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Database: UniProt
Entry: SCUB1_HUMAN
LinkDB: SCUB1_HUMAN
Original site: SCUB1_HUMAN 
ID   SCUB1_HUMAN             Reviewed;         988 AA.
AC   Q8IWY4; Q5R336;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=SCUBE1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-398 AND PRO-648, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=12270931; DOI=10.1074/jbc.m207410200;
RA   Yang R.-B., Ng C.K.D., Wasserman S.M., Colman S.D., Shenoy S., Mehraban F.,
RA   Koemueves L.G., Tomlinson J.E., Topper J.N.;
RT   "Identification of a novel family of cell-surface proteins expressed in
RT   human vascular endothelium.";
RL   J. Biol. Chem. 277:46364-46373(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16753137; DOI=10.1016/j.cardiores.2006.04.010;
RA   Tu C.-F., Su Y.-H., Huang Y.-N., Tsai M.-T., Li L.-T., Chen Y.-L.,
RA   Cheng C.-J., Dai D.-F., Yang R.-B.;
RT   "Localization and characterization of a novel secreted protein SCUBE1 in
RT   human platelets.";
RL   Cardiovasc. Res. 71:486-495(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [5]
RP   INTERACTION WITH SCUBE3.
RX   PubMed=33308444; DOI=10.1016/j.ajhg.2020.11.015;
RG   Genomics England Research Consortium;
RA   Lin Y.C., Niceta M., Muto V., Vona B., Pagnamenta A.T., Maroofian R.,
RA   Beetz C., van Duyvenvoorde H., Dentici M.L., Lauffer P., Vallian S.,
RA   Ciolfi A., Pizzi S., Bauer P., Gruening N.M., Bellacchio E.,
RA   Del Fattore A., Petrini S., Shaheen R., Tiosano D., Halloun R.,
RA   Pode-Shakked B., Albayrak H.M., Isik E., Wit J.M., Dittrich M.,
RA   Freire B.L., Bertola D.R., Jorge A.A.L., Barel O., Sabir A.H.,
RA   Al Tenaiji A.M.J., Taji S.M., Al-Sannaa N., Al-Abdulwahed H., Digilio M.C.,
RA   Irving M., Anikster Y., Bhavani G.S.L., Girisha K.M., Haaf T., Taylor J.C.,
RA   Dallapiccola B., Alkuraya F.S., Yang R.B., Tartaglia M.;
RT   "SCUBE3 loss-of-function causes a recognizable recessive developmental
RT   disorder due to defective bone morphogenetic protein signaling.";
RL   Am. J. Hum. Genet. 108:115-133(2021).
CC   -!- FUNCTION: Could function as an adhesive molecule and its matrix bound
CC       and soluble fragments may play a critical role in vascular biology.
CC       {ECO:0000269|PubMed:16753137}.
CC   -!- SUBUNIT: Forms homooligomers. Forms heterooligomers with SCUBE2. Forms
CC       heterooligomers with SCUBE3 (PubMed:33308444). {ECO:0000250,
CC       ECO:0000269|PubMed:33308444}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12270931,
CC       ECO:0000269|PubMed:16753137}. Cell membrane
CC       {ECO:0000269|PubMed:16753137}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16753137}.
CC   -!- TISSUE SPECIFICITY: Detected in endothelial cells. Highly expressed in
CC       platelets. Stored in platelet alpha granules, and transferred to the
CC       cell surface upon activation and aggregation. A smaller form, probably
CC       produced by limited proteolysis, after being released from the storage
CC       granules, is associated with thrombus and localized with the
CC       subendothelial matrices in atherosclerotic plaques.
CC       {ECO:0000269|PubMed:12270931, ECO:0000269|PubMed:16753137}.
CC   -!- INDUCTION: Down-regulated by inflammatory cytokines.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12270931}.
CC   -!- PTM: Could be proteolytically cleaved to release a smaller active
CC       fragment.
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DR   EMBL; AF525689; AAN77133.1; -; mRNA.
DR   EMBL; Z99756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z82214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS14048.1; -.
DR   RefSeq; NP_766638.2; NM_173050.3.
DR   AlphaFoldDB; Q8IWY4; -.
DR   STRING; 9606.ENSP00000354080; -.
DR   GlyCosmos; Q8IWY4; 6 sites, No reported glycans.
DR   GlyGen; Q8IWY4; 8 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q8IWY4; -.
DR   PhosphoSitePlus; Q8IWY4; -.
DR   BioMuta; SCUBE1; -.
DR   DMDM; 145559527; -.
DR   jPOST; Q8IWY4; -.
DR   MassIVE; Q8IWY4; -.
DR   PaxDb; 9606-ENSP00000354080; -.
DR   PeptideAtlas; Q8IWY4; -.
DR   ProteomicsDB; 70926; -.
DR   Antibodypedia; 306; 115 antibodies from 22 providers.
DR   DNASU; 80274; -.
DR   Ensembl; ENST00000360835.9; ENSP00000354080.3; ENSG00000159307.20.
DR   GeneID; 80274; -.
DR   KEGG; hsa:80274; -.
DR   MANE-Select; ENST00000360835.9; ENSP00000354080.3; NM_173050.5; NP_766638.2.
DR   UCSC; uc003bdt.3; human.
DR   AGR; HGNC:13441; -.
DR   CTD; 80274; -.
DR   DisGeNET; 80274; -.
DR   GeneCards; SCUBE1; -.
DR   HGNC; HGNC:13441; SCUBE1.
DR   HPA; ENSG00000159307; Tissue enhanced (ovary).
DR   MIM; 611746; gene.
DR   neXtProt; NX_Q8IWY4; -.
DR   OpenTargets; ENSG00000159307; -.
DR   PharmGKB; PA35019; -.
DR   VEuPathDB; HostDB:ENSG00000159307; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000153185; -.
DR   HOGENOM; CLU_013079_0_0_1; -.
DR   InParanoid; Q8IWY4; -.
DR   OMA; YQDVEGQ; -.
DR   OrthoDB; 5477406at2759; -.
DR   PhylomeDB; Q8IWY4; -.
DR   TreeFam; TF351672; -.
DR   PathwayCommons; Q8IWY4; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   BioGRID-ORCS; 80274; 21 hits in 1141 CRISPR screens.
DR   ChiTaRS; SCUBE1; human.
DR   GenomeRNAi; 80274; -.
DR   Pharos; Q8IWY4; Tbio.
DR   PRO; PR:Q8IWY4; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q8IWY4; Protein.
DR   Bgee; ENSG00000159307; Expressed in mucosa of stomach and 144 other cell types or tissues.
DR   ExpressionAtlas; Q8IWY4; baseline and differential.
DR   Genevisible; Q8IWY4; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0007512; P:adult heart development; NAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; NAS:UniProtKB.
DR   GO; GO:0045446; P:endothelial cell differentiation; NAS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; NAS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR24046:SF4; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF07699; Ephrin_rec_like; 3.
DR   Pfam; PF14670; FXa_inhibition; 3.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 6.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 6.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..988
FT                   /note="Signal peptide, CUB and EGF-like domain-containing
FT                   protein 1"
FT                   /id="PRO_0000254648"
FT   DOMAIN          33..73
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          74..116
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          117..153
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          166..202
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          206..241
FT                   /note="EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          245..280
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          282..322
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          323..361
FT                   /note="EGF-like 8; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          362..402
FT                   /note="EGF-like 9; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          798..910
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        466
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        750
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        779
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        789
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        286..297
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..306
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..321
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..337
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..346
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        366..377
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..386
FT                   /evidence="ECO:0000250"
FT   DISULFID        388..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        798..824
FT                   /evidence="ECO:0000250"
FT   DISULFID        851..872
FT                   /evidence="ECO:0000250"
FT   VARIANT         398
FT                   /note="G -> R (in dbSNP:rs129415)"
FT                   /evidence="ECO:0000269|PubMed:12270931"
FT                   /id="VAR_028850"
FT   VARIANT         648
FT                   /note="S -> P (in dbSNP:rs138993)"
FT                   /evidence="ECO:0000269|PubMed:12270931"
FT                   /id="VAR_028851"
FT   CONFLICT        53
FT                   /note="T -> A (in Ref. 1; AAN77133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="E -> G (in Ref. 1; AAN77133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="L -> P (in Ref. 1; AAN77133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   988 AA;  107910 MW;  AB2C2AB53F3D3C2B CRC64;
     MGAAAVRWHL CVLLALGTRG RLAGGSGLPG SVDVDECSEG TDDCHIDAIC QNTPKSYKCL
     CKPGYKGEGK QCEDIDECEN DYYNGGCVHE CINIPGNYRC TCFDGFMLAH DGHNCLDVDE
     CQDNNGGCQQ ICVNAMGSYE CQCHSGFFLS DNQHTCIHRS NEGMNCMNKD HGCAHICRET
     PKGGVACDCR PGFDLAQNQK DCTLTCNYGN GGCQHSCEDT DTGPTCGCHQ KYALHSDGRT
     CIETCAVNNG GCDRTCKDTA TGVRCSCPVG FTLQPDGKTC KDINECLVNN GGCDHFCRNT
     VGSFECGCRK GYKLLTDERT CQDIDECSFE RTCDHICINS PGSFQCLCHR GYILYGTTHC
     GDVDECSMSN GSCDQGCVNT KGSYECVCPP GRRLHWNGKD CVETGKCLSR AKTSPRAQLS
     CSKAGGVESC FLSCPAHTLF VPDSENSYVL SCGVPGPQGK ALQKRNGTSS GLGPSCSDAP
     TTPIKQKARF KIRDAKCHLR PHSQARAKET ARQPLLDHCH VTFVTLKCDS SKKRRRGRKS
     PSKEVSHITA EFEIETKMEE ASDTCEADCL RKRAEQSLQA AIKTLRKSIG RQQFYVQVSG
     TEYEVAQRPA KALEGQGACG AGQVLQDSKC VACGPGTHFG GELGQCVSCM PGTYQDMEGQ
     LSCTPCPSSD GLGLPGARNV SECGGQCSPG FFSADGFKPC QACPVGTYQP EPGRTGCFPC
     GGGLLTKHEG TTSFQDCEAK VHCSPGHHYN TTTHRCIRCP VGTYQPEFGQ NHCITCPGNT
     STDFDGSTNV THCKNQHCGG ELGDYTGYIE SPNYPGDYPA NAECVWHIAP PPKRRILIVV
     PEIFLPIEDE CGDVLVMRKS ASPTSITTYE TCQTYERPIA FTSRSRKLWI QFKSNEGNSG
     KGFQVPYVTY DEDYQQLIED IVRDGRLYAS ENHQEILKDK KLIKALFDVL AHPQNYFKYT
     AQESKEMFPR SFIKLLRSKV SRFLRPYK
//
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