   TURN        179    182       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      185    190       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       196    208       {ECO:0000244|PDB:1ZOY}.
FT   TURN        209    212       {ECO:0000244|PDB:4YXD}.
FT   STRAND      214    217       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      219    227       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      230    238       {ECO:0000244|PDB:1ZOY}.
FT   TURN        239    241       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      244    248       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      250    254       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       260    262       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      263    268       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       275    282       {ECO:0000244|PDB:1ZOY}.
FT   TURN        289    291       {ECO:0000244|PDB:4YXD}.
FT   STRAND      293    297       {ECO:0000244|PDB:1ZOY}.
FT   TURN        301    303       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       310    314       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      317    319       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      323    325       {ECO:0000244|PDB:3AE2}.
FT   TURN        327    329       {ECO:0000244|PDB:3SFD}.
FT   TURN        332    336       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       340    353       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      357    361       {ECO:0000244|PDB:3SFD}.
FT   STRAND      365    367       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      369    371       {ECO:0000244|PDB:3AE1}.
FT   HELIX       375    378       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       381    391       {ECO:0000244|PDB:1ZOY}.
FT   TURN        395    397       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      400    402       {ECO:0000244|PDB:4YXD}.
FT   STRAND      405    409       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      412    415       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      419    425       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      428    437       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       439    441       {ECO:0000244|PDB:3AEF}.
FT   STRAND      442    444       {ECO:0000244|PDB:3SFD}.
FT   HELIX       456    474       {ECO:0000244|PDB:1ZOY}.
FT   TURN        486    489       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       490    500       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      505    507       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       508    522       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      523    527       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       529    545       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      548    550       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       560    584       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      587    589       {ECO:0000244|PDB:3AE6}.
FT   STRAND      594    596       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      606    608       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      610    613       {ECO:0000244|PDB:1ZOY}.
FT   HELIX       618    620       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      624    630       {ECO:0000244|PDB:1ZOY}.
FT   TURN        632    634       {ECO:0000244|PDB:1ZOY}.
FT   STRAND      637    642       {ECO:0000244|PDB:1ZOY}.
FT   TURN        651    653       {ECO:0000244|PDB:1ZOY}.
SQ   SEQUENCE   664 AA;  72832 MW;  0120E14F7F6F60EE CRC64;
     MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA ISTQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAR NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLAVRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLRHVNGQDQ VVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK
     VPSIKPNAGE ESVMNLDKLR FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL
     RLYGDLQHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER
     VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN EADCATVPPA
     IRSY
//
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