GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5B_HUMAN
LinkDB: KMT5B_HUMAN
Original site: KMT5B_HUMAN 
ID   KMT5B_HUMAN             Reviewed;         885 AA.
AC   Q4FZB7; B7WNX7; Q3SX56; Q4V775; Q6P150; Q96E44; Q9BUL0; Q9H022;
AC   Q9H2K3; Q9NXV3; Q9Y393;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 4.
DT   20-JUN-2018, entry version 120.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5B {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 5B;
DE   AltName: Full=Lysine-specific methyltransferase 5B {ECO:0000312|HGNC:HGNC:24283};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 1;
DE            Short=Su(var)4-20 homolog 1;
DE            Short=Suv4-20h1;
GN   Name=KMT5B {ECO:0000312|HGNC:HGNC:24283}; Synonyms=SUV420H1;
GN   ORFNames=CGI-85;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP   VARIANT ASN-9.
RC   TISSUE=Mammary gland, Placenta, Testis, and Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-275 (ISOFORM 1).
RX   PubMed=11401438; DOI=10.1006/geno.2000.6492;
RA   Twells R.C.J., Metzker M.L., Brown S.D., Cox R., Garey C., Hammond H.,
RA   Hey P.J., Levy E., Nakagawa Y., Philips M.S., Todd J.A., Hess J.F.;
RT   "The sequence and gene characterization of a 400-kb candidate region
RT   for IDDM4 on chromosome 11q13.";
RL   Genomics 72:231-242(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-885 (ISOFORM 2).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-884.
RC   TISSUE=Colon;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-885.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   INDUCTION.
RX   PubMed=16322686; DOI=10.4161/cbt.5.1.2288;
RA   Tryndyak V.P., Kovalchuk O., Pogribny I.P.;
RT   "Loss of DNA methylation and histone H4 lysine 20 trimethylation in
RT   human breast cancer cells is associated with aberrant expression of
RT   DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and
RT   methyl-binding proteins.";
RL   Cancer Biol. Ther. 5:65-70(2006).
RN   [8]
RP   FUNCTION, INTERACTION WITH FRG1, AND SUBCELLULAR LOCATION.
RX   PubMed=23720823; DOI=10.1093/jmcb/mjt018;
RA   Neguembor M.V., Xynos A., Onorati M.C., Caccia R., Bortolanza S.,
RA   Godio C., Pistoni M., Corona D.F., Schotta G., Gabellini D.;
RT   "FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone
RT   methyltransferase and impairs myogenesis.";
RL   J. Mol. Cell Biol. 5:294-307(2013).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-555, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-555, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-555, 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: Histone methyltransferase that specifically
CC       trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in pericentric heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin in these regions. KMT5B is targeted
CC       to histone H3 via its interaction with RB1 family proteins (RB1,
CC       RBL1 and RBL2) (By similarity). Plays a role in myogenesis by
CC       regulating the expression of target genes, such as EID3.
CC       {ECO:0000250, ECO:0000269|PubMed:23720823}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00903}.
CC   -!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
CC       Interacts with RB1 family proteins RB1, RBL1 and RBL2 (By
CC       similarity). Interacts (via C-terminus) with FRG1. {ECO:0000250,
CC       ECO:0000269|PubMed:23720823}.
CC   -!- INTERACTION:
CC       Q61026:Ncoa2 (xeno); NbExp=4; IntAct=EBI-15746366, EBI-688662;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23720823}.
CC       Chromosome {ECO:0000250}. Note=Associated with pericentric
CC       heterochromatin. CBX1 and CBX5 are required for the localization
CC       to pericentric heterochromatin (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4FZB7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4FZB7-2; Sequence=VSP_024051, VSP_024052;
CC       Name=3;
CC         IsoId=Q4FZB7-4; Sequence=VSP_040034, VSP_040035;
CC         Note=No experimental confirmation available.;
CC   -!- INDUCTION: Strongly down-regulated in breast cancer cells.
CC       {ECO:0000269|PubMed:16322686}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00903}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD34080.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAG36937.1; Type=Frameshift; Positions=233, 249, 254, 272; Evidence={ECO:0000305};
CC       Sequence=AAH98121.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC       Sequence=AAI04484.1; Type=Frameshift; Positions=396; Evidence={ECO:0000305};
CC       Sequence=BAA90905.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AP002992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002522; AAH02522.2; -; mRNA.
DR   EMBL; BC012933; AAH12933.2; -; mRNA.
DR   EMBL; BC065287; AAH65287.1; -; mRNA.
DR   EMBL; BC087834; AAH87834.1; -; mRNA.
DR   EMBL; BC098121; AAH98121.1; ALT_SEQ; mRNA.
DR   EMBL; BC099714; AAH99714.1; -; mRNA.
DR   EMBL; BC103498; AAI03499.1; -; mRNA.
DR   EMBL; BC104483; AAI04484.1; ALT_FRAME; mRNA.
DR   EMBL; AF264782; AAG36937.1; ALT_FRAME; mRNA.
DR   EMBL; AF151843; AAD34080.1; ALT_INIT; mRNA.
DR   EMBL; AK000046; BAA90905.1; ALT_INIT; mRNA.
DR   EMBL; AL512763; CAC21680.1; -; mRNA.
DR   CCDS; CCDS31623.1; -. [Q4FZB7-1]
DR   CCDS; CCDS44660.1; -. [Q4FZB7-2]
DR   RefSeq; NP_001287838.1; NM_001300909.1.
DR   RefSeq; NP_057112.3; NM_016028.4.
DR   RefSeq; NP_060105.3; NM_017635.4.
DR   RefSeq; XP_005274092.2; XM_005274035.3.
DR   RefSeq; XP_011543393.1; XM_011545091.1.
DR   RefSeq; XP_011543395.1; XM_011545093.2.
DR   RefSeq; XP_011543396.1; XM_011545094.2.
DR   UniGene; Hs.632120; -.
DR   PDB; 3S8P; X-ray; 1.85 A; A/B=63-335.
DR   PDB; 5CPR; X-ray; 2.22 A; B=69-335.
DR   PDB; 5WBV; X-ray; 2.30 A; A/B=63-335.
DR   PDBsum; 3S8P; -.
DR   PDBsum; 5CPR; -.
DR   PDBsum; 5WBV; -.
DR   ProteinModelPortal; Q4FZB7; -.
DR   SMR; Q4FZB7; -.
DR   BioGrid; 119300; 6.
DR   DIP; DIP-48656N; -.
DR   IntAct; Q4FZB7; 7.
DR   STRING; 9606.ENSP00000305899; -.
DR   BindingDB; Q4FZB7; -.
DR   ChEMBL; CHEMBL2321645; -.
DR   GuidetoPHARMACOLOGY; 2717; -.
DR   iPTMnet; Q4FZB7; -.
DR   PhosphoSitePlus; Q4FZB7; -.
DR   BioMuta; SUV420H1; -.
DR   DMDM; 332278247; -.
DR   EPD; Q4FZB7; -.
DR   MaxQB; Q4FZB7; -.
DR   PaxDb; Q4FZB7; -.
DR   PeptideAtlas; Q4FZB7; -.
DR   PRIDE; Q4FZB7; -.
DR   ProteomicsDB; 62098; -.
DR   ProteomicsDB; 62099; -. [Q4FZB7-2]
DR   ProteomicsDB; 62100; -. [Q4FZB7-4]
DR   Ensembl; ENST00000304363; ENSP00000305899; ENSG00000110066.
DR   Ensembl; ENST00000401547; ENSP00000385965; ENSG00000110066.
DR   Ensembl; ENST00000405515; ENSP00000385640; ENSG00000110066.
DR   Ensembl; ENST00000615954; ENSP00000484858; ENSG00000110066.
DR   GeneID; 51111; -.
DR   KEGG; hsa:51111; -.
DR   UCSC; uc001onm.2; human. [Q4FZB7-1]
DR   CTD; 51111; -.
DR   DisGeNET; 51111; -.
DR   EuPathDB; HostDB:ENSG00000110066.14; -.
DR   GeneCards; KMT5B; -.
DR   HGNC; HGNC:24283; KMT5B.
DR   HPA; HPA063648; -.
DR   MalaCards; KMT5B; -.
DR   MIM; 610881; gene.
DR   neXtProt; NX_Q4FZB7; -.
DR   PharmGKB; PA134958369; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   HOVERGEN; HBG105761; -.
DR   InParanoid; Q4FZB7; -.
DR   KO; K11429; -.
DR   OrthoDB; EOG091G0IUY; -.
DR   PhylomeDB; Q4FZB7; -.
DR   TreeFam; TF106433; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; KMT5B; human.
DR   GeneWiki; SUV420H1; -.
DR   GenomeRNAi; 51111; -.
DR   PRO; PR:Q4FZB7; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000110066; -.
DR   ExpressionAtlas; Q4FZB7; baseline and differential.
DR   Genevisible; Q4FZB7; HS.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:Ensembl.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Isopeptide bond; Methyltransferase; Myogenesis;
KW   Nucleus; Polymorphism; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    885       Histone-lysine N-methyltransferase KMT5B.
FT                                /FTId=PRO_0000281787.
FT   DOMAIN      193    308       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   CROSSLNK    555    555       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ     274    274       D -> DLINS (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040034.
FT   VAR_SEQ     275    885       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040035.
FT   VAR_SEQ     392    393       TS -> SK (in isoform 2).
FT                                {ECO:0000303|PubMed:10810093,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024051.
FT   VAR_SEQ     394    885       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10810093,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024052.
FT   VARIANT       9      9       I -> N (in dbSNP:rs2512606).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_047765.
FT   CONFLICT     74     74       A -> P (in Ref. 4; AAD34080).
FT                                {ECO:0000305}.
FT   CONFLICT     79     79       E -> G (in Ref. 4; AAD34080).
FT                                {ECO:0000305}.
FT   CONFLICT     99     99       K -> Q (in Ref. 4; AAD34080).
FT                                {ECO:0000305}.
FT   CONFLICT    108    108       R -> W (in Ref. 3; AAG36937).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       N -> K (in Ref. 4; AAD34080).
FT                                {ECO:0000305}.
FT   CONFLICT    135    135       E -> G (in Ref. 4; AAD34080).
FT                                {ECO:0000305}.
FT   CONFLICT    469    469       K -> E (in Ref. 5; BAA90905).
FT                                {ECO:0000305}.
FT   CONFLICT    483    483       V -> A (in Ref. 5; BAA90905).
FT                                {ECO:0000305}.
FT   HELIX        74     93       {ECO:0000244|PDB:3S8P}.
FT   HELIX       134    147       {ECO:0000244|PDB:3S8P}.
FT   HELIX       150    157       {ECO:0000244|PDB:3S8P}.
FT   HELIX       161    167       {ECO:0000244|PDB:3S8P}.
FT   HELIX       172    187       {ECO:0000244|PDB:3S8P}.
FT   HELIX       191    193       {ECO:0000244|PDB:3S8P}.
FT   STRAND      195    200       {ECO:0000244|PDB:3S8P}.
FT   STRAND      207    216       {ECO:0000244|PDB:3S8P}.
FT   STRAND      223    234       {ECO:0000244|PDB:3S8P}.
FT   HELIX       236    242       {ECO:0000244|PDB:3S8P}.
FT   TURN        245    247       {ECO:0000244|PDB:3S8P}.
FT   STRAND      252    255       {ECO:0000244|PDB:3S8P}.
FT   TURN        256    259       {ECO:0000244|PDB:3S8P}.
FT   STRAND      260    266       {ECO:0000244|PDB:3S8P}.
FT   HELIX       267    270       {ECO:0000244|PDB:3S8P}.
FT   STRAND      278    285       {ECO:0000244|PDB:3S8P}.
FT   STRAND      288    295       {ECO:0000244|PDB:3S8P}.
FT   TURN        309    312       {ECO:0000244|PDB:3S8P}.
FT   HELIX       314    316       {ECO:0000244|PDB:3S8P}.
FT   HELIX       322    327       {ECO:0000244|PDB:3S8P}.
FT   HELIX       330    332       {ECO:0000244|PDB:3S8P}.
SQ   SEQUENCE   885 AA;  99187 MW;  B4D4812C1F1A64AB CRC64;
     MKWLGESKIM VVNGRRNGGK LSNDHQQNQS KLQHTGKDTL KAGKNAVERR SNRCNGNSGF
     EGQSRYVPSS GMSAKELCEN DDLATSLVLD PYLGFQTHKM NTSAFPSRSS RHFSKSDSFS
     HNNPVRFRPI KGRQEELKEV IERFKKDEHL EKAFKCLTSG EWARHYFLNK NKMQEKLFKE
     HVFIYLRMFA TDSGFEILPC NRYSSEQNGA KIVATKEWKR NDKIELLVGC IAELSEIEEN
     MLLRHGENDF SVMYSTRKNC AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKALRDIEPG
     EEISCYYGDG FFGENNEFCE CYTCERRGTG AFKSRVGLPA PAPVINSKYG LRETDKRLNR
     LKKLGDSSKN SDSQSVSSNT DADTTQEKNN ATSNRKSSVG VKKNSKSRTL TRQSMSRIPA
     SSNSTSSKLT HINNSRVPKK LKKPAKPLLS KIKLRNHCKR LEQKNASRKL EMGNLVLKEP
     KVVLYKNLPI KKDKEPEGPA QAAVASGCLT RHAAREHRQN PVRGAHSQGE SSPCTYITRR
     SVRTRTNLKE ASDIKLEPNT LNGYKSSVTE PCPDSGEQLQ PAPVLQEEEL AHETAQKGEA
     KCHKSDTGMS KKKSRQGKLV KQFAKIEEST PVHDSPGKDD AVPDLMGPHS DQGEHSGTVG
     VPVSYTDCAP SPVGCSVVTS DSFKTKDSFR TAKSKKKRRI TRYDAQLILE NNSGIPKLTL
     RRRHDSSSKT NDQENDGMNS SKISIKLSKD HDNDNNLYVA KLNNGFNSGS GSSSTKLKIQ
     LKRDEENRGS YTEGLHENGV CCSDPLSLLE SRMEVDDYSQ YEEESTDDSS SSEGDEEEDD
     YDDDFEDDFI PLPPAKRLRL IVGKDSIDID ISSRRREDQS LRLNA
//
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