GenomeNet

Database: UniProt
Entry: P18084
LinkDB: P18084
Original site: P18084 
ID   ITB5_HUMAN              Reviewed;         799 AA.
AC   P18084; B0LPF8; B2RD70;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   10-APR-2019, entry version 202.
DE   RecName: Full=Integrin beta-5;
DE   Flags: Precursor;
GN   Name=ITGB5;
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].
RC   TISSUE=Thymic epithelium;
RX   PubMed=2328726;
RA   Ramaswamy H., Hemler M.E.;
RT   "Cloning, primary structure and properties of a novel human integrin
RT   beta subunit.";
RL   EMBO J. 9:1561-1568(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2371275; DOI=10.1073/pnas.87.14.5354;
RA   Suzuki S., Huang Z.S., Tanihara H.;
RT   "Cloning of an integrin beta subunit exhibiting high homology with
RT   integrin beta 3 subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5354-5358(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2211615;
RA   McLean J.W., Vestal D.J., Cheresh D.A., Bodary S.C.;
RT   "cDNA sequence of the human integrin beta 5 subunit.";
RL   J. Biol. Chem. 265:17126-17131(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-431.
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [7]
RP   INTERACTION WITH MYO10.
RX   PubMed=15156152; DOI=10.1038/ncb1136;
RA   Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA   Cheney R.E., Stromblad S.;
RT   "Myosin-X provides a motor-based link between integrins and the
RT   cytoskeleton.";
RL   Nat. Cell Biol. 6:523-531(2004).
RN   [8]
RP   INTERACTION WITH CCN3.
RX   PubMed=15611078; DOI=10.1074/jbc.M404903200;
RA   Lin C.G., Chen C.C., Leu S.J., Grzeszkiewicz T.M., Lau L.F.;
RT   "Integrin-dependent functions of the angiogenic inducer NOV (CCN3):
RT   implication in wound healing.";
RL   J. Biol. Chem. 280:8229-8237(2005).
RN   [9]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS TYPE C
RP   PENTON PROTEIN.
RX   PubMed=20615244; DOI=10.1186/1743-422X-7-148;
RA   Lyle C., McCormick F.;
RT   "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-
RT   negative cells.";
RL   Virol. J. 7:148-148(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for
CC       fibronectin. It recognizes the sequence R-G-D in its ligand.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a
CC       receptor for adenovirus type C. {ECO:0000269|PubMed:20615244}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5
CC       (ITGB5) associates with alpha-V (ITGAV). Interacts with MYO10
CC       (PubMed:15156152). Interacts with DAB2. Integrin ITGAV:ITGB5
CC       interacts with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB5
CC       interacts with CCN3 (PubMed:15611078).
CC       {ECO:0000250|UniProtKB:O70309, ECO:0000269|PubMed:15156152,
CC       ECO:0000269|PubMed:15611078}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB5 interacts with
CC       adenovirus type C penton protein. {ECO:0000269|PubMed:20615244}.
CC   -!- INTERACTION:
CC       Q9BY76:ANGPTL4; NbExp=3; IntAct=EBI-1223434, EBI-2968146;
CC       Q7Z6J6:FRMD5; NbExp=3; IntAct=EBI-1223434, EBI-727282;
CC       P06756:ITGAV; NbExp=2; IntAct=EBI-1223434, EBI-298282;
CC       Q9HD67:MYO10; NbExp=2; IntAct=EBI-1223434, EBI-307061;
CC       P97479:Myo7a (xeno); NbExp=8; IntAct=EBI-1223434, EBI-1149557;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; X53002; CAA37188.1; -; mRNA.
DR   EMBL; M35011; AAA52707.1; -; mRNA.
DR   EMBL; J05633; AAA59183.1; -; mRNA.
DR   EMBL; AK315429; BAG37817.1; -; mRNA.
DR   EMBL; EU332848; ABY87537.1; -; Genomic_DNA.
DR   EMBL; BC006541; AAH06541.1; -; mRNA.
DR   CCDS; CCDS3030.1; -.
DR   PIR; A38308; A38308.
DR   RefSeq; NP_002204.2; NM_002213.4.
DR   UniGene; Hs.13155; -.
DR   UniGene; Hs.536663; -.
DR   ProteinModelPortal; P18084; -.
DR   SMR; P18084; -.
DR   BioGrid; 109899; 42.
DR   ComplexPortal; CPX-1796; Integrin alphav-beta5 complex.
DR   CORUM; P18084; -.
DR   ELM; P18084; -.
DR   IntAct; P18084; 38.
DR   MINT; P18084; -.
DR   STRING; 9606.ENSP00000296181; -.
DR   BindingDB; P18084; -.
DR   ChEMBL; CHEMBL2096675; -.
DR   GlyConnect; 1418; -.
DR   iPTMnet; P18084; -.
DR   PhosphoSitePlus; P18084; -.
DR   BioMuta; ITGB5; -.
DR   DMDM; 124970; -.
DR   EPD; P18084; -.
DR   jPOST; P18084; -.
DR   MaxQB; P18084; -.
DR   PaxDb; P18084; -.
DR   PeptideAtlas; P18084; -.
DR   PRIDE; P18084; -.
DR   ProteomicsDB; 53546; -.
DR   DNASU; 3693; -.
DR   Ensembl; ENST00000296181; ENSP00000296181; ENSG00000082781.
DR   GeneID; 3693; -.
DR   KEGG; hsa:3693; -.
DR   UCSC; uc003eho.4; human.
DR   CTD; 3693; -.
DR   DisGeNET; 3693; -.
DR   EuPathDB; HostDB:ENSG00000082781.11; -.
DR   GeneCards; ITGB5; -.
DR   HGNC; HGNC:6160; ITGB5.
DR   HPA; CAB022050; -.
DR   HPA; HPA001820; -.
DR   MIM; 147561; gene.
DR   neXtProt; NX_P18084; -.
DR   OpenTargets; ENSG00000082781; -.
DR   PharmGKB; PA29959; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P18084; -.
DR   KO; K06588; -.
DR   OMA; PECGTAP; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P18084; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000170; Syndecan interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR   SignaLink; P18084; -.
DR   SIGNOR; P18084; -.
DR   ChiTaRS; ITGB5; human.
DR   GeneWiki; Integrin,_beta_5; -.
DR   GenomeRNAi; 3693; -.
DR   PRO; PR:P18084; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000082781; Expressed in 230 organ(s), highest expression level in thoracic aorta.
DR   ExpressionAtlas; P18084; baseline and differential.
DR   Genevisible; P18084; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR   GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027067; Integrin_beta-5.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF26; PTHR10082:SF26; 1.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
KW   Host cell receptor for virus entry; Host-virus interaction; Integrin;
KW   Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    799       Integrin beta-5.
FT                                /FTId=PRO_0000016348.
FT   TOPO_DOM     24    719       Extracellular. {ECO:0000255}.
FT   TRANSMEM    720    742       Helical. {ECO:0000255}.
FT   TOPO_DOM    743    799       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27     76       PSI.
FT   DOMAIN      136    378       VWFA.
FT   REPEAT      465    512       I.
FT   REPEAT      513    554       II.
FT   REPEAT      555    593       III.
FT   REPEAT      594    630       IV.
FT   REGION      465    630       Cysteine-rich tandem repeats.
FT   MOD_RES     770    770       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    460    460       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    477    477       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    505    505       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    552    552       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    586    586       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    654    654       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    705    705       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28    463       {ECO:0000250}.
FT   DISULFID     36     46       {ECO:0000250}.
FT   DISULFID     39     75       {ECO:0000250}.
FT   DISULFID     49     64       {ECO:0000250}.
FT   DISULFID    202    211       {ECO:0000250}.
FT   DISULFID    259    300       {ECO:0000250}.
FT   DISULFID    401    413       {ECO:0000250}.
FT   DISULFID    433    682       {ECO:0000250}.
FT   DISULFID    461    465       {ECO:0000250}.
FT   DISULFID    476    487       {ECO:0000250}.
FT   DISULFID    484    522       {ECO:0000250}.
FT   DISULFID    489    498       {ECO:0000250}.
FT   DISULFID    500    513       {ECO:0000250}.
FT   DISULFID    528    533       {ECO:0000250}.
FT   DISULFID    530    563       {ECO:0000250}.
FT   DISULFID    535    548       {ECO:0000250}.
FT   DISULFID    550    555       {ECO:0000250}.
FT   DISULFID    569    574       {ECO:0000250}.
FT   DISULFID    571    602       {ECO:0000250}.
FT   DISULFID    576    585       {ECO:0000250}.
FT   DISULFID    587    594       {ECO:0000250}.
FT   DISULFID    608    613       {ECO:0000250}.
FT   DISULFID    610    657       {ECO:0000250}.
FT   DISULFID    615    625       {ECO:0000250}.
FT   DISULFID    628    631       {ECO:0000250}.
FT   DISULFID    635    644       {ECO:0000250}.
FT   DISULFID    641    714       {ECO:0000250}.
FT   DISULFID    661    690       {ECO:0000250}.
FT   VARIANT     428    428       L -> V (in dbSNP:rs2291090).
FT                                /FTId=VAR_024290.
FT   VARIANT     431    431       R -> Q (in dbSNP:rs2291089).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_049634.
FT   VARIANT     477    477       N -> S (in dbSNP:rs2291087).
FT                                /FTId=VAR_049635.
FT   CONFLICT    193    193       T -> A (in Ref. 2; AAA52707).
FT                                {ECO:0000305}.
FT   CONFLICT    645    645       L -> P (in Ref. 3; AAA59183).
FT                                {ECO:0000305}.
FT   CONFLICT    790    792       Missing (in Ref. 2; AAA52707).
FT                                {ECO:0000305}.
SQ   SEQUENCE   799 AA;  88054 MW;  D7E4727CA310512B CRC64;
     MPRAPAPLYA CLLGLCALLP RLAGLNICTS GSATSCEECL LIHPKCAWCS KEDFGSPRSI
     TSRCDLRANL VKNGCGGEIE SPASSFHVLR SLPLSSKGSG SAGWDVIQMT PQEIAVNLRP
     GDKTTFQLQV RQVEDYPVDL YYLMDLSLSM KDDLDNIRSL GTKLAEEMRK LTSNFRLGFG
     SFVDKDISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS
     RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC
     HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL
     DGDSKNIIQL IINAYNSIRS KVELSVWDQP EDLNLFFTAT CQDGVSYPGQ RKCEGLKIGD
     TASFEVSLEA RSCPSRHTEH VFALRPVGFR DSLEVGVTYN CTCGCSVGLE PNSARCNGSG
     TYVCGLCECS PGYLGTRCEC QDGENQSVYQ NLCREAEGKP LCSGRGDCSC NQCSCFESEF
     GKIYGPFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD ISTCRGRDGQ
     ICSERGHCLC GQCQCTEPGA FGEMCEKCPT CPDACSTKRD CVECLLLHSG KPDNQTCHSL
     CRDEVITWVD TIVKDDQEAV LCFYKTAKDC VMMFTYVELP SGKSNLTVLR EPECGNTPNA
     MTILLAVVGS ILLVGLALLA IWKLLVTIHD RREFAKFQSE RSRARYEMAS NPLYRKPIST
     HTVDFTFNKF NKSYNGTVD
//
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