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Database: UniProt/SWISS-PROT
Entry: PFKAL_MOUSE
LinkDB: PFKAL_MOUSE
Original site: PFKAL_MOUSE 
ID   PFKAL_MOUSE             Reviewed;         780 AA.
AC   P12382; Q8VDX7;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   16-JAN-2019, entry version 177.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase, liver type {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=PFK-L;
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=6-phosphofructokinase type B;
DE   AltName: Full=Phosphofructo-1-kinase isozyme B;
DE            Short=PFK-B;
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=Pfkl {ECO:0000312|MGI:MGI:97547}; Synonyms=Pfk-l, Pfkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2969893;
RA   Gehnrich S.C., Gekakis N., Sul H.S.;
RT   "Liver (B-type) phosphofructokinase mRNA. Cloning, structure, and
RT   expression.";
RL   J. Biol. Chem. 263:11755-11759(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Pituitary;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 130-141; 257-269; 367-374; 655-672 AND 716-726,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-640, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION.
RX   PubMed=26194095; DOI=10.1038/ncomms8838;
RA   Graham D.B., Becker C.E., Doan A., Goel G., Villablanca E.J.,
RA   Knights D., Mok A., Ng A.C., Doench J.G., Root D.E., Clish C.B.,
RA   Xavier R.J.;
RT   "Functional genomics identifies negative regulatory nodes controlling
RT   phagocyte oxidative burst.";
RL   Nat. Commun. 6:7838-7838(2015).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis (By similarity). Negatively regulates the phagocyte
CC       oxidative burst in response to bacterial infection by controlling
CC       cellular NADPH biosynthesis and NADPH oxidase-derived reactive
CC       oxygen species. Upon macrophage activation, drives the metabolic
CC       switch toward glycolysis, thus preventing glucose turnover that
CC       produces NADPH via pentose phosphate pathway (PubMed:26194095).
CC       {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:26194095}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. GlcNAcylation by OGT overcomes allosteric regulation (By
CC       similarity). {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homo- and heterotetramers (By similarity).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity,
CC       leading to redirect glucose flux through the oxidative pentose
CC       phosphate pathway. Glycosylation is stimulated by both hypoxia and
CC       glucose deprivation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
DR   EMBL; J03928; AAA20076.1; -; mRNA.
DR   EMBL; AK030511; BAC26997.1; -; mRNA.
DR   EMBL; AK036318; BAC29382.1; -; mRNA.
DR   EMBL; AK081313; BAC38193.1; -; mRNA.
DR   EMBL; AK159328; BAE34994.1; -; mRNA.
DR   EMBL; CH466553; EDL31763.1; -; Genomic_DNA.
DR   EMBL; BC020097; AAH20097.1; -; mRNA.
DR   CCDS; CCDS35955.1; -.
DR   PIR; A31070; A31070.
DR   RefSeq; NP_032852.2; NM_008826.4.
DR   UniGene; Mm.269649; -.
DR   ProteinModelPortal; P12382; -.
DR   SMR; P12382; -.
DR   BioGrid; 202124; 6.
DR   ComplexPortal; CPX-2052; 6-phosphofructokinase, L4 homotetramer.
DR   ComplexPortal; CPX-2055; 6-phosphofructokinase, ML3 heterotetramer.
DR   ComplexPortal; CPX-2056; 6-phosphofructokinase, M2L2 heterotetramer.
DR   ComplexPortal; CPX-2057; 6-phosphofructokinase, M3L heterotetramer.
DR   IntAct; P12382; 10.
DR   MINT; P12382; -.
DR   STRING; 10090.ENSMUSP00000020522; -.
DR   iPTMnet; P12382; -.
DR   PhosphoSitePlus; P12382; -.
DR   SwissPalm; P12382; -.
DR   EPD; P12382; -.
DR   jPOST; P12382; -.
DR   MaxQB; P12382; -.
DR   PaxDb; P12382; -.
DR   PeptideAtlas; P12382; -.
DR   PRIDE; P12382; -.
DR   Ensembl; ENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277.
DR   GeneID; 18641; -.
DR   KEGG; mmu:18641; -.
DR   UCSC; uc007fwo.2; mouse.
DR   CTD; 5211; -.
DR   MGI; MGI:97547; Pfkl.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000159292; -.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P12382; -.
DR   KO; K00850; -.
DR   OMA; DPFNIQD; -.
DR   OrthoDB; 172878at2759; -.
DR   TreeFam; TF300411; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-70171; Glycolysis.
DR   SABIO-RK; P12382; -.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:P12382; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000020277; Expressed in 347 organ(s), highest expression level in stria vascularis of cochlear duct.
DR   CleanEx; MM_PFKL; -.
DR   ExpressionAtlas; P12382; baseline and differential.
DR   Genevisible; P12382; MM.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:MGI.
DR   GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0070061; F:fructose binding; ISO:MGI.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR   GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:MGI.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR   GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IDA:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
DR   GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   GO; GO:0009749; P:response to glucose; IDA:MGI.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Glycoprotein;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P17858}.
FT   CHAIN         2    780       ATP-dependent 6-phosphofructokinase,
FT                                liver type.
FT                                /FTId=PRO_0000112022.
FT   NP_BIND      88     89       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     118    121       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        2    390       N-terminal catalytic PFK domain 1.
FT   REGION      164    166       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      208    210       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      298    301       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      391    400       Interdomain linker.
FT   REGION      401    780       C-terminal regulatory PFK domain 2.
FT   REGION      527    531       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      572    574       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      660    663       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       119    119       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      25     25       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     201    201       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     292    292       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     470    470       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     565    565       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     628    628       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     654    654       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     734    734       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P17858}.
FT   MOD_RES     377    377       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47857}.
FT   MOD_RES     640    640       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18034455}.
FT   MOD_RES     775    775       Phosphoserine.
FT                                {ECO:0000244|PubMed:19131326}.
FT   CARBOHYD    529    529       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   CONFLICT    419    419       R -> P (in Ref. 1; AAA20076).
FT                                {ECO:0000305}.
SQ   SEQUENCE   780 AA;  85360 MW;  0C12E2C222020B7F CRC64;
     MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE
     GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA AAYNLLQHGI TNLCVIGGDG
     SLTGANIFRN EWGSLLEELV KEGKISESTA QNYAHLTIAG LVGSIDNDFC GTDMTIGTDS
     ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE
     NFMCERLGET RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
     RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME CVQVTKDVQK
     AMDEERFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF SLAILNVGAP AAGMNAAVRS
     AVRTGISEGH TVYIVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI
     VENLRTYNIH ALLVIGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG
     SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
     IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV FDCRTNVLGH
     LQQGGAPTPF DRNYGTKLGV KAMLWVSEKL RDVYRKGRVF ANAPDSACVI GLRKKVVAFS
     PVTELKKETD FEHRMPREQW WLNLRLMLKM LAHYRISMAD YVSGELEHVT RRTLSIDKGF
//
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