GenomeNet

Database: UniProt
Entry: P57071
LinkDB: P57071
Original site: P57071 
ID   PRD15_HUMAN             Reviewed;        1507 AA.
AC   P57071; E9PDJ6; E9PF37; E9PGL3; Q4W8S0; Q4W8S3; Q4W8S4; Q4W8S5;
AC   Q8N0X3; Q8NEX0; Q9NQV3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 4.
DT   13-FEB-2019, entry version 179.
DE   RecName: Full=PR domain zinc finger protein 15 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
DE   AltName: Full=PR domain-containing protein 15 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 298;
GN   Name=PRDM15 {ECO:0000312|HGNC:HGNC:13999};
GN   Synonyms=C21orf83 {ECO:0000312|HGNC:HGNC:13999},
GN   ZNF298 {ECO:0000312|HGNC:HGNC:13999};
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).
RX   PubMed=12036298; DOI=10.1006/geno.2002.6782;
RA   Gardiner K., Slavov D., Bechtel L., Davisson M.;
RT   "Annotation of human chromosome 21 for relevance to Down syndrome:
RT   gene structure and expression analysis.";
RL   Genomics 79:833-843(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANT PRO-1481,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Thymus;
RX   PubMed=15904895; DOI=10.1016/j.bbrc.2005.04.159;
RA   Shibuya K., Kudoh J., Okui M., Shimizu N.;
RT   "Identification of a novel zinc finger protein gene (ZNF298) in the
RT   GAP2 of human chromosome 21q.";
RL   Biochem. Biophys. Res. Commun. 332:557-568(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-1481.
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-951 (ISOFORM 1).
RA   Yang X.-H., Huang S.;
RT   "A family of novel PR-domain (PRDM) genes as candidate tumor
RT   suppressors.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1507 (ISOFORMS 1/2), AND VARIANT
RP   PRO-1481.
RX   PubMed=12036297; DOI=10.1006/geno.2002.6781;
RA   Reymond A., Camargo A.A., Deutsch S., Stevenson B.J., Parmigiani R.B.,
RA   Ucla C., Bettoni F., Rossier C., Lyle R., Guipponi M., de Souza S.,
RA   Iseli C., Jongeneel C.V., Bucher P., Simpson A.J.G., Antonarakis S.E.;
RT   "Nineteen additional unpredicted transcripts from human chromosome
RT   21.";
RL   Genomics 79:824-832(2002).
RN   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-883, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [8]
RP   FUNCTION.
RX   PubMed=28740264; DOI=10.1038/ng.3922;
RA   Mzoughi S., Zhang J., Hequet D., Teo S.X., Fang H., Xing Q.R.,
RA   Bezzi M., Seah M.K.Y., Ong S.L.M., Shin E.M., Wollmann H.,
RA   Wong E.S.M., Al-Haddawi M., Stewart C.L., Tergaonkar V., Loh Y.H.,
RA   Dunn N.R., Messerschmidt D.M., Guccione E.;
RT   "PRDM15 safeguards naive pluripotency by transcriptionally regulating
RT   WNT and MAPK-ERK signaling.";
RL   Nat. Genet. 49:1354-1363(2017).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-883, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Sequence-specific DNA-binding transcriptional regulator.
CC       Plays a role as a molecular node in a transcriptional network
CC       regulating embryonic development and cell fate decision.
CC       Stimulates the expression of upstream key transcriptional
CC       activators and repressors of the Wnt/beta-catenin and MAPK/ERK
CC       pathways, respectively, that are essential for naive pluripotency
CC       and self-renewal maintenance of embryonic stem cells (ESCs).
CC       Specifically promotes SPRY1 and RSPO1 transcription activation
CC       through recognition and direct binding of a specific DNA sequence
CC       in their promoter regions. Involved in early embryo development
CC       (By similarity). Plays also a role in induced pluripotent stem
CC       cells (iPSCs) reprogramming (PubMed:28740264).
CC       {ECO:0000250|UniProtKB:E9Q8T2, ECO:0000269|PubMed:28740264}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15904895}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P57071-1; Sequence=Displayed;
CC       Name=2; Synonyms=ZNF298b;
CC         IsoId=P57071-2; Sequence=VSP_055110, VSP_055111, VSP_055113;
CC       Name=3; Synonyms=ZNF298a;
CC         IsoId=P57071-3; Sequence=VSP_055110, VSP_055111;
CC       Name=4; Synonyms=ZNF298c;
CC         IsoId=P57071-5; Sequence=VSP_055110, VSP_055111, VSP_055114,
CC                                  VSP_055117;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC       Name=5; Synonyms=ZNF298d;
CC         IsoId=P57071-6; Sequence=VSP_055110, VSP_055111, VSP_055112,
CC                                  VSP_055115, VSP_055116;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC   -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC       {ECO:0000269|PubMed:15904895}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues.
CC       {ECO:0000269|PubMed:15904895}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL60596.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAM53515.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC       Sequence=AAM53516.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC       Sequence=BAA95527.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD99015.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAD99016.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAD99017.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAD99018.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
CC       Sequence=BAD99020.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
DR   EMBL; AY078498; AAL85487.2; -; mRNA.
DR   EMBL; AB051812; BAD99015.1; ALT_INIT; mRNA.
DR   EMBL; AB051813; BAD99016.1; ALT_INIT; mRNA.
DR   EMBL; AB051814; BAD99017.1; ALT_INIT; mRNA.
DR   EMBL; AB051814; BAD99018.1; ALT_SEQ; mRNA.
DR   EMBL; AB051815; BAD99020.1; ALT_SEQ; mRNA.
DR   EMBL; AB126081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001745; BAA95527.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP002955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471079; EAX09585.1; -; Genomic_DNA.
DR   EMBL; AF276513; AAF78093.1; -; mRNA.
DR   EMBL; AY063456; AAL60596.1; ALT_INIT; mRNA.
DR   EMBL; AF426259; AAM53515.1; ALT_SEQ; mRNA.
DR   EMBL; AF426260; AAM53516.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS13676.1; -. [P57071-1]
DR   CCDS; CCDS42932.1; -. [P57071-3]
DR   CCDS; CCDS63370.1; -. [P57071-2]
DR   RefSeq; NP_001035514.1; NM_001040424.2. [P57071-3]
DR   RefSeq; NP_001269863.1; NM_001282934.1. [P57071-2]
DR   RefSeq; NP_071398.3; NM_022115.4. [P57071-1]
DR   UniGene; Hs.473893; -.
DR   UniGene; Hs.726680; -.
DR   ProteinModelPortal; P57071; -.
DR   SMR; P57071; -.
DR   BioGrid; 122024; 19.
DR   IntAct; P57071; 3.
DR   MINT; P57071; -.
DR   STRING; 9606.ENSP00000269844; -.
DR   iPTMnet; P57071; -.
DR   PhosphoSitePlus; P57071; -.
DR   BioMuta; PRDM15; -.
DR   DMDM; 118572696; -.
DR   EPD; P57071; -.
DR   jPOST; P57071; -.
DR   MaxQB; P57071; -.
DR   PaxDb; P57071; -.
DR   PeptideAtlas; P57071; -.
DR   PRIDE; P57071; -.
DR   ProteomicsDB; 56980; -.
DR   DNASU; 63977; -.
DR   Ensembl; ENST00000269844; ENSP00000269844; ENSG00000141956. [P57071-1]
DR   Ensembl; ENST00000398548; ENSP00000381556; ENSG00000141956. [P57071-3]
DR   Ensembl; ENST00000422911; ENSP00000408592; ENSG00000141956. [P57071-2]
DR   Ensembl; ENST00000433067; ENSP00000415471; ENSG00000141956. [P57071-1]
DR   Ensembl; ENST00000449395; ENSP00000396943; ENSG00000141956. [P57071-5]
DR   GeneID; 63977; -.
DR   KEGG; hsa:63977; -.
DR   UCSC; uc002yzo.4; human. [P57071-1]
DR   CTD; 63977; -.
DR   DisGeNET; 63977; -.
DR   EuPathDB; HostDB:ENSG00000141956.13; -.
DR   GeneCards; PRDM15; -.
DR   HGNC; HGNC:13999; PRDM15.
DR   HPA; HPA024268; -.
DR   HPA; HPA029255; -.
DR   HPA; HPA029256; -.
DR   MIM; 617692; gene.
DR   neXtProt; NX_P57071; -.
DR   OpenTargets; ENSG00000141956; -.
DR   PharmGKB; PA33713; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000157890; -.
DR   HOGENOM; HOG000115685; -.
DR   HOVERGEN; HBG093153; -.
DR   InParanoid; P57071; -.
DR   OMA; HGCSICN; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P57071; -.
DR   TreeFam; TF331419; -.
DR   GenomeRNAi; 63977; -.
DR   PRO; PR:P57071; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; ENSG00000141956; Expressed in 168 organ(s), highest expression level in cerebellum.
DR   ExpressionAtlas; P57071; baseline and differential.
DR   Genevisible; P57071; HS.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA: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:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 17.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Polymorphism; Reference proteome; Repeat;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1507       PR domain zinc finger protein 15.
FT                                /FTId=PRO_0000047772.
FT   DOMAIN      415    525       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     563    585       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     738    760       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     765    788       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     826    848       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     853    875       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     902    924       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     929    951       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     992   1015       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1020   1042       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1056   1078       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1084   1106       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1112   1134       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1140   1162       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1168   1190       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1196   1219       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1225   1248       C2H2-type 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS     92     97       Poly-Pro.
FT   COMPBIAS    690    695       Poly-Thr.
FT   COMPBIAS   1499   1503       Poly-Gln.
FT   CROSSLNK    883    883       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ      35    297       Missing (in isoform 2, isoform 3, isoform
FT                                4 and isoform 5).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055110.
FT   VAR_SEQ     344    409       Missing (in isoform 2, isoform 3, isoform
FT                                4 and isoform 5).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055111.
FT   VAR_SEQ     701    720       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055112.
FT   VAR_SEQ     821    821       T -> TGLIAHPGEGGPGGSRLRDLP (in isoform
FT                                2). {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055113.
FT   VAR_SEQ     822    884       DDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMF
FT                                YRKDVMLDHQRRHLEGVRRVKR -> GLIAHPGEGGPGGSR
FT                                LRDLPATSPSTRRSTATRSLPVRSAARCSTARTSCWTTSAG
FT                                TWKECGE (in isoform 4).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055114.
FT   VAR_SEQ     822    864       DDKTFQCEMCFRFFSTNSNLSKHKKKHGDKKFACEVCSKMF
FT                                YR -> ATSPSTRRSTATRSLPVRSAARCSTARTSCWTTSA
FT                                GTWKECGE (in isoform 5).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055115.
FT   VAR_SEQ     865   1507       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055116.
FT   VAR_SEQ     885   1507       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15904895}.
FT                                /FTId=VSP_055117.
FT   VARIANT    1342   1342       V -> I (in dbSNP:rs3819158).
FT                                /FTId=VAR_014992.
FT   VARIANT    1376   1376       T -> S (in dbSNP:rs2236695).
FT                                /FTId=VAR_014993.
FT   VARIANT    1481   1481       S -> P (in dbSNP:rs3850706).
FT                                {ECO:0000269|PubMed:12036297,
FT                                ECO:0000269|PubMed:15904895,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_014994.
FT   CONFLICT   1147   1147       R -> G (in Ref. 6; AAL60596).
FT                                {ECO:0000305}.
FT   CONFLICT   1167   1167       D -> I (in Ref. 6; AAL60596).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1507 AA;  169269 MW;  E980A7EDB97239D0 CRC64;
     MPRRRPPASG AAQFPERIAT RSPDPIPLCT FQRQPRAAPV QPPCRLFFVT FAGCGHRWRS
     ESKPGWISRS RSGIALRAAR PPGSSPPRPA APRPPPPGGV VAEAPGDVVI PRPRVQPMRV
     ARGGPWTPNP AFREAESWSQ IGNQRVSEQL LETSLGNEVS DTEPLSPASA GLRRNPALPP
     GPFAQNFSWG NQENLPPALG KIANGGGTGA GKAECGYETE SHLLEPHEIP LNVNTHKFSD
     CEFPYEFCTV CFSPFKLLGM SGVEGVWNQH SRSASMHTFL NHSATGIREA GCRKDMPVSE
     MAEDGSEEIM FIWCEDCSQY HDSECPELGP VVMVKDSFVL SRARSWPASG HVHTQAGQGM
     RGYEDRDRAD PQQLPEAVPA GLVRRLSGQQ LPCRSTLTWG RLCHLVAQGR SSLPPNLEIR
     RLEDGAEGVF AITQLVKRTQ FGPFESRRVA KWEKESAFPL KVFQKDGHPV CFDTSNEDDC
     NWMMLVRPAA EAEHQNLTAY QHGSDVYFTT SRDIPPGTEL RVWYAAFYAK KMDKPMLKQA
     GSGVHAAGTP ENSAPVESEP SQWACKVCSA TFLELQLLNE HLLGHLEQAK SLPPGSQSEA
     AAPEKEQDTP RGEPPAVPES ENVATKEQKK KPRRGRKPKV SKAEQPLVIV EDKEPTEQVA
     EIITEVPPDE PVSATPDERI MELVLGKLAT TTTDTSSVPK FTHHQNNTIT LKRSLILSSR
     HGIRRKLIKQ LGEHKRVYQC NICSKIFQNS SNLSRHVRSH GDKLFKCEEC AKLFSRKESL
     KQHVSYKHSR NEVDGEYRYR CGTCEKTFRI ESALEFHNCR TDDKTFQCEM CFRFFSTNSN
     LSKHKKKHGD KKFACEVCSK MFYRKDVMLD HQRRHLEGVR RVKREDLEAG GENLVRYKKE
     PSGCPVCGKV FSCRSNMNKH LLTHGDKKYT CEICGRKFFR VDVLRDHIHV HFKDIALMDD
     HQREEFIGKI GISSEENDDN SDESADSEPH KYSCKRCQLT FGRGKEYLKH IMEVHKEKGY
     GCSICNRRFA LKATYHAHMV IHRENLPDPN VQKYIHPCEI CGRIFNSIGN LERHKLIHTG
     VKSHACEQCG KSFARKDMLK EHMRVHDNVR EYLCAECGKG MKTKHALRHH MKLHKGIKEY
     ECKECHRRFA QKVNMLKHCK RHTGIKDFMC ELCGKTFSER NTMETHKLIH TVGKQWTCSV
     CDKKYVTEYM LQKHVQLTHD KVEAQSCQLC GTKVSTRASM SRHMRRKHPE VLAVRIDDLD
     HLPETTTIDA SSIGIVQPEL TLEQEDLAEG KHGKAAKRSH KRKQKPEEEA GAPVPEDATF
     SEYSEKETEF TGSVGDETNS AVQSIQQVVV TLGDPNVTTP SSSVGLTNIT VTPITTAAAT
     QFTNLQPVAV GHLTTPERQL QLDNSILTVT FDTVSGSAML HNRQNDVQIH PQPEASNPQS
     VAHFINLTTL VNSITPLGSQ LSDQHPLTWR AVPQTDVLPP SQPQAPPQQA AQPQVQAEQQ
     QQQMYSY
//
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