GenomeNet

Database: UniProt
Entry: Q9NQX1
LinkDB: Q9NQX1
Original site: Q9NQX1 
ID   PRDM5_HUMAN             Reviewed;         630 AA.
AC   Q9NQX1; Q0VAI9; Q0VAJ0; Q6NXQ7;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   13-FEB-2019, entry version 166.
DE   RecName: Full=PR domain zinc finger protein 5;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 5;
GN   Name=PRDM5; Synonyms=PFM2;
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), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15077163; DOI=10.1038/sj.onc.1207615;
RA   Deng Q., Huang S.;
RT   "PRDM5 is silenced in human cancers and has growth suppressive
RT   activities.";
RL   Oncogene 23:4903-4910(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Brain;
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   TISSUE SPECIFICITY.
RX   PubMed=17699856; DOI=10.1158/1078-0432.CCR-07-0305;
RA   Watanabe Y., Toyota M., Kondo Y., Suzuki H., Imai T., Ohe-Toyota M.,
RA   Maruyama R., Nojima M., Sasaki Y., Sekido Y., Hiratsuka H.,
RA   Shinomura Y., Imai K., Itoh F., Tokino T.;
RT   "PRDM5 identified as a target of epigenetic silencing in colorectal
RT   and gastric cancer.";
RL   Clin. Cancer Res. 13:4786-4794(2007).
RN   [6]
RP   FUNCTION, INTERACTION WITH EHMT2; GFI1 AND HDAC1, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17636019; DOI=10.1128/MCB.00762-07;
RA   Duan Z., Person R.E., Lee H.-H., Huang S., Donadieu J., Badolato R.,
RA   Grimes H.L., Papayannopoulou T., Horwitz M.S.;
RT   "Epigenetic regulation of protein-coding and microRNA genes by the
RT   Gfi1-interacting tumor suppressor PRDM5.";
RL   Mol. Cell. Biol. 27:6889-6902(2007).
RN   [7]
RP   VARIANT BCS2 CYS-107, AND FUNCTION.
RX   PubMed=21664999; DOI=10.1016/j.ajhg.2011.05.007;
RA   Burkitt Wright E.M., Spencer H.L., Daly S.B., Manson F.D., Zeef L.A.,
RA   Urquhart J., Zoppi N., Bonshek R., Tosounidis I., Mohan M., Madden C.,
RA   Dodds A., Chandler K.E., Banka S., Au L., Clayton-Smith J., Khan N.,
RA   Biesecker L.G., Wilson M., Rohrbach M., Colombi M., Giunta C.,
RA   Black G.C.;
RT   "Mutations in PRDM5 in brittle cornea syndrome identify a pathway
RT   regulating extracellular matrix development and maintenance.";
RL   Am. J. Hum. Genet. 88:767-777(2011).
CC   -!- FUNCTION: Sequence-specific DNA-binding transcription factor.
CC       Represses transcription at least in part by recruitment of the
CC       histone methyltransferase EHMT2/G9A and histone deacetylases such
CC       as HDAC1. Regulates hematopoiesis-associated protein-coding and
CC       microRNA (miRNA) genes. May regulate the expression of proteins
CC       involved in extracellular matrix development and maintenance,
CC       including fibrillar collagens, such as COL4A1 and COL11A1,
CC       connective tissue components, such as HAPLN1, and molecules
CC       regulating cell migration and adhesion, including EDIL3 and TGFB2.
CC       May caused G2/M arrest and apoptosis in cancer cells.
CC       {ECO:0000269|PubMed:15077163, ECO:0000269|PubMed:17636019,
CC       ECO:0000269|PubMed:21664999}.
CC   -!- SUBUNIT: Interacts with EHMT2/G9A, GFI1 and HDAC1.
CC       {ECO:0000269|PubMed:17636019}.
CC   -!- INTERACTION:
CC       Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-4292031, EBI-744366;
CC       Q99684:GFI1; NbExp=2; IntAct=EBI-4292031, EBI-949368;
CC       Q13547:HDAC1; NbExp=3; IntAct=EBI-4292031, EBI-301834;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15077163,
CC       ECO:0000269|PubMed:17636019}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9NQX1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQX1-2; Sequence=VSP_035654;
CC       Name=3;
CC         IsoId=Q9NQX1-3; Sequence=VSP_035652, VSP_035653;
CC       Name=4;
CC         IsoId=Q9NQX1-4; Sequence=VSP_035654, VSP_054395, VSP_054396;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in colon
CC       and ovary. Tends to be silenced in breast, colorectal, gastric and
CC       liver cancer tissues. {ECO:0000269|PubMed:15077163,
CC       ECO:0000269|PubMed:17699856}.
CC   -!- DISEASE: Brittle cornea syndrome 2 (BCS2) [MIM:614170]: A disorder
CC       characterized by extreme corneal thinning resulting in corneal
CC       rupture after minor trauma, blue sclerae, keratoconus or
CC       keratoglobus, hyperelasticity of the skin, and hypermobile joints.
CC       {ECO:0000269|PubMed:21664999}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AF272897; AAF78077.1; -; mRNA.
DR   EMBL; AK056352; BAG51686.1; -; mRNA.
DR   EMBL; AC025741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066942; AAH66942.1; -; mRNA.
DR   EMBL; BC121037; AAI21038.1; -; mRNA.
DR   EMBL; BC121038; AAI21039.1; -; mRNA.
DR   CCDS; CCDS3716.1; -. [Q9NQX1-1]
DR   CCDS; CCDS75187.1; -. [Q9NQX1-4]
DR   CCDS; CCDS75188.1; -. [Q9NQX1-2]
DR   RefSeq; NP_001287752.1; NM_001300823.1. [Q9NQX1-2]
DR   RefSeq; NP_001287753.1; NM_001300824.1. [Q9NQX1-4]
DR   RefSeq; NP_061169.2; NM_018699.3. [Q9NQX1-1]
DR   UniGene; Hs.666782; -.
DR   ProteinModelPortal; Q9NQX1; -.
DR   SMR; Q9NQX1; -.
DR   BioGrid; 116287; 43.
DR   IntAct; Q9NQX1; 11.
DR   STRING; 9606.ENSP00000264808; -.
DR   MoonDB; Q9NQX1; Predicted.
DR   iPTMnet; Q9NQX1; -.
DR   PhosphoSitePlus; Q9NQX1; -.
DR   SwissPalm; Q9NQX1; -.
DR   BioMuta; PRDM5; -.
DR   DMDM; 212276458; -.
DR   PaxDb; Q9NQX1; -.
DR   PeptideAtlas; Q9NQX1; -.
DR   PRIDE; Q9NQX1; -.
DR   ProteomicsDB; 82218; -.
DR   ProteomicsDB; 82219; -. [Q9NQX1-2]
DR   ProteomicsDB; 82220; -. [Q9NQX1-3]
DR   Ensembl; ENST00000264808; ENSP00000264808; ENSG00000138738. [Q9NQX1-1]
DR   Ensembl; ENST00000394435; ENSP00000377955; ENSG00000138738. [Q9NQX1-3]
DR   Ensembl; ENST00000428209; ENSP00000404832; ENSG00000138738. [Q9NQX1-2]
DR   Ensembl; ENST00000515109; ENSP00000422309; ENSG00000138738. [Q9NQX1-4]
DR   GeneID; 11107; -.
DR   KEGG; hsa:11107; -.
DR   UCSC; uc003idn.4; human. [Q9NQX1-1]
DR   CTD; 11107; -.
DR   DisGeNET; 11107; -.
DR   EuPathDB; HostDB:ENSG00000138738.10; -.
DR   GeneCards; PRDM5; -.
DR   HGNC; HGNC:9349; PRDM5.
DR   HPA; HPA051406; -.
DR   MalaCards; PRDM5; -.
DR   MIM; 614161; gene.
DR   MIM; 614170; phenotype.
DR   neXtProt; NX_Q9NQX1; -.
DR   OpenTargets; ENSG00000138738; -.
DR   Orphanet; 90354; Brittle cornea syndrome.
DR   PharmGKB; PA33717; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000158340; -.
DR   HOGENOM; HOG000234617; -.
DR   HOVERGEN; HBG098380; -.
DR   InParanoid; Q9NQX1; -.
DR   KO; K22534; -.
DR   OMA; MDNIHGE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9NQX1; -.
DR   TreeFam; TF106478; -.
DR   ChiTaRS; PRDM5; human.
DR   GenomeRNAi; 11107; -.
DR   PRO; PR:Q9NQX1; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000138738; Expressed in 145 organ(s), highest expression level in stomach.
DR   ExpressionAtlas; Q9NQX1; baseline and differential.
DR   Genevisible; Q9NQX1; HS.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070491; F:repressing transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0016575; P:histone deacetylation; IMP:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR017125; Znf_PRDM5-like.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   PIRSF; PIRSF037162; PRDM; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 16.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Disease mutation; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    630       PR domain zinc finger protein 5.
FT                                /FTId=PRO_0000047761.
FT   DOMAIN        8    124       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     167    190       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     199    221       C2H2-type 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     234    256       C2H2-type 3; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     262    287       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     295    317       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     320    342       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     348    370       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     376    398       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     404    426       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     432    455       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     461    483       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     489    511       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     517    539       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     545    567       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     573    595       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     602    625       C2H2-type 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   VAR_SEQ     101    111       EGENIFYLAVE -> DKNLGPAEWRG (in isoform
FT                                3). {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035652.
FT   VAR_SEQ     112    630       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035653.
FT   VAR_SEQ     218    248       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035654.
FT   VAR_SEQ     515    532       RPYQCPYCEKGFSKNDGL -> AVQVLRVQQGLQPEARPG
FT                                (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054395.
FT   VAR_SEQ     533    630       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054396.
FT   VARIANT     107    107       Y -> C (in BCS2; dbSNP:rs387907111).
FT                                {ECO:0000269|PubMed:21664999}.
FT                                /FTId=VAR_066393.
FT   CONFLICT    261    261       R -> K (in Ref. 1; AAF78077).
FT                                {ECO:0000305}.
SQ   SEQUENCE   630 AA;  73090 MW;  D16AF81AB5A34398 CRC64;
     MLGMYVPDRF SLKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE NMDYRLMWEV
     RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QEQKNLAAIQ EGENIFYLAV EDIETDTELL
     IGYLDSDMEA EEEEQQIMTV IKEGEVENSR RQSTAGRKDR LGCKEDYACP QCESSFTSED
     ILAEHLQTLH QKPTEEKEFK CKNCGKKFPV KQALQRHVLQ CTAKSSLKES SRSFQCSVCN
     SSFSSASSFE QHQETCRGDA RFVCKADSCG KRLKSKDALK RHQENVHTGD PKKKLICSVC
     NKKCSSASSL QEHRKIHEIF DCQECMKKFI SANQLKRHMI THSEKRPYNC EICNKSFKRL
     DQVGAHKVIH SEDKPYKCKL CGKGFAHRNV YKNHKKTHSE ERPFQCEECK ALFRTPFSLQ
     RHLLIHNSER TFKCHHCDAT FKRKDTLNVH VQVVHERHKK YRCELCNKAF VTPSVLRSHK
     KTHTGEKEKI CPYCGQKFAS SGTLRVHIRS HTGERPYQCP YCEKGFSKND GLKMHIRTHT
     REKPYKCSEC SKAFSQKRGL DEHKRTHTGE KPFQCDVCDL AFSLKKMLIR HKMTHNPNRP
     LAECQFCHKK FTRNDYLKVH MDNIHGVADS
//
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