GenomeNet

Database: UniProt/SWISS-PROT
Entry: GPDM_HUMAN
LinkDB: GPDM_HUMAN
Original site: GPDM_HUMAN 
ID   GPDM_HUMAN              Reviewed;         727 AA.
AC   P43304; A8K4V0; B3KSA9; Q59FR1; Q9HAP9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   27-SEP-2017, entry version 175.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase, mitochondrial;
DE            Short=GPD-M;
DE            Short=GPDH-M;
DE            EC=1.1.5.3;
DE   AltName: Full=mtGPD;
DE   Flags: Precursor;
GN   Name=GPD2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-264 AND
RP   HIS-525.
RX   PubMed=7821823; DOI=10.1016/0378-1119(94)90469-3;
RA   Lehn D.A., Brown L.J., Simonson G.D., Moran S.M., McDonald M.J.;
RT   "The sequence of a human mitochondrial glycerol-3-phosphate
RT   dehydrogenase-encoding cDNA.";
RL   Gene 150:417-418(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-264.
RX   PubMed=8549872; DOI=10.2337/diab.45.2.262;
RA   Ferrer J., Aoki M., Behn P., Nestorowicz A., Riggs A., Permutt M.A.;
RT   "Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an
RT   alternatively spliced human islet-cell cDNA, tissue distribution,
RT   physical mapping, and identification of a polymorphic genetic
RT   marker.";
RL   Diabetes 45:262-266(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-264.
RX   PubMed=8682323; DOI=10.1016/0378-1119(96)00019-4;
RA   Brown L.J., Stoffel M., Moran S.M., Fernald A.A., Lehn D.A.,
RA   LeBeau M.M., MacDonald M.J.;
RT   "Structural organization and mapping of the human mitochondrial
RT   glycerol phosphate dehydrogenase-encoding gene and pseudogene.";
RL   Gene 172:309-312(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-264 AND
RP   HIS-525.
RC   TISSUE=Testis;
RA   Yin L.L., Li J.M., Sha J.H.;
RT   "A novel glycerol-3-phosphate dehydrogenase 3 from adult testis.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   HIS-264.
RC   TISSUE=Testis, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   HIS-264.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-264.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-408, AND VARIANT HIS-264.
RC   TISSUE=Brain;
RX   PubMed=9110174;
RA   Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA   Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT   "Large-scale concatenation cDNA sequencing.";
RL   Genome Res. 7:353-358(1997).
RN   [10]
RP   PROTEIN SEQUENCE OF 212-227 AND 558-572, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [11]
RP   PROTEIN SEQUENCE OF 340-348; 410-418; 526-538; 558-572 AND 715-722,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Platelet;
RA   Bienvenut W.V., Claeys D.;
RL   Submitted (JAN-2006) to UniProtKB.
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- ENZYME REGULATION: Calcium-binding enhance the activity of the
CC       enzyme.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P43304-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P43304-2; Sequence=VSP_017134;
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92636.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; U12424; AAA65701.1; -; mRNA.
DR   EMBL; U36310; AAB60403.1; -; mRNA.
DR   EMBL; U40367; AAC50556.1; -; Genomic_DNA.
DR   EMBL; U40353; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40354; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40355; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40357; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40358; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40359; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40360; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40361; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40362; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40363; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40364; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; U40365; AAC50556.1; JOINED; Genomic_DNA.
DR   EMBL; AF311325; AAG33851.1; -; mRNA.
DR   EMBL; AK093198; BAG52671.1; -; mRNA.
DR   EMBL; AK291065; BAF83754.1; -; mRNA.
DR   EMBL; AK292817; BAF85506.1; -; mRNA.
DR   EMBL; AB209399; BAD92636.1; ALT_INIT; mRNA.
DR   EMBL; AC011308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471058; EAX11453.1; -; Genomic_DNA.
DR   EMBL; U79250; AAB50200.1; -; mRNA.
DR   CCDS; CCDS2202.1; -. [P43304-1]
DR   PIR; G02093; G02093.
DR   RefSeq; NP_000399.3; NM_000408.4. [P43304-1]
DR   RefSeq; NP_001076581.2; NM_001083112.2. [P43304-1]
DR   RefSeq; XP_005246526.1; XM_005246469.2. [P43304-1]
DR   RefSeq; XP_011509279.1; XM_011510977.2. [P43304-1]
DR   RefSeq; XP_016859319.1; XM_017003830.1. [P43304-1]
DR   UniGene; Hs.512382; -.
DR   ProteinModelPortal; P43304; -.
DR   SMR; P43304; -.
DR   BioGrid; 109081; 32.
DR   IntAct; P43304; 4.
DR   MINT; MINT-4530883; -.
DR   STRING; 9606.ENSP00000308610; -.
DR   ChEMBL; CHEMBL3391681; -.
DR   SwissLipids; SLP:000000147; -.
DR   iPTMnet; P43304; -.
DR   PhosphoSitePlus; P43304; -.
DR   SwissPalm; P43304; -.
DR   BioMuta; GPD2; -.
DR   DMDM; 229462943; -.
DR   REPRODUCTION-2DPAGE; IPI00017895; -.
DR   UCD-2DPAGE; P43304; -.
DR   EPD; P43304; -.
DR   MaxQB; P43304; -.
DR   PaxDb; P43304; -.
DR   PeptideAtlas; P43304; -.
DR   PRIDE; P43304; -.
DR   Ensembl; ENST00000310454; ENSP00000308610; ENSG00000115159. [P43304-1]
DR   Ensembl; ENST00000409125; ENSP00000386484; ENSG00000115159. [P43304-2]
DR   Ensembl; ENST00000409674; ENSP00000386425; ENSG00000115159. [P43304-1]
DR   Ensembl; ENST00000409861; ENSP00000386626; ENSG00000115159. [P43304-1]
DR   Ensembl; ENST00000438166; ENSP00000409708; ENSG00000115159. [P43304-1]
DR   GeneID; 2820; -.
DR   KEGG; hsa:2820; -.
DR   UCSC; uc002tzd.5; human. [P43304-1]
DR   CTD; 2820; -.
DR   DisGeNET; 2820; -.
DR   EuPathDB; HostDB:ENSG00000115159.15; -.
DR   GeneCards; GPD2; -.
DR   H-InvDB; HIX0002519; -.
DR   HGNC; HGNC:4456; GPD2.
DR   HPA; HPA008012; -.
DR   HPA; HPA045506; -.
DR   MalaCards; GPD2; -.
DR   MIM; 138430; gene.
DR   neXtProt; NX_P43304; -.
DR   OpenTargets; ENSG00000115159; -.
DR   PharmGKB; PA28837; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   eggNOG; COG0578; LUCA.
DR   GeneTree; ENSGT00390000001718; -.
DR   HOGENOM; HOG000004813; -.
DR   HOVERGEN; HBG005897; -.
DR   InParanoid; P43304; -.
DR   KO; K00111; -.
DR   OMA; VPYYWVG; -.
DR   OrthoDB; EOG091G03ER; -.
DR   PhylomeDB; P43304; -.
DR   TreeFam; TF300359; -.
DR   BioCyc; MetaCyc:HS03841-MONOMER; -.
DR   BRENDA; 1.1.5.3; 2681.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-163560; Triglyceride catabolism.
DR   UniPathway; UPA00618; UER00673.
DR   ChiTaRS; GPD2; human.
DR   GenomeRNAi; 2820; -.
DR   PRO; PR:P43304; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000115159; -.
DR   CleanEx; HS_GPD2; -.
DR   ExpressionAtlas; P43304; baseline and differential.
DR   Genevisible; P43304; HS.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; TAS:Reactome.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006127; P:glycerophosphate shuttle; TAS:Reactome.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome;
KW   Direct protein sequencing; FAD; Flavoprotein; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion. {ECO:0000250}.
FT   CHAIN        43    727       Glycerol-3-phosphate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000010429.
FT   DOMAIN      623    658       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      659    694       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND      71     99       FAD. {ECO:0000255}.
FT   CA_BIND     672    683       {ECO:0000255|PROSITE-ProRule:PRU00448}.
FT   MOD_RES     601    601       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q64521}.
FT   VAR_SEQ       1    126       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_017134.
FT   VARIANT     264    264       R -> H (in dbSNP:rs2116665).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:7821823,
FT                                ECO:0000269|PubMed:8549872,
FT                                ECO:0000269|PubMed:8682323,
FT                                ECO:0000269|PubMed:9110174,
FT                                ECO:0000269|Ref.4, ECO:0000269|Ref.6,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_049113.
FT   VARIANT     453    453       K -> Q (in dbSNP:rs35096779).
FT                                /FTId=VAR_049114.
FT   VARIANT     525    525       R -> H (in dbSNP:rs1051916).
FT                                {ECO:0000269|PubMed:7821823,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_025215.
SQ   SEQUENCE   727 AA;  80853 MW;  70D8B4E5CB4F2EFD CRC64;
     MAFQKAVKGT ILVGGGALAT VLGLSQFAHY RRKQMNLAYV KAADCISEPV NREPPSREAQ
     LLTLQNTSEF DILVIGGGAT GSGCALDAVT RGLKTALVER DDFSSGTSSR STKLIHGGVR
     YLQKAIMKLD IEQYRMVKEA LHERANLLEI APHLSAPLPI MLPVYKWWQL PYYWVGIKLY
     DLVAGSNCLK SSYVLSKSRA LEHFPMLQKD KLVGAIVYYD GQHNDARMNL AIALTAARYG
     AATANYMEVV SLLKKTDPQT GKVRVSGARC KDVLTGQEFD VRAKCVINAT GPFTDSVRKM
     DDKDAAAICQ PSAGVHIVMP GYYSPESMGL LDPATSDGRV IFFLPWQKMT IAGTTDTPTD
     VTHHPIPSEE DINFILNEVR NYLSCDVEVR RGDVLAAWSG IRPLVTDPKS ADTQSISRNH
     VVDISESGLI TIAGGKWTTY RSMAEDTINA AVKTHNLKAG PSRTVGLFLQ GGKDWSPTLY
     IRLVQDYGLE SEVAQHLAAT YGDKAFEVAK MASVTGKRWP IVGVRLVSEF PYIEAEVKYG
     IKEYACTAVD MISRRTRLAF LNVQAAEEAL PRIVELMGRE LNWDDYKKQE QLETARKFLY
     YEMGYKSRSE QLTDRSEISL LPSDIDRYKK RFHKFDADQK GFITIVDVQR VLESINVQMD
     ENTLHEILNE VDLNKNGQVE LNEFLQLMSA IQKGRVSGSR LAILMKTAEE NLDRRVPIPV
     DRSCGGL
//
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