NSD1_MOUSE
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 03-AUG-2022, entry version 154.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE EC=2.1.1.357 {ECO:0000269|PubMed:12805229};
DE AltName: Full=H3-K36-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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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; RXRA AND
RP ESRRA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-803; 804-SER-THR-805
RP 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., Lutz Y.,
RA Chambon P., Losson R.;
RT "Two distinct nuclear receptor interaction domains in NSD1, a novel SET
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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., Losson R.;
RT "Nizp1, a novel multitype zinc finger protein that interacts with the NSD1
RT 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 AND
RP SER-2369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Histone methyltransferase that dimethylates Lys-36 of histone
CC H3 (H3K36me2). Transcriptional intermediary factor capable of
CC negatively 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(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357;
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 THRA
CC in the absence of ligand; in the presence of ligand the interaction is
CC severely disrupted but some binding still occurs. Interacts with the
CC ligand-binding domains of RXRA and ESRRA only in the presence of
CC ligand. Interacts with ZNF496. {ECO:0000250,
CC ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:9628876}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9628876}. Chromosome
CC {ECO:0000305|PubMed:9628876}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryo and the outer region of the
CC uterine decidua at early post-implantation 5.5 dpc stage. Uniformly
CC expressed in embryonic and extraembryonic tissues during gastrulation
CC stage 7.5 dpc. Expressed differentially after stage 14.5 dpc with
CC highest expression in proliferating cells. Enriched in the
CC telencephalic region of the brain, spinal cord, intestinal crypt, tooth
CC buds, thymus and salivary glands at stage 16.5 dpc. Also expressed in
CC the ossification region of developing bones and in the periosteum.
CC {ECO:0000269|PubMed:12805229}.
CC -!- DOMAIN: Contains 2 adjacent but distinct nuclear receptor interaction
CC domains (NID+L and NID-L) to which nuclear receptors bind
CC differentially in the presence and absence of ligand respectively.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AF064553; AAC40182.1; -; mRNA.
DR EMBL; AK082820; BAC38635.1; -; mRNA.
DR EMBL; AK004485; BAB23326.1; -; mRNA.
DR PIR; T14342; T14342.
DR PDB; 2NAA; NMR; -; A=2014-2104.
DR PDBsum; 2NAA; -.
DR AlphaFoldDB; O88491; -.
DR SMR; O88491; -.
DR IntAct; O88491; 1.
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 ProteomicsDB; 253018; -.
DR MGI; MGI:1276545; Nsd1.
DR eggNOG; KOG1081; Eukaryota.
DR InParanoid; O88491; -.
DR PhylomeDB; O88491; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR ChiTaRS; Nsd1; mouse.
DR PRO; PR:O88491; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88491; protein.
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:0003682; F:chromatin binding; IDA:MGI.
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:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PF17982; C5HCH; 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 SUPFAM; SSF82199; SSF82199; 1.
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 Developmental protein; Isopeptide bond; Metal-binding; Methyltransferase;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2588
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000186071"
FT DOMAIN 1654..1716
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 1788..1838
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1840..1957
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1964..1980
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 1441..1487
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1488..1544
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1605..1649
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 2016..2063
FT /note="PHD-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 209..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..1964
FT /note="Inhibits enzyme activity in the absence of bound
FT histone"
FT /evidence="ECO:0000250"
FT REGION 1989..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2333..2423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2447..2521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2560..2588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2130..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2199..2213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2367..2393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1850..1852
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1892..1895
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1918..1919
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1963
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1969
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT MOD_RES 1408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT MOD_RES 2360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT MOD_RES 2369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 802
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT CROSSLNK 1237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT CROSSLNK 2509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96L73"
FT MUTAGEN 803
FT /note="F->A,Y: No effect on interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:9628876"
FT MUTAGEN 804..805
FT /note="ST->AA: Abolishes interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:9628876"
FT MUTAGEN 806..807
FT /note="LL->AA: Strongly decreases interaction with liganded
FT nuclear receptors. No effect on interaction with non-
FT liganded nuclear receptors."
FT /evidence="ECO:0000269|PubMed:9628876"
FT MUTAGEN 1920
FT /note="C->S: Increases methyltransferase activity towards
FT H3 and H4. Increases methyltransferase activity; when
FT associated with E-1950."
FT /evidence="ECO:0000269|PubMed:12805229"
FT MUTAGEN 1950
FT /note="T->E: Does not affect histone methyltransferase
FT activity. Increases methyltransferase activity; when
FT associated with S-1920."
FT /evidence="ECO:0000269|PubMed:12805229"
FT STRAND 2017..2019
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2020..2022
FT /evidence="ECO:0007829|PDB:2NAA"
FT STRAND 2026..2030
FT /evidence="ECO:0007829|PDB:2NAA"
FT STRAND 2039..2041
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2042..2046
FT /evidence="ECO:0007829|PDB:2NAA"
FT HELIX 2058..2060
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2063..2065
FT /evidence="ECO:0007829|PDB:2NAA"
FT STRAND 2066..2068
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2082..2084
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2086..2088
FT /evidence="ECO:0007829|PDB:2NAA"
FT STRAND 2089..2091
FT /evidence="ECO:0007829|PDB:2NAA"
FT TURN 2093..2095
FT /evidence="ECO:0007829|PDB:2NAA"
FT STRAND 2098..2100
FT /evidence="ECO:0007829|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
