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Database: UniProt
Entry: VHAA3_ARATH
LinkDB: VHAA3_ARATH
Original site: VHAA3_ARATH 
ID   VHAA3_ARATH             Reviewed;         821 AA.
AC   Q8W4S4; Q0WLI9; Q42216; Q56WQ9; Q9SVI5;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-APR-2018, entry version 111.
DE   RecName: Full=V-type proton ATPase subunit a3;
DE            Short=V-ATPase subunit a3;
DE   AltName: Full=V-type proton ATPase 95 kDa subunit a isoform 3;
DE            Short=V-ATPase 95 kDa isoform a3;
DE   AltName: Full=Vacuolar H(+)-ATPase subunit a isoform 3;
DE   AltName: Full=Vacuolar proton pump subunit a3;
DE   AltName: Full=Vacuolar proton translocating ATPase 95 kDa subunit a isoform 3;
GN   Name=VHA-a3; OrderedLocusNames=At4g39080; ORFNames=F19H22.180;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-569.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RA   Desprez T., Amselem J., Chiapello H., Caboche M., Hoefte H.;
RT   "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11950611; DOI=10.1016/S1360-1385(02)02240-9;
RA   Sze H., Schumacher K., Mueller M.L., Padmanaban S., Taiz L.;
RT   "A simple nomenclature for a complex proton pump: VHA genes encode the
RT   vacuolar H(+)-ATPase.";
RL   Trends Plant Sci. 7:157-161(2002).
RN   [7]
RP   SUBCELLULAR LOCATION, AND GENE FAMILY.
RX   PubMed=16461582; DOI=10.1105/tpc.105.037978;
RA   Dettmer J., Hong-Hermesdorf A., Stierhof Y.-D., Schumacher K.;
RT   "Vacuolar H(+)-ATPase activity is required for endocytic and secretory
RT   trafficking in Arabidopsis.";
RL   Plant Cell 18:715-730(2006).
RN   [8]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16581873; DOI=10.1104/pp.106.079533;
RA   Endler A., Meyer S., Schelbert S., Schneider T., Weschke W.,
RA   Peters S.W., Keller F., Baginsky S., Martinoia E., Schmidt U.G.;
RT   "Identification of a vacuolar sucrose transporter in barley and
RT   Arabidopsis mesophyll cells by a tonoplast proteomic approach.";
RL   Plant Physiol. 141:196-207(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=17151019; DOI=10.1074/mcp.M600250-MCP200;
RA   Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V.,
RA   Bruley C., Garin J., Bourguignon J.;
RT   "A proteomics dissection of Arabidopsis thaliana vacuoles isolated
RT   from cell culture.";
RL   Mol. Cell. Proteomics 6:394-412(2007).
RN   [10]
RP   DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=18441211; DOI=10.1105/tpc.108.058362;
RA   Bruex A., Liu T.-Y., Krebs M., Stierhof Y.-D., Lohmann J.U.,
RA   Miersch O., Wasternack C., Schumacher K.;
RT   "Reduced V-ATPase activity in the trans-Golgi network causes oxylipin-
RT   dependent hypocotyl growth Inhibition in Arabidopsis.";
RL   Plant Cell 20:1088-1100(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20133698; DOI=10.1073/pnas.0913035107;
RA   Krebs M., Beyhl D., Goerlich E., Al-Rasheid K.A.S., Marten I.,
RA   Stierhof Y.-D., Hedrich R., Schumacher K.;
RT   "Arabidopsis V-ATPase activity at the tonoplast is required for
RT   efficient nutrient storage but not for sodium accumulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3251-3256(2010).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. Involved in vacuolar nutrient storage (e.g.
CC       accumulation and storage of nitrate) and in tolerance to some
CC       toxic ions (e.g. zinc ions sequestration in vacuoles).
CC       {ECO:0000269|PubMed:20133698}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c'', d
CC       and e). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane
CC       {ECO:0000269|PubMed:16461582, ECO:0000269|PubMed:16581873,
CC       ECO:0000269|PubMed:17151019, ECO:0000269|PubMed:18441211}; Multi-
CC       pass membrane protein {ECO:0000255, ECO:0000269|PubMed:16461582,
CC       ECO:0000269|PubMed:16581873, ECO:0000269|PubMed:18441211}.
CC   -!- TISSUE SPECIFICITY: Expressed in etiolated seedlings hypocotyls.
CC       {ECO:0000269|PubMed:18441211}.
CC   -!- DISRUPTION PHENOTYPE: When associated with VHA-a2 disruption, day-
CC       length-dependent growth retardation associated with a reduced
CC       accumulation and storage of nitrate ions in vacuoles. Increased
CC       sensitivity to zinc ions due to a lower zinc ions sequestration in
CC       vacuoles. Reduced calcium content. No effect on sensitivity to
CC       sodium ions. {ECO:0000269|PubMed:18441211,
CC       ECO:0000269|PubMed:20133698}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB38828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035679; CAB38828.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161594; CAB80571.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE87015.1; -; Genomic_DNA.
DR   EMBL; AY060557; AAL31187.1; -; mRNA.
DR   EMBL; BT002615; AAO11531.1; -; mRNA.
DR   EMBL; AK221976; BAD94513.1; -; mRNA.
DR   EMBL; AK227321; BAE99335.1; -; mRNA.
DR   EMBL; AK230210; BAF02018.1; -; mRNA.
DR   EMBL; Z29167; CAA82406.1; -; mRNA.
DR   PIR; T06068; T06068.
DR   RefSeq; NP_568051.1; NM_120068.5.
DR   UniGene; At.10101; -.
DR   UniGene; At.70994; -.
DR   ProteinModelPortal; Q8W4S4; -.
DR   BioGrid; 15343; 1.
DR   STRING; 3702.AT4G39080.1; -.
DR   iPTMnet; Q8W4S4; -.
DR   SwissPalm; Q8W4S4; -.
DR   PaxDb; Q8W4S4; -.
DR   PRIDE; Q8W4S4; -.
DR   EnsemblPlants; AT4G39080.1; AT4G39080.1; AT4G39080.
DR   GeneID; 830063; -.
DR   Gramene; AT4G39080.1; AT4G39080.1; AT4G39080.
DR   KEGG; ath:AT4G39080; -.
DR   Araport; AT4G39080; -.
DR   TAIR; locus:2120217; AT4G39080.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q8W4S4; -.
DR   KO; K02154; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG093602BG; -.
DR   PhylomeDB; Q8W4S4; -.
DR   Reactome; R-ATH-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-ATH-6798695; Neutrophil degranulation.
DR   Reactome; R-ATH-77387; Insulin receptor recycling.
DR   Reactome; R-ATH-917977; Transferrin endocytosis and recycling.
DR   PRO; PR:Q8W4S4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8W4S4; baseline and differential.
DR   Genevisible; Q8W4S4; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IDA:TAIR.
DR   GO; GO:0045735; F:nutrient reservoir activity; IMP:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IDA:TAIR.
DR   GO; GO:0032119; P:sequestering of zinc ion; IMP:UniProtKB.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IMP:UniProtKB.
DR   GO; GO:0043181; P:vacuolar sequestering; IMP:UniProtKB.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Complete proteome; Hydrogen ion transport;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    821       V-type proton ATPase subunit a3.
FT                                /FTId=PRO_0000419781.
FT   TOPO_DOM      2    421       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    422    442       Helical. {ECO:0000255}.
FT   TOPO_DOM    443    469       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    470    490       Helical. {ECO:0000255}.
FT   TOPO_DOM    491    548       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    549    569       Helical. {ECO:0000255}.
FT   TOPO_DOM    570    581       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    582    602       Helical. {ECO:0000255}.
FT   TOPO_DOM    603    640       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    641    661       Helical. {ECO:0000255}.
FT   TOPO_DOM    662    758       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    759    779       Helical. {ECO:0000255}.
FT   TOPO_DOM    780    821       Cytoplasmic. {ECO:0000255}.
FT   COILED       97    144       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   MOD_RES     174    174       Phosphoserine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   CONFLICT    512    513       AT -> VP (in Ref. 5; CAA82406).
FT                                {ECO:0000305}.
FT   CONFLICT    728    728       L -> M (in Ref. 4; BAF02018).
FT                                {ECO:0000305}.
SQ   SEQUENCE   821 AA;  92833 MW;  576EDE3C6545EA49 CRC64;
     MAESGGGGGC CPPMDLMRSE TMQLVQLIVP MESAHLTVSY LGDLGLVQFK DLNSEKSPFQ
     RTYAAQIKRC GEMARKIRFF RDQMSKAGVP AKEMQGKEND IDLDDVEVKL GELEAELVEI
     NANNDKLQRS YNELMEYKLV LQKAGEFFSS AHRSAADQQR ETESQQAGED LLESPLLQEE
     KSIDSTKQVK LGFLTGLVPR EKSMVFERIL FRATRGNIFI RQTVIEEPVI DPNSGEKAEK
     NVFVVFYSGE RAKSKILKIC EAFGANRYPF SEDLGRQAQM ITEVSGRLSE LKTTIDAGLG
     QRNILLQTIG DKFELWNLKV RKEKAIYHTL NMLSLDVTKK CLVAEGWSPV FASREIQDAL
     QRAAVDSNSQ VGSIFQVLRT KESPPTYFRT NKFTSAIQEI VDAYGVAKYQ EANPGVFTIV
     TFPFLFAVMF GDWGHGICIL LATMYLILKE KKLASQKLGD IMEMAFGGRY VILMMSLFSI
     YTGLIYNEFF SIPFPLFAPS AYDCRDVSCS EATTIGLIKV RDTYPFGLDP VWHGSRSELP
     FLNSLKMKMS ILLGVSQMNL GIIMSYFNAR FFKSSVNIWF QFIPQMIFLN SLFGYLSVLI
     IIKWCTGSQA DLYHVMIYMF LSPMDELGEN QLFPHQKTLQ LVLLFLALVS VPCMLLPKPF
     ILKKQHEARH QGQAYAPLDE TDESLHVETN GGGSHGHEEF EFSEIFVHQL IHTIEFVLGA
     VSNTASYLRL WALSLAHSEL SSVFYEKVLL LAWGYNNPLI LIVGVLVFIF ATVGVLLVME
     TLSAFLHALR LHWVEFQNKF YEGDGYKFAP FTFIFTANED E
//
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