GenomeNet

Database: UniProt
Entry: O88491
LinkDB: O88491
Original site: O88491 
ID   NSD1_MOUSE              Reviewed;        2588 AA.
AC   O88491; Q8C480; Q9CT70;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=H3-K36-HMTase;
DE   AltName: Full=H4-K20-HMTase;
DE   AltName: Full=Nuclear receptor-binding SET domain-containing protein 1;
DE            Short=NR-binding SET domain-containing protein;
GN   Name=Nsd1 {ECO:0000312|MGI:MGI:1276545};
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] {ECO:0000305, ECO:0000312|EMBL:AAC40182.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RARA; THRA;
RP   RXRA AND ESRRA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-803;
RP   804-SER-THR-805 AND 806-LEU-LEU-807.
RC   TISSUE=Embryo {ECO:0000269|PubMed:9628876};
RX   PubMed=9628876; DOI=10.1093/emboj/17.12.3398;
RA   Huang N., vom Baur E., Garnier J.-M., Lerouge T., Vonesch J.-L.,
RA   Lutz Y., Chambon P., Losson R.;
RT   "Two distinct nuclear receptor interaction domains in NSD1, a novel
RT   SET protein that exhibits characteristics of both corepressors and
RT   coactivators.";
RL   EMBO J. 17:3398-3412(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2220-2588.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [3] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   CYS-1920 AND THR-1950.
RX   PubMed=12805229; DOI=10.1093/emboj/cdg288;
RA   Rayasam G.V., Wendling O., Angrand P.-O., Mark M., Niederreither K.,
RA   Song L., Lerouge T., Hager G.L., Chambon P., Losson R.;
RT   "NSD1 is essential for early post-implantation development and has a
RT   catalytically active SET domain.";
RL   EMBO J. 22:3153-3163(2003).
RN   [4]
RP   INTERACTION WITH ZNF496.
RX   PubMed=15169884; DOI=10.1128/MCB.24.12.5184-5196.2004;
RA   Nielsen A.L., Jorgensen P., Lerouge T., Cervino M., Chambon P.,
RA   Losson R.;
RT   "Nizp1, a novel multitype zinc finger protein that interacts with the
RT   NSD1 histone lysine methyltransferase through a unique C2HR motif.";
RL   Mol. Cell. Biol. 24:5184-5196(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-118; SER-1408
RP   AND SER-2369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Histone methyltransferase. Preferentially methylates
CC       'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro).
CC       Transcriptional intermediary factor capable of negatively
CC       influencing transcription. May also positively influence
CC       transcription. Essential for early post-implantation development.
CC       {ECO:0000269|PubMed:12805229, ECO:0000269|PubMed:9628876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:12805229};
CC   -!- SUBUNIT: Interacts with AR DNA- and ligand-binding domains (By
CC       similarity). Interacts with the ligand-binding domains of RARA and
CC       THRA in the absence of ligand; in the presence of ligand the
CC       interaction is severely disrupted but some binding still occurs.
CC       Interacts with the ligand-binding domains of RXRA and ESRRA only
CC       in the presence of ligand. Interacts with ZNF496. {ECO:0000250,
CC       ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:9628876}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9628876}.
CC       Chromosome {ECO:0000305|PubMed:9628876}.
CC   -!- TISSUE SPECIFICITY: Expressed in the embryo and the outer region
CC       of the uterine decidua at early post-implantation E5.5 stage.
CC       Uniformly expressed in embryonic and extraembryonic tissues during
CC       gastrulation stage E7.5. Expressed differentially after stage 14.5
CC       with highest expression in proliferating cells. Enriched in the
CC       telencephalic region of the brain, spinal cord, intestinal crypt,
CC       tooth buds, thymus and salivary glands at stage E16.5. Also
CC       expressed in the ossification region of developing bones and in
CC       the periosteum. {ECO:0000269|PubMed:12805229}.
CC   -!- DOMAIN: Contains 2 adjacent but distinct nuclear receptor
CC       interaction domains (NID+L and NID-L) to which nuclear receptors
CC       bind differentially in the presence and absence of ligand
CC       respectively.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AF064553; AAC40182.1; -; mRNA.
DR   EMBL; AK082820; BAC38635.1; -; mRNA.
DR   EMBL; AK004485; BAB23326.1; -; mRNA.
DR   PIR; T14342; T14342.
DR   UniGene; Mm.168965; -.
DR   PDB; 2NAA; NMR; -; A=2014-2104.
DR   PDBsum; 2NAA; -.
DR   ProteinModelPortal; O88491; -.
DR   SMR; O88491; -.
DR   IntAct; O88491; 2.
DR   MINT; O88491; -.
DR   STRING; 10090.ENSMUSP00000097089; -.
DR   iPTMnet; O88491; -.
DR   PhosphoSitePlus; O88491; -.
DR   EPD; O88491; -.
DR   jPOST; O88491; -.
DR   MaxQB; O88491; -.
DR   PaxDb; O88491; -.
DR   PeptideAtlas; O88491; -.
DR   PRIDE; O88491; -.
DR   MGI; MGI:1276545; Nsd1.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000113857; -.
DR   HOVERGEN; HBG007518; -.
DR   InParanoid; O88491; -.
DR   PhylomeDB; O88491; -.
DR   ChiTaRS; Nsd1; mouse.
DR   PRO; PR:O88491; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0035097; C:histone methyltransferase complex; IC:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
DR   GO; GO:0042054; F:histone methyltransferase activity; IDA:MGI.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
DR   GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
DR   GO; GO:0046965; F:retinoid X receptor binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0000414; P:regulation of histone H3-K36 methylation; ISO:MGI.
DR   GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 4.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00249; PHD; 5.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 3.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromatin regulator; Chromosome;
KW   Complete proteome; Developmental protein; Isopeptide bond;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   2588       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 and H4 lysine-20 specific.
FT                                /FTId=PRO_0000186071.
FT   DOMAIN     1654   1716       PWWP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN     1788   1838       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1840   1957       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1964   1980       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING    1441   1487       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1488   1544       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1605   1649       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    2016   2063       PHD-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   REGION     1850   1852       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1892   1895       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1918   1919       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1958   1964       Inhibits enzyme activity in the absence
FT                                of bound histone. {ECO:0000250}.
FT   COMPBIAS    841    896       Ser-rich. {ECO:0000255}.
FT   COMPBIAS   2213   2251       Pro-rich. {ECO:0000255}.
FT   BINDING    1963   1963       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1969   1969       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     110    110       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     380    380       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   MOD_RES     383    383       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   MOD_RES    1408   1408       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2267   2267       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   MOD_RES    2360   2360       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   MOD_RES    2369   2369       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    802    802       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   CROSSLNK   1237   1237       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   CROSSLNK   2509   2509       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96L73}.
FT   MUTAGEN     803    803       F->A,Y: No effect on interaction with
FT                                nuclear receptors.
FT                                {ECO:0000269|PubMed:9628876}.
FT   MUTAGEN     804    805       ST->AA: Abolishes interaction with
FT                                nuclear receptors.
FT                                {ECO:0000269|PubMed:9628876}.
FT   MUTAGEN     806    807       LL->AA: Strongly decreases interaction
FT                                with liganded nuclear receptors. No
FT                                effect on interaction with non-liganded
FT                                nuclear receptors.
FT                                {ECO:0000269|PubMed:9628876}.
FT   MUTAGEN    1920   1920       C->S: Increases methyltransferase
FT                                activity towards H3 and H4. Increases
FT                                methyltransferase activity; when
FT                                associated with E-1950.
FT                                {ECO:0000269|PubMed:12805229}.
FT   MUTAGEN    1950   1950       T->E: Does not affect histone
FT                                methyltransferase activity. Increases
FT                                methyltransferase activity; when
FT                                associated with S-1920.
FT                                {ECO:0000269|PubMed:12805229}.
FT   STRAND     2017   2019       {ECO:0000244|PDB:2NAA}.
FT   TURN       2020   2022       {ECO:0000244|PDB:2NAA}.
FT   STRAND     2026   2030       {ECO:0000244|PDB:2NAA}.
FT   STRAND     2039   2041       {ECO:0000244|PDB:2NAA}.
FT   TURN       2042   2046       {ECO:0000244|PDB:2NAA}.
FT   HELIX      2058   2060       {ECO:0000244|PDB:2NAA}.
FT   TURN       2063   2065       {ECO:0000244|PDB:2NAA}.
FT   STRAND     2066   2068       {ECO:0000244|PDB:2NAA}.
FT   TURN       2082   2084       {ECO:0000244|PDB:2NAA}.
FT   TURN       2086   2088       {ECO:0000244|PDB:2NAA}.
FT   STRAND     2089   2091       {ECO:0000244|PDB:2NAA}.
FT   TURN       2093   2095       {ECO:0000244|PDB:2NAA}.
FT   STRAND     2098   2100       {ECO:0000244|PDB:2NAA}.
SQ   SEQUENCE   2588 AA;  284084 MW;  145DFCF2F285A959 CRC64;
     MDRTCELSRR NCLLSFSNPV NLDASEDKDS PFGNGQSNFS EPLNGCTMQL PTAASGTSQN
     AYGQDSPSCY IPLRRLQDLA SMINVEYLSG SADGSESFQD PAKSDSRAQS PIVCTSLSPG
     GPTALAMKQE PTCNNSPELQ LRVTKTTKNG FLHFENFTGV DDADVDSEMD PEQPVTEDES
     IEEIFEETQT NATCNYEPKS ENGVEVAMGS EQDSMPESRH GAVERPFLPL APQTEKQKNK
     QRSEVDGSNE KTALLPAPTS LGDTNVTVEE QFNSINLSFQ DDPDSSPSPL GNMLEIPGTS
     SPSTSQELPF VPQKILSKWE ASVGLAEQYD VPKGSKNQKC VSSSVKLDSE EDMPFEDCTN
     DPDSEHLLLN GCLKSLAFDS EHSADEKEKP CAKSRVRKSS DNIKRTSVKK DLVPFESRKE
     ERRGKIPDNL GLDFISGGVS DKQASNELSR IANSLTGSST APGSFLFSSS VQNTAKTDFE
     TPDCDSLSGL SESALISKHS GEKKKLHPGQ VCSSKVQLCY VGAGDEEKRS NSVSVSTTSD
     DGCSDLDPTE HNSGFQNSVL GITDAFDKTE NALSVHKNET QYSRYPVTNR IKEKQKSLIT
     NSHADHLMGS TKTMEPETAE LSQVNLSDLK ISSPIPKPQP EFRNDGLTTK FSAPPGIRNE
     NPLTKGGLAN QTLLPLKCRQ PKFRSIKCKH KESPAVAETS ATSEDLSLKC CSSDTNGSPL
     ANISKSGKGE GLKLLNNMHE KTRDSSDIET AVVKHVLSEL KELSYRSLSE DVSDSGTAKA
     SKPLLFSSAS SQNHIPIEPD YKFSTLLMML KDMHDSKTKE QRLMTAQNLA SYRTPDRGDC
     SSGSPVGTSK VLVLGSSTPN SEKPGDSTQD SVHQSPGGGD SALSGELSSS LSSLASDKRE
     LPACGKIRSN CIPRRNCGRA KPSSKLRETI SAQMVKPSVN PKALKTERKR KFSRLPAVTL
     AANRLGNKES GSVNGPSRGG AEDPGKEEPL QQMDLLRNED THFSDVHFDS KAKQSDPDKN
     LEKEPSFENR KGPELGSEMN TENDELHGVN QVVPKKRWQR LNQRRPKPGK RANRFREKEN
     SEGAFGVLLP ADAVQKARED YLEQRAPPTS KPEDSAADPN HGSHSESVAP RLNVCEKSSV
     GMGDVEKETG IPSLMPQTKL PEPAIRSEKK RLRKPSKWLL EYTEEYDQIF APKKKQKKVQ
     EQVHKVSSRC EDESLLARCQ PSAQNKQVDE NSLISTKEEP PVLEREAPFL EGPLAQSDLG
     VTHAELPQLT LSVPVAPEAS PRPALESEEL LVKTPGNYES KRQRKPTKKL LESNDLDPGF
     MPKKGDLGLS RKCFEASRSG NGIVESRATS HLKEFSGGTT KIFDKPRKRK RQRLVTARVH
     YKKVKKEDLT KDTPSSEGEL LIHRTAASPK EILEEGVEHD PGMSASKKLQ VERGGGAALK
     ENVCQNCEKL GELLLCEAQC CGAFHLECLG LPEMPRGKFI CNECHTGIHT CFVCKQSGED
     VKRCLLPLCG KFYHEECVQK YPPTVTQNKG FRCPLHICIT CHAANPANVS ASKGRLMRCV
     RCPVAYHAND FCLAAGSKIL ASNSIICPNH FTPRRGCRNH EHVNVSWCFV CSEGGSLLCC
     DSCPAAFHRE CLNIDIPEGN WYCNDCKAGK KPHYREIVWV KVGRYRWWPA EICHPRAVPS
     NIDKMRHDVG EFPVLFFGSN DYLWTHQARV FPYMEGDVSS KDKMGKGVDG TYKKALQEAA
     ARFEELKARK ELRQLQEDRK NDKKPPPYKH IKVNRPIGRV QIFTADLSEI PRCNCKATDE
     NPCGIDSECI NRMLLYECHP TVCPAGVRCQ NQCFSKRQYP DVEIFRTLQR GWGLRTKTDI
     KKGEFVNEYV GELIDEEECR ARIRYAQEHD ITNFYMLTLD KDRIIDAGPK GNYARFMNHC
     CQPNCETQKW SVNGDTRVGL FALSDIKAGT ELTFNYNLEC LGNGKTVCKC GAPNCSGFLG
     VRPKNQPIVT EEKSRKFKRK PHGKRRSQGE VTKEREDECF SCGDAGQLVS CKKPGCPKVY
     HADCLNLTKR PAGKWECPWH QCDVCGKEAA SFCEMCPSSF CKQHREGMLF ISKLDGRLSC
     TEHDPCGPNP LEPGEIREYV PPTATSPPSP GTQPKEQSSE MATQGPKKSD QPPTDATQLL
     PLSKKALTGS CQRPLLPERP PERTDSSSHL LDRIRDLAGS GTKSQSLVSS QRPQDRPPAK
     EGPRPQPPDR ASPMTRPSSS PSVSSLPLER PLRMTDSRLD KSIGAASPKS QAVEKTPAST
     GLRLSSPDRL LTTNSPKPQI SDRPPEKSHA SLTQRLPPPE KVLSAVVQSL VAKEKALRPV
     DQNTQSKHRP AVVMDLIDLT PRQKERAASP QEVTPQADEK TAMLESSSWP SSKGLGHIPR
     ATEKISVSES LQPSGKVAAP SEHPWQAVKS LTHARFLSPP SAKAFLYESA TQASGRTPVG
     AEQTPGPPSP APGLVKQVKQ LSRGLTAKSG QSFRSLGKIS ASLPNEEKKL TTTEQSPWGL
     GKASPGAGLW PIVAGQTLAQ ACWSAGGTQT LAQTCWSLGR GQDPKPENAI QALNQAPSSR
     KCADSEKK
//
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