MSL2_HUMAN
ID MSL2_HUMAN Reviewed; 577 AA.
AC Q9HCI7; B4DYL4; G5E9I1; Q0D2P1; Q8NDB4; Q9NVS4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase MSL2;
DE EC=2.3.2.-;
DE AltName: Full=E3 ubiquitin-protein transferase MSL2 {ECO:0000305};
DE AltName: Full=Male-specific lethal 2-like 1;
DE Short=MSL2-like 1;
DE AltName: Full=Male-specific lethal-2 homolog;
DE Short=MSL-2;
DE AltName: Full=Male-specific lethal-2 homolog 1;
DE AltName: Full=RING finger protein 184;
GN Name=MSL2; Synonyms=KIAA1585, MSL2L1, RNF184;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 339-577 (ISOFORM 1).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION OF MSL COMPLEX COMPONENTS, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16227571; DOI=10.1128/mcb.25.21.9175-9188.2005;
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RT "A human protein complex homologous to the Drosophila MSL complex is
RT responsible for the majority of histone H4 acetylation at lysine 16.";
RL Mol. Cell. Biol. 25:9175-9188(2005).
RN [8]
RP ERRATUM OF PUBMED:16227571.
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RL Mol. Cell. Biol. 26:387-387(2006).
RN [9]
RP IDENTIFICATION IN THE MSL COMPLEX.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [10]
RP FUNCTION AS E3 UBIQUITIN LIGASE, AND MUTAGENESIS OF HIS-64.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase
RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.";
RL Mol. Cell 43:132-144(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-375, AND IDENTIFICATION BY MASS
RP 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-375, AND IDENTIFICATION BY MASS
RP 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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-116 IN COMPLEX WITH MSL1 AND
RP ZINC IONS, SUBUNIT, AND INTERACTION WITH MSL1.
RX PubMed=23084835; DOI=10.1016/j.molcel.2012.09.014;
RA Hallacli E., Lipp M., Georgiev P., Spielman C., Cusack S., Akhtar A.,
RA Kadlec J.;
RT "Msl1-mediated dimerization of the dosage compensation complex is essential
RT for male X-chromosome regulation in Drosophila.";
RL Mol. Cell 48:587-600(2012).
CC -!- FUNCTION: Component of histone acetyltransferase complex responsible
CC for the majority of histone H4 acetylation at lysine 16 which is
CC implicated in the formation of higher-order chromatin structure. Acts
CC as an E3 ubiquitin ligase that promotes monoubiquitination of histone
CC H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is
CC greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in
CC turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79'
CC (H3K79me) and leads to gene activation, including that of HOXA9 and
CC MEIS1. {ECO:0000269|PubMed:21726816}.
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and
CC MSL3 (PubMed:16543150, PubMed:23084835). Forms a MSL heterotetrameric
CC core with MSL1 (PubMed:16543150). {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:23084835}.
CC -!- INTERACTION:
CC Q9HCI7; Q68DK7: MSL1; NbExp=2; IntAct=EBI-2560775, EBI-2560816;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCI7-2; Sequence=VSP_046200;
CC -!- SIMILARITY: Belongs to the MSL2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32719.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91673.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13411.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046805; BAB13411.1; ALT_INIT; mRNA.
DR EMBL; AK001408; BAA91673.1; ALT_INIT; mRNA.
DR EMBL; AK302491; BAG63776.1; -; mRNA.
DR EMBL; AL834289; CAD38963.2; -; mRNA.
DR EMBL; AC092991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79119.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79120.1; -; Genomic_DNA.
DR EMBL; BC032719; AAH32719.1; ALT_INIT; mRNA.
DR EMBL; BC093764; AAH93764.1; -; mRNA.
DR EMBL; BC093790; AAH93790.1; -; mRNA.
DR CCDS; CCDS33861.1; -. [Q9HCI7-1]
DR CCDS; CCDS46922.1; -. [Q9HCI7-2]
DR RefSeq; NP_001138889.1; NM_001145417.1. [Q9HCI7-2]
DR RefSeq; NP_060603.2; NM_018133.3. [Q9HCI7-1]
DR RefSeq; XP_005247628.1; XM_005247571.3. [Q9HCI7-2]
DR RefSeq; XP_006713747.1; XM_006713684.3. [Q9HCI7-2]
DR RefSeq; XP_011511251.1; XM_011512949.2. [Q9HCI7-2]
DR PDB; 4B7Y; X-ray; 3.25 A; C/D=1-116.
DR PDB; 4B86; X-ray; 3.50 A; C/D/G/H/K/L=1-116.
DR PDBsum; 4B7Y; -.
DR PDBsum; 4B86; -.
DR AlphaFoldDB; Q9HCI7; -.
DR SMR; Q9HCI7; -.
DR BioGRID; 120467; 36.
DR ComplexPortal; CPX-815; MSL histone acetyltransferase complex.
DR CORUM; Q9HCI7; -.
DR IntAct; Q9HCI7; 16.
DR MINT; Q9HCI7; -.
DR STRING; 9606.ENSP00000311827; -.
DR iPTMnet; Q9HCI7; -.
DR PhosphoSitePlus; Q9HCI7; -.
DR BioMuta; MSL2; -.
DR DMDM; 158564022; -.
DR EPD; Q9HCI7; -.
DR jPOST; Q9HCI7; -.
DR MassIVE; Q9HCI7; -.
DR MaxQB; Q9HCI7; -.
DR PaxDb; Q9HCI7; -.
DR PeptideAtlas; Q9HCI7; -.
DR PRIDE; Q9HCI7; -.
DR ProteomicsDB; 33946; -.
DR ProteomicsDB; 81733; -. [Q9HCI7-1]
DR Antibodypedia; 1091; 174 antibodies from 22 providers.
DR DNASU; 55167; -.
DR Ensembl; ENST00000309993.3; ENSP00000311827.2; ENSG00000174579.4. [Q9HCI7-1]
DR Ensembl; ENST00000434835.2; ENSP00000387948.2; ENSG00000174579.4. [Q9HCI7-2]
DR GeneID; 55167; -.
DR KEGG; hsa:55167; -.
DR MANE-Select; ENST00000309993.3; ENSP00000311827.2; NM_018133.4; NP_060603.2.
DR UCSC; uc003eqx.2; human. [Q9HCI7-1]
DR CTD; 55167; -.
DR DisGeNET; 55167; -.
DR GeneCards; MSL2; -.
DR HGNC; HGNC:25544; MSL2.
DR HPA; ENSG00000174579; Low tissue specificity.
DR MIM; 614802; gene.
DR neXtProt; NX_Q9HCI7; -.
DR OpenTargets; ENSG00000174579; -.
DR PharmGKB; PA164723152; -.
DR VEuPathDB; HostDB:ENSG00000174579; -.
DR eggNOG; ENOG502QPJR; Eukaryota.
DR GeneTree; ENSGT00390000016814; -.
DR HOGENOM; CLU_038772_0_0_1; -.
DR InParanoid; Q9HCI7; -.
DR OMA; LCTTGID; -.
DR OrthoDB; 1446941at2759; -.
DR PhylomeDB; Q9HCI7; -.
DR TreeFam; TF328848; -.
DR PathwayCommons; Q9HCI7; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9HCI7; -.
DR SIGNOR; Q9HCI7; -.
DR BioGRID-ORCS; 55167; 33 hits in 1123 CRISPR screens.
DR ChiTaRS; MSL2; human.
DR GenomeRNAi; 55167; -.
DR Pharos; Q9HCI7; Tbio.
DR PRO; PR:Q9HCI7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HCI7; protein.
DR Bgee; ENSG00000174579; Expressed in secondary oocyte and 192 other tissues.
DR ExpressionAtlas; Q9HCI7; baseline and differential.
DR Genevisible; Q9HCI7; HS.
DR GO; GO:0072487; C:MSL complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR CDD; cd13122; MSL2_CXC; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037922; MSL2.
DR InterPro; IPR032049; Msl2-CXC.
DR InterPro; IPR032043; Msl2_Znf-RING.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16048; PTHR16048; 1.
DR Pfam; PF16682; MSL2-CXC; 1.
DR Pfam; PF16685; zf-RING_10; 1.
DR SMART; SM01114; CXC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="E3 ubiquitin-protein ligase MSL2"
FT /id="PRO_0000299536"
FT ZN_FING 44..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..116
FT /note="Sufficient for interaction with MSL1"
FT /evidence="ECO:0000269|PubMed:23084835"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046200"
FT MUTAGEN 64
FT /note="H->Y: Great reduction in H2B ubiquitination. No
FT effect on MSL1-binding."
FT /evidence="ECO:0000269|PubMed:21726816"
FT CONFLICT 348
FT /note="D -> E (in Ref. 2; BAG63776)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="S -> G (in Ref. 2; BAA91673)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:4B7Y"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:4B7Y"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4B7Y"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4B7Y"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4B7Y"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4B7Y"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4B7Y"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:4B7Y"
SQ SEQUENCE 577 AA; 62541 MW; 756C7625E0AF1CA6 CRC64;
MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL LQDPIAPTNS
TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV NCYKKLCEYI TQTTLARDII
EAVDCSSDIL ALLNDGSLFC EETEKPSDSS FTLCLTHSPL PSTSEPTTDP QASLSPMSES
TLSIAIGSSV INGLPTYNGL SIDRFGINIP SPEHSNTIDV CNTVDIKTED LSDSLPPVCD
TVATDLCSTG IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKIAKLNR KRSRSESDSE KVQPLPISTI
IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT VLLSTKSMKK SHEHGSKKSH
SKTKPGILKK DKAVKEKIPS HHFMPGSPTK TVYKKPQEKK GCKCGRATQN PSVLTCRGQR
CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS
TSTSVINVTG SPVTTFLAAS THDDKSLDEA IDMRFDC
