GenomeNet

Database: UniProt
Entry: ITA8_MOUSE
LinkDB: ITA8_MOUSE
Original site: ITA8_MOUSE 
ID   ITA8_MOUSE              Reviewed;        1062 AA.
AC   A2ARA8; O70304; Q3UXV8; Q8BRG3; Q8C0H7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   01-OCT-2014, entry version 74.
DE   RecName: Full=Integrin alpha-8;
DE   Contains:
DE     RecName: Full=Integrin alpha-8 heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-8 light chain;
DE   Flags: Precursor;
GN   Name=Itga8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 45-1056 (ISOFORM 1), FUNCTION,
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Fibroblast;
RX   PubMed=9054500; DOI=10.1016/S0092-8674(00)81903-0;
RA   Mueller U., Wang D., Denda S., Meneses J.J., Pedersen R.A.,
RA   Reichardt L.F.;
RT   "Integrin alpha8beta1 is critically important for epithelial-
RT   mesenchymal interactions during kidney morphogenesis.";
RL   Cell 88:603-613(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=9548928; DOI=10.1021/bi9727489;
RA   Denda S., Mueller U., Crossin K.L., Erickson H.P., Reichardt L.F.;
RT   "Utilization of a soluble integrin-alkaline phosphatase chimera to
RT   characterize integrin alpha 8 beta 1 receptor interactions with
RT   tenascin: murine alpha 8 beta 1 binds to the RGD site in tenascin-C
RT   fragments, but not to native tenascin-C.";
RL   Biochemistry 37:5464-5474(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=9614184; DOI=10.1091/mbc.9.6.1425;
RA   Denda S., Reichardt L.F., Mueller U.;
RT   "Identification of osteopontin as a novel ligand for the integrin
RT   alpha8 beta1 and potential roles for this integrin-ligand interaction
RT   in kidney morphogenesis.";
RL   Mol. Biol. Cell 9:1425-1435(1998).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=10024342;
RA   Pinkstaff J.K., Detterich J., Lynch G., Gall C.;
RT   "Integrin subunit gene expression is regionally differentiated in
RT   adult brain.";
RL   J. Neurosci. 19:1541-1556(1999).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=10504498; DOI=10.1046/j.1523-1755.1999.00662.x;
RA   Hartner A., Schoecklmann H., Proels F., Mueller U., Sterzel R.B.;
RT   "Alpha8 integrin in glomerular mesangial cells and in experimental
RT   glomerulonephritis.";
RL   Kidney Int. 56:1468-1480(1999).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=10742111; DOI=10.1038/74286;
RA   Littlewood Evans A., Mueller U.;
RT   "Stereocilia defects in the sensory hair cells of the inner ear in
RT   mice deficient in integrin alpha8beta1.";
RL   Nat. Genet. 24:424-428(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11470831; DOI=10.1083/jcb.200103069;
RA   Brandenberger R., Schmidt A., Linton J., Wang D., Backus C., Denda S.,
RA   Mueller U., Reichardt L.F.;
RT   "Identification and characterization of a novel extracellular matrix
RT   protein nephronectin that is associated with integrin alpha8beta1 in
RT   the embryonic kidney.";
RL   J. Cell Biol. 154:447-458(2001).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11891185; DOI=10.1016/S0002-9440(10)64909-7;
RA   Hartner A., Cordasic N., Klanke B., Mueller U., Sterzel R.B.,
RA   Hilgers K.F.;
RT   "The alpha8 integrin chain affords mechanical stability to the
RT   glomerular capillary tuft in hypertensive glomerular disease.";
RL   Am. J. Pathol. 160:861-867(2002).
RN   [11]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14500699; DOI=10.1177/002215540305101008;
RA   Wagner T.E., Frevert C.W., Herzog E.L., Schnapp L.M.;
RT   "Expression of the integrin subunit alpha8 in murine lung
RT   development.";
RL   J. Histochem. Cytochem. 51:1307-1315(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=12787402; DOI=10.1046/j.1523-1755.2003.00057.x;
RA   Bieritz B., Spessotto P., Colombatti A., Jahn A., Prols F.,
RA   Hartner A.;
RT   "Role of alpha8 integrin in mesangial cell adhesion, migration, and
RT   proliferation.";
RL   Kidney Int. 64:119-127(2003).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17537792; DOI=10.1242/dev.005033;
RA   Linton J.M., Martin G.R., Reichardt L.F.;
RT   "The ECM protein nephronectin promotes kidney development via integrin
RT   alpha8beta1-mediated stimulation of Gdnf expression.";
RL   Development 134:2501-2509(2007).
CC   -!- FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of
CC       kidney and probably of other organs by regulating the recruitment
CC       of mesenchymal cells into epithelial structures. It recognizes the
CC       sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1
CC       TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in
CC       kidney genesis. Neuronal receptor for TNC it mediates cell-cell
CC       interactions and regulates neurite outgrowth of sensory and motor
CC       neurons. {ECO:0000269|PubMed:10742111,
CC       ECO:0000269|PubMed:11470831, ECO:0000269|PubMed:11891185,
CC       ECO:0000269|PubMed:12787402, ECO:0000269|PubMed:17537792,
CC       ECO:0000269|PubMed:9054500, ECO:0000269|PubMed:9548928,
CC       ECO:0000269|PubMed:9614184}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
CC       subunit is composed of a heavy and a light chain linked by a
CC       disulfide bond. Alpha-8 associates with beta-1.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10742111};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:10742111}.
CC       Cell membrane {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2ARA8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2ARA8-2; Sequence=VSP_027364, VSP_027365;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: In brain, expressed in deep cortex,
CC       hippocampal CA1, basolateral amygdala and striatum. In kidney,
CC       expressed in glomerular mesengium (at protein level).
CC       {ECO:0000269|PubMed:10024342, ECO:0000269|PubMed:10504498}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in mesenchymal cells of developing
CC       organs such as gut, lung, gonads and nephrogenic cord.
CC       {ECO:0000269|PubMed:14500699, ECO:0000269|PubMed:9054500}.
CC   -!- DISRUPTION PHENOTYPE: Mice display renal agenesis and dysgenesis.
CC       This is associated with a reduced expression of Gdnf that is
CC       similarly found in mice lacking Npnt. Adult mice also display
CC       increased susceptibility to glomerular capillary destruction upon
CC       mechanical stress. Mice lacking Itga8 also have difficulty
CC       balancing associated with structural defects in the inner ear
CC       where utricular hair cells lack stereocilia.
CC       {ECO:0000269|PubMed:10742111, ECO:0000269|PubMed:11891185,
CC       ECO:0000269|PubMed:17537792, ECO:0000269|PubMed:9054500}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats. {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; AK031326; BAC27348.1; -; mRNA.
DR   EMBL; AK044910; BAC32137.1; -; mRNA.
DR   EMBL; AK135193; BAE22455.1; -; mRNA.
DR   EMBL; AL845313; CAM17354.1; -; Genomic_DNA.
DR   EMBL; AF041409; AAC15665.1; -; mRNA.
DR   CCDS; CCDS15689.1; -. [A2ARA8-1]
DR   RefSeq; NP_001001309.1; NM_001001309.2. [A2ARA8-1]
DR   UniGene; Mm.329997; -.
DR   ProteinModelPortal; A2ARA8; -.
DR   SMR; A2ARA8; 38-1001, 1008-1048.
DR   IntAct; A2ARA8; 1.
DR   MINT; MINT-4105300; -.
DR   PhosphoSite; A2ARA8; -.
DR   MaxQB; A2ARA8; -.
DR   PaxDb; A2ARA8; -.
DR   PRIDE; A2ARA8; -.
DR   Ensembl; ENSMUST00000028106; ENSMUSP00000028106; ENSMUSG00000026768. [A2ARA8-1]
DR   GeneID; 241226; -.
DR   KEGG; mmu:241226; -.
DR   UCSC; uc008ijk.1; mouse. [A2ARA8-1]
DR   UCSC; uc008ijl.1; mouse. [A2ARA8-2]
DR   CTD; 8516; -.
DR   MGI; MGI:109442; Itga8.
DR   eggNOG; NOG26407; -.
DR   GeneTree; ENSGT00750000117267; -.
DR   HOGENOM; HOG000231603; -.
DR   HOVERGEN; HBG006186; -.
DR   InParanoid; A2ARA8; -.
DR   KO; K06584; -.
DR   OMA; CRQIPFD; -.
DR   OrthoDB; EOG7HQN77; -.
DR   PhylomeDB; A2ARA8; -.
DR   TreeFam; TF105391; -.
DR   Reactome; REACT_196606; ECM proteoglycans.
DR   Reactome; REACT_198998; Molecules associated with elastic fibres.
DR   Reactome; REACT_216309; Integrin cell surface interactions.
DR   NextBio; 384935; -.
DR   PRO; PR:A2ARA8; -.
DR   ArrayExpress; A2ARA8; -.
DR   Bgee; A2ARA8; -.
DR   CleanEx; MM_ITGA8; -.
DR   Genevestigator; A2ARA8; -.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0032591; C:dendritic spine membrane; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0001656; P:metanephros development; IMP:MGI.
DR   GO; GO:2000721; P:positive regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:BHF-UCL.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 6.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Integrin; Membrane; Metal-binding; Neurogenesis; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36   1062       Integrin alpha-8.
FT                                /FTId=PRO_0000297709.
FT   CHAIN        38    905       Integrin alpha-8 heavy chain.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000297710.
FT   CHAIN       906   1062       Integrin alpha-8 light chain.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000297711.
FT   TOPO_DOM     36   1010       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1011   1031       Helical. {ECO:0000255}.
FT   TOPO_DOM   1032   1062       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       41    104       FG-GAP 1.
FT   REPEAT      121    182       FG-GAP 2.
FT   REPEAT      187    239       FG-GAP 3.
FT   REPEAT      252    309       FG-GAP 4.
FT   REPEAT      310    371       FG-GAP 5.
FT   REPEAT      372    430       FG-GAP 6.
FT   REPEAT      434    497       FG-GAP 7.
FT   CA_BIND     328    336       {ECO:0000255}.
FT   CA_BIND     394    402       {ECO:0000255}.
FT   CA_BIND     458    466       {ECO:0000255}.
FT   MOTIF       454    456       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    176    176       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    238    238       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    301    301       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    310    310       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    503    503       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    600    600       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    604    604       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    718    718       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    736    736       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    752    752       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    779    779       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    895    895       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    922    922       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1004   1004       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     95    105       {ECO:0000250}.
FT   DISULFID    149    170       {ECO:0000250}.
FT   DISULFID    186    199       {ECO:0000250}.
FT   DISULFID    506    517       {ECO:0000250}.
FT   DISULFID    523    579       {ECO:0000250}.
FT   DISULFID    640    646       {ECO:0000250}.
FT   DISULFID    712    725       {ECO:0000250}.
FT   DISULFID    866    923       Interchain (between heavy and light
FT                                chains). {ECO:0000250}.
FT   DISULFID    928    933       {ECO:0000250}.
FT   VAR_SEQ     282    286       ELVAG -> GQRHP (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_027364.
FT   VAR_SEQ     287   1062       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_027365.
FT   CONFLICT     66     66       D -> G (in Ref. 1; BAE22455).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1062 AA;  117556 MW;  DB1ACA43FADD3AC0 CRC64;
     MSAGTHCGPP GNRAPPFARL CCVSAALGML WSPACLAFNL DVDKLTVYSG PEGSYFGYSL
     DFYIPDARTA SVLVGAPKAN TSQPDIVEGG AVYYCPWPSE RSAQCKQIPF DTTNNRKIRV
     NGTKEPIEFK SNQWFGATVR AHKGKVVACA PLYHWRTLKP NPAKDPVGTC YVAIQNFSAY
     AEHSPCRNSN ADPEGQGYCQ AGFSLDFYKN GDLIVGGPGS FYWQGQVITV SIADIIANYS
     FKDILRKLAA EKQTDVAPAS YDDSYLGYSV AAGEFTGDSQ QELVAGIPRG AQNFGYVSII
     NSTDMTFIQN FTGEQMASYF GYTVVVSDVN NDGMDDILVG APLFMEREFE SNPREVGQVY
     LYLQASALLF QDPQVLTGTE TFGRFGSSVA HLGDLNQDGY NDIAIGVPFA GKDQRGKVLI
     YNGNPRGLHS KPSQVLQGIW GSQTIPSGFG FSLRGDADID KNDYPDLLVG AFGKGKVAVY
     RARPVVTVDA QLLLHPMIIN LENKTCQIPE FPTPVACFSV RVCASIAGQS ISNTIALLAE
     VQLDFLKQKG AIKRTLFLHN HQSHFTFPFV MKQQKSLHCQ DFMVYLRDET EFRDKLSPIN
     ISLNYSLDDS TFKDSLEVKP ILNHYRDNVV TEQAHILVDC GEDNLCVPDL KLSARPDKHQ
     IIIGDENHLM LIINARNEGE GAYEAELFVI IPEEADYVGI ERNNKGLRPL SCEYKMENVT
     RMVVCDLGNP MVTGTNFSLG LRFAVPRLEK TNMSINFDLQ IRSSNKDNPD SNFERVQINI
     TAIAQVEIRG VSHPPQIVLP IHNWEPEKKP HKEEEVGPLV EHIYELHNIG PSTISDSILD
     VGWPFSARDE FLLYIFHLQT LGPLQCQTNP EINPQDIKPA ASPEDTPELS AFLRNATIPH
     LVRKRDVPVV QLHRQSPARI LNCTNIDCLQ ISCAVGRLGG GESAVLKVRS RLWAHTFLKR
     KNDHYALASL VSFEVKKMPY KEQPAKLPAG STAVKTSVIW ATPNVSFSIP LWVIILAILL
     GLLVLAILTL ALWKCGFFDR ARPPQDEMTD REQLTSDKTP EA
//
DBGET integrated database retrieval system