GenomeNet

Database: UniProt
Entry: Q8CGT6
LinkDB: Q8CGT6
Original site: Q8CGT6 
ID   PIWL4_MOUSE             Reviewed;         848 AA.
AC   Q8CGT6; A6P4B9; A6X963; A6X964; Q8CC75;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   13-NOV-2019, entry version 120.
DE   RecName: Full=Piwi-like protein 4;
DE            Short=mAgo5;
GN   Name=Piwil4; Synonyms=Miwi2 {ECO:0000303|PubMed:18381894};
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   1).
RX   PubMed=12414724; DOI=10.1101/gad.1026102;
RA   Carmell M.A., Xuan Z., Zhang M.Q., Hannon G.J.;
RT   "The Argonaute family: tentacles that reach into RNAi, developmental
RT   control, stem cell maintenance, and tumorigenesis.";
RL   Genes Dev. 16:2733-2742(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18381894; DOI=10.1101/gad.1640708;
RA   Kuramochi-Miyagawa S., Watanabe T., Gotoh K., Totoki Y., Toyoda A.,
RA   Ikawa M., Asada N., Kojima K., Yamaguchi Y., Ijiri T.W., Hata K.,
RA   Li E., Matsuda Y., Kimura T., Okabe M., Sakaki Y., Sasaki H.,
RA   Nakano T.;
RT   "DNA methylation of retrotransposon genes is regulated by Piwi family
RT   members MILI and MIWI2 in murine fetal testes.";
RL   Genes Dev. 22:908-917(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 667-848 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Epididymis;
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   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17395546; DOI=10.1016/j.devcel.2007.03.001;
RA   Carmell M.A., Girard A., van de Kant H.J.G., Bourc'his D.,
RA   Bestor T.H., de Rooij D.G., Hannon G.J.;
RT   "MIWI2 is essential for spermatogenesis and repression of transposons
RT   in the mouse male germline.";
RL   Dev. Cell 12:503-514(2007).
RN   [6]
RP   FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18922463; DOI=10.1016/j.molcel.2008.09.003;
RA   Aravin A.A., Sachidanandam R., Bourc'his D., Schaefer C., Pezic D.,
RA   Toth K.F., Bestor T., Hannon G.J.;
RT   "A piRNA pathway primed by individual transposons is linked to de novo
RT   DNA methylation in mice.";
RL   Mol. Cell 31:785-799(2008).
RN   [7]
RP   METHYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH TDRD1; TDRKH
RP   AND TDRD9.
RX   PubMed=19584108; DOI=10.1101/gad.1814809;
RA   Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA   Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT   "Proteomic analysis of murine Piwi proteins reveals a role for
RT   arginine methylation in specifying interaction with Tudor family
RT   members.";
RL   Genes Dev. 23:1749-1762(2009).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19465913; DOI=10.1038/nsmb.1615;
RA   Reuter M., Chuma S., Tanaka T., Franz T., Stark A., Pillai R.S.;
RT   "Loss of the Mili-interacting Tudor domain-containing protein-1
RT   activates transposons and alters the Mili-associated small RNA
RT   profile.";
RL   Nat. Struct. Mol. Biol. 16:639-646(2009).
RN   [9]
RP   INTERACTION WITH MOV10L1.
RX   PubMed=20534472; DOI=10.1073/pnas.1003953107;
RA   Zheng K., Xiol J., Reuter M., Eckardt S., Leu N.A., McLaughlin K.J.,
RA   Stark A., Sachidanandam R., Pillai R.S., Wang P.J.;
RT   "Mouse MOV10L1 associates with Piwi proteins and is an essential
RT   component of the Piwi-interacting RNA (piRNA) pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11841-11846(2010).
RN   [10]
RP   INTERACTION WITH MOV10L1.
RX   PubMed=20547853; DOI=10.1073/pnas.1007158107;
RA   Frost R.J., Hamra F.K., Richardson J.A., Qi X., Bassel-Duby R.,
RA   Olson E.N.;
RT   "MOV10L1 is necessary for protection of spermatocytes against
RT   retrotransposons by Piwi-interacting RNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11847-11852(2010).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF ASP-688.
RX   PubMed=22020280; DOI=10.1038/nature10547;
RA   De Fazio S., Bartonicek N., Di Giacomo M., Abreu-Goodger C.,
RA   Sankar A., Funaya C., Antony C., Moreira P.N., Enright A.J.,
RA   O'Carroll D.;
RT   "The endonuclease activity of Mili fuels piRNA amplification that
RT   silences LINE1 elements.";
RL   Nature 480:259-263(2011).
RN   [12]
RP   INTERACTION WITH TDRKH.
RX   PubMed=23714778; DOI=10.1038/emboj.2013.121;
RA   Saxe J.P., Chen M., Zhao H., Lin H.;
RT   "Tdrkh is essential for spermatogenesis and participates in primary
RT   piRNA biogenesis in the germline.";
RL   EMBO J. 32:1869-1885(2013).
RN   [13]
RP   TISSUE SPECIFICITY.
RX   PubMed=25038252; DOI=10.1093/nar/gku620;
RA   Keam S.P., Young P.E., McCorkindale A.L., Dang T.H., Clancy J.L.,
RA   Humphreys D.T., Preiss T., Hutvagner G., Martin D.I., Cropley J.E.,
RA   Suter C.M.;
RT   "The human Piwi protein Hiwi2 associates with tRNA-derived piRNAs in
RT   somatic cells.";
RL   Nucleic Acids Res. 42:8984-8995(2014).
RN   [14]
RP   FUNCTION.
RX   PubMed=26669262; DOI=10.1016/j.molcel.2015.11.009;
RA   Yang Z., Chen K.M., Pandey R.R., Homolka D., Reuter M., Janeiro B.K.,
RA   Sachidanandam R., Fauvarque M.O., McCarthy A.A., Pillai R.S.;
RT   "PIWI slicing and EXD1 drive biogenesis of nuclear piRNAs from
RT   cytosolic targets of the mouse piRNA pathway.";
RL   Mol. Cell 61:138-152(2016).
CC   -!- FUNCTION: Plays a central role during spermatogenesis by
CC       repressing transposable elements and preventing their
CC       mobilization, which is essential for the germline integrity
CC       (PubMed:17395546, PubMed:18381894, PubMed:18922463,
CC       PubMed:26669262, PubMed:22020280). Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements
CC       during meiosis by forming complexes composed of piRNAs and Piwi
CC       proteins and governs the methylation and subsequent repression of
CC       transposons (PubMed:17395546, PubMed:18381894, PubMed:18922463,
CC       PubMed:26669262, PubMed:22020280). Directly binds piRNAs, a class
CC       of 24 to 30 nucleotide RNAs that are generated by a Dicer-
CC       independent mechanism and are primarily derived from transposons
CC       and other repeated sequence elements. Associates with secondary
CC       piRNAs antisense and PIWIL2/MILI is required for such association
CC       (PubMed:17395546, PubMed:18381894, PubMed:18922463,
CC       PubMed:26669262, PubMed:22020280). The piRNA process acts upstream
CC       of known mediators of DNA methylation (PubMed:17395546,
CC       PubMed:18381894, PubMed:18922463, PubMed:26669262,
CC       PubMed:22020280). Does not show endonuclease activity
CC       (PubMed:22020280). Plays a key role in the piRNA amplification
CC       loop, also named ping-pong amplification cycle, by acting as a
CC       'slicer-incompetent' component that loads cleaved piRNAs from the
CC       'slicer-competent' component PIWIL2 and target them on genomic
CC       transposon loci in the nucleus (PubMed:22020280). In addition to
CC       its role in germline, PIWIL4 also plays a role in the regulation
CC       of somatic cells activities. Plays a role in pancreatic beta cell
CC       function and insulin secretion (By similarity). Involved in
CC       maintaining cell morphology and functional integrity of retinal
CC       epithelial through Akt/GSK3alpha/beta signaling pathway (By
CC       similarity). {ECO:0000250|UniProtKB:Q4G033,
CC       ECO:0000250|UniProtKB:Q7Z3Z4, ECO:0000269|PubMed:17395546,
CC       ECO:0000269|PubMed:18381894, ECO:0000269|PubMed:18922463,
CC       ECO:0000269|PubMed:22020280, ECO:0000269|PubMed:26669262}.
CC   -!- SUBUNIT: Interacts with PRMT5 and WDR77 (PubMed:19584108).
CC       Interacts (when methylated on arginine residues) with TDRD1,
CC       TDRKH/TDRD2 and TDRD9 (PubMed:19584108, PubMed:23714778).
CC       Interacts with MOV10L1 (PubMed:20534472, PubMed:20547853).
CC       {ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:20534472,
CC       ECO:0000269|PubMed:20547853, ECO:0000269|PubMed:23714778}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922463}.
CC       Cytoplasm {ECO:0000269|PubMed:18922463,
CC       ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}.
CC       Note=Probable component of the meiotic nuage, also named P
CC       granule, a germ-cell-specific organelle required to repress
CC       transposon activity during meiosis. PIWIL2/MILI is required for
CC       nuclear localization. {ECO:0000269|PubMed:18922463,
CC       ECO:0000269|PubMed:19465913, ECO:0000269|PubMed:19584108}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CGT6-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=2;
CC         IsoId=Q8CGT6-2; Sequence=VSP_018376;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q8CGT6-3; Sequence=VSP_036666;
CC   -!- TISSUE SPECIFICITY: Detected in male germ cells beginning around
CC       14.5-15.5 dpc but is absent from female germ cells
CC       (PubMed:18922463, PubMed:25038252). From 15.5 dpc and until birth,
CC       it is present in male germ cells. Not detected in somatic cells of
CC       the embryonic gonad. Expression declines soon after birth,
CC       reaching undetectable levels in 4 day-old mice (at protein level).
CC       {ECO:0000269|PubMed:18922463, ECO:0000269|PubMed:25038252}.
CC   -!- PTM: Arginine methylation by PRMT5 is required for the interaction
CC       with Tudor domain-containing protein (TDRD1, TDRKH/TDRD2 and
CC       TDRD9) and subsequent localization to the meiotic nuage, also
CC       named P granule. {ECO:0000269|PubMed:19584108}.
CC   -!- DISRUPTION PHENOTYPE: Males show spermatogenesis defects due to
CC       demethylation and subsequent derepression of transposable
CC       elements. Meiotic-progression is impaired during early prophase of
CC       meiosis I, followed by a marked and progressive loss of germ cells
CC       with age. {ECO:0000269|PubMed:17395546,
CC       ECO:0000269|PubMed:18381894}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Piwi subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN75583.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAC28462.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAO77951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY135692; AAN75583.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB258534; BAF65667.1; -; mRNA.
DR   EMBL; CT030247; CAO77949.1; -; Genomic_DNA.
DR   EMBL; CT030247; CAO77951.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK033746; BAC28462.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS22824.1; -. [Q8CGT6-1]
DR   RefSeq; NP_808573.2; NM_177905.3.
DR   SMR; Q8CGT6; -.
DR   iPTMnet; Q8CGT6; -.
DR   PhosphoSitePlus; Q8CGT6; -.
DR   jPOST; Q8CGT6; -.
DR   PeptideAtlas; Q8CGT6; -.
DR   PRIDE; Q8CGT6; -.
DR   DNASU; 330890; -.
DR   Ensembl; ENSMUST00000115644; ENSMUSP00000111308; ENSMUSG00000036912. [Q8CGT6-1]
DR   UCSC; uc009oet.1; mouse. [Q8CGT6-1]
DR   UCSC; uc009oev.1; mouse. [Q8CGT6-3]
DR   CTD; 143689; -.
DR   MGI; MGI:3041167; Piwil4.
DR   GeneTree; ENSGT00950000183200; -.
DR   HOGENOM; HOG000254789; -.
DR   InParanoid; Q8CGT6; -.
DR   OMA; WSKDMRN; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; Q8CGT6; -.
DR   TreeFam; TF354206; -.
DR   PRO; PR:Q8CGT6; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000036912; Expressed in 43 organ(s), highest expression level in gonadal ridge.
DR   ExpressionAtlas; Q8CGT6; baseline and differential.
DR   Genevisible; Q8CGT6; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR   GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR   GO; GO:0034584; F:piRNA binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR   GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR   GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR003165; Piwi.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF02171; Piwi; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS50822; PIWI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Developmental protein; Differentiation; Meiosis; Methylation; Nucleus;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW   Spermatogenesis; Translation regulation.
FT   CHAIN         1    848       Piwi-like protein 4.
FT                                /FTId=PRO_0000234573.
FT   DOMAIN      263    379       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      541    834       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   VAR_SEQ     761    761       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:18381894}.
FT                                /FTId=VSP_036666.
FT   VAR_SEQ     811    848       GLISVPAPCQYAHKLTFLVAQSVHKEPSLELANNLFYL ->
FT                                SCHGIQAALKPVTVPLPQLLSTGTMQ (in isoform
FT                                2). {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_018376.
FT   MUTAGEN     688    688       D->A: In DAH mutant; does not lead to
FT                                arrest in meiotic prophase and failure of
FT                                transposon piRNA amplification.
FT                                {ECO:0000269|PubMed:22020280}.
FT   CONFLICT    644    644       W -> R (in Ref. 2; BAF65667).
FT                                {ECO:0000305}.
FT   CONFLICT    808    808       N -> D (in Ref. 2; BAF65667).
FT                                {ECO:0000305}.
SQ   SEQUENCE   848 AA;  95773 MW;  907DB987D47947FD CRC64;
     MSGRARVRAR GITTGHSARE VGRSSRDLMV TSASPGDSEA GGGTSVISQP YELGVSSGDG
     GRTFMERRGK GRQDFEELGV CTREKLTHVK DCKTGSSGIP VRLVTNLFNL DLPQDWQLYQ
     YHVTYSPDLA SRRLRIALLY NHSILSDKAK AFDGASLFLS EKLDQKVTEL TSETQRGETI
     KITLTLTSKL FPNSPVCIQF FNVIFRKILK NLSMYQIGRN FYKPSEPVEI PQYKLSLWPG
     FAISVSHFES KLLFNADVNY KVLRNETVLD FMTDLCLRTG MSCFTEMCHK QLVGLVVLTR
     YNNKTYRIDD IDWSVKPTQA FQKRDGSEVT YVDYYKQQYD ITLSDLNQPV LVSLLKRKRN
     DNSEPQMVHL MPELCFLTGL SSQATSDFRL MKAVAEETRL SPVGRQQQLA RLVDDIQRNP
     VARFELETWG LHFGSQLSLT GRVVPSEKIL LQDHTCQPAF AADWSKDMRS CKVLSSQPLN
     RWLIVCCNRA EHLIEAFLSC LRRVGGSMGF NVGYPKIIKV DETPAAFLRA IQVHGDPDVQ
     LVMCILPSNQ KNYYDSIKKY LSSDCPVPSQ CVLTRTLNKQ GTMLSVATKI AMQMTCKLGG
     ELWSVEIPLK SLMVVGIDIC RDALNKNVVV VGFVASINSR ITRWFSRCVL QRTAADIADC
     LKVCMTGALN RWYRHNHDLP ARIVVYRDGV GNGQLKAVLE YEVPQLLKSV TECGSDARSC
     RLSVVVVRKR CLLRLFASTD HTVQNPPLGT VVDSEATRPE WYDFYLISQT ANRGTVSPTH
     YNVIYDDNAL KPDHMQRLTF KLCHLYYNWQ GLISVPAPCQ YAHKLTFLVA QSVHKEPSLE
     LANNLFYL
//
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