SMYD1_MOUSE
ID SMYD1_MOUSE Reviewed; 490 AA.
AC P97443; P97442; P97444; Q6DFW7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Histone-lysine N-methyltransferase Smyd1;
DE EC=2.1.1.354 {ECO:0000269|PubMed:20943667};
DE AltName: Full=CD8b-opposite;
DE AltName: Full=SET and MYND domain-containing protein 1;
DE AltName: Full=Zinc finger protein BOP;
DE Short=m-BOP;
GN Name=Smyd1; Synonyms=Bop;
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}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP VARIANTS ARG-95; LEU-160 AND THR-344.
RC STRAIN=BALB/cJ {ECO:0000269|PubMed:9013956}, and
RC C57BL/6J {ECO:0000269|PubMed:9013956};
RC TISSUE=Skeletal muscle {ECO:0000269|PubMed:9013956}, and
RC Spleen {ECO:0000269|PubMed:9013956};
RX PubMed=9013956;
RA Hwang I., Gottlieb P.D.;
RT "The Bop gene adjacent to the mouse CD8b gene encodes distinct zinc-finger
RT proteins expressed in CTLs and in muscle.";
RL J. Immunol. 158:1165-1174(1997).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION TO N-TERMINUS.
RA Gottlieb P.D., Hwang I.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFOFRM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP HDAC1; HDAC2 AND HDAC3.
RX PubMed=11923873; DOI=10.1038/ng866;
RA Gottlieb P.D., Pierce S.A., Sims R.J. III, Yamagishi H., Weihe E.K.,
RA Harriss J.V., Maika S.D., Kuziel W.A., King H.L., Olson E.N., Nakagawa O.,
RA Srivastava D.;
RT "Bop encodes a muscle-restricted protein containing MYND and SET domains
RT and is essential for cardiac differentiation and morphogenesis.";
RL Nat. Genet. 31:25-32(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-ORNITHINE,
RP CATALYTIC ACTIVITY, ZINC-BINDING SITES, FUNCTION, AND INTERACTION WITH NACA
RP ISOFORM SKNAC.
RX PubMed=20943667; DOI=10.1074/jbc.m110.168187;
RA Sirinupong N., Brunzelle J., Ye J., Pirzada A., Nico L., Yang Z.;
RT "Crystal structure of cardiac-specific histone methyltransferase SmyD1
RT reveals unusual active site architecture.";
RL J. Biol. Chem. 285:40635-40644(2010).
CC -!- FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me). Acts as a
CC transcriptional repressor. Essential for cardiomyocyte differentiation
CC and cardiac morphogenesis. {ECO:0000269|PubMed:11923873,
CC ECO:0000269|PubMed:20943667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000269|PubMed:20943667};
CC -!- SUBUNIT: Interacts with HDAC1, HDAC2 and HDAC3. Interacts (via MYND-
CC type zinc finger) with NACA isoform skNAC.
CC {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:20943667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11923873}. Nucleus
CC {ECO:0000269|PubMed:11923873}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ISKM-BOP1 {ECO:0000269|PubMed:9013956};
CC IsoId=P97443-1; Sequence=Displayed;
CC Name=2; Synonyms=SKM-BOP2 {ECO:0000269|PubMed:9013956};
CC IsoId=P97443-2; Sequence=VSP_050403, VSP_050404;
CC Name=3; Synonyms=T-BOP {ECO:0000269|PubMed:9013956};
CC IsoId=P97443-3; Sequence=VSP_050402;
CC -!- TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle,
CC lymphocytes and thymus. {ECO:0000269|PubMed:11923873,
CC ECO:0000269|PubMed:9013956}.
CC -!- DOMAIN: The SET domain is split between the S-sequence (residues 1-49)
CC and the core SET domain (residues 181-258), however the two segments
CC still come together to form a conserved SET domain fold.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53021.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC53022.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U76371; AAC53020.1; -; mRNA.
DR EMBL; U76373; AAC53021.2; ALT_INIT; mRNA.
DR EMBL; U76374; AAC53022.2; ALT_INIT; mRNA.
DR EMBL; AK142252; BAE24995.1; -; mRNA.
DR EMBL; CH466523; EDK98934.1; -; Genomic_DNA.
DR EMBL; BC076601; AAH76601.1; -; mRNA.
DR CCDS; CCDS20227.2; -. [P97443-2]
DR CCDS; CCDS51805.1; -. [P97443-1]
DR RefSeq; NP_001153599.1; NM_001160127.1. [P97443-1]
DR RefSeq; NP_033892.2; NM_009762.2. [P97443-2]
DR PDB; 3N71; X-ray; 2.30 A; A=1-490.
DR PDBsum; 3N71; -.
DR AlphaFoldDB; P97443; -.
DR SMR; P97443; -.
DR BioGRID; 198379; 10.
DR ELM; P97443; -.
DR IntAct; P97443; 1.
DR STRING; 10090.ENSMUSP00000073911; -.
DR iPTMnet; P97443; -.
DR PhosphoSitePlus; P97443; -.
DR MaxQB; P97443; -.
DR PaxDb; P97443; -.
DR PRIDE; P97443; -.
DR ProteomicsDB; 261586; -. [P97443-1]
DR ProteomicsDB; 261587; -. [P97443-2]
DR ProteomicsDB; 261588; -. [P97443-3]
DR Antibodypedia; 47498; 233 antibodies from 27 providers.
DR DNASU; 12180; -.
DR Ensembl; ENSMUST00000074301; ENSMUSP00000073911; ENSMUSG00000055027. [P97443-1]
DR Ensembl; ENSMUST00000114186; ENSMUSP00000109824; ENSMUSG00000055027. [P97443-2]
DR GeneID; 12180; -.
DR KEGG; mmu:12180; -.
DR UCSC; uc009cgj.2; mouse. [P97443-1]
DR CTD; 150572; -.
DR MGI; MGI:104790; Smyd1.
DR VEuPathDB; HostDB:ENSMUSG00000055027; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00940000156114; -.
DR HOGENOM; CLU_018406_1_1_1; -.
DR InParanoid; P97443; -.
DR OMA; YAHGVFP; -.
DR OrthoDB; 981799at2759; -.
DR PhylomeDB; P97443; -.
DR TreeFam; TF106487; -.
DR BioGRID-ORCS; 12180; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Smyd1; mouse.
DR EvolutionaryTrace; P97443; -.
DR PRO; PR:P97443; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P97443; protein.
DR Bgee; ENSMUSG00000055027; Expressed in hindlimb stylopod muscle and 155 other tissues.
DR ExpressionAtlas; P97443; baseline and differential.
DR Genevisible; P97443; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IPI:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR CDD; cd10526; SET_SMYD1; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044418; SMYD1_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..490
FT /note="Histone-lysine N-methyltransferase Smyd1"
FT /id="PRO_0000218308"
FT DOMAIN 7..253
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 52..90
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 17..19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 205..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 270..272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT VAR_SEQ 6..45
FT /note="MENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFD -> MKNGEACG
FT GWQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9013956"
FT /id="VSP_050402"
FT VAR_SEQ 220
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9013956"
FT /id="VSP_050403"
FT VAR_SEQ 221..233
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9013956"
FT /id="VSP_050404"
FT VARIANT 95
FT /note="K -> R (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:9013956"
FT VARIANT 160
FT /note="P -> L (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:9013956"
FT VARIANT 344
FT /note="A -> T (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:9013956"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 76..96
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 277..281
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3N71"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:3N71"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 390..405
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:3N71"
FT HELIX 432..465
FT /evidence="ECO:0007829|PDB:3N71"
SQ SEQUENCE 490 AA; 56496 MW; 5D18208678771CBE CRC64;
MTIGSMENVE VFTSEGKGRG LKATKEFWAA DVIFAERAYS AVVFDSLINF VCHTCFKRQE
KLHRCGQCKF AHYCDRTCQK DAWLNHKNEC AAIKKYGKVP NENIRLAARI MWRVEREGTG
LTEGCLVSVD DLQNHVEHFG EEEQKELRVD VDTFLQYWPP QSQQFSMQYI SHIFGVINCN
GFTLSDQRGL QAVGVGIFPN LGLVNHDCWP NCTVIFNNGN HEAVKSMFHT QMRIELRALG
KISEGEELTV SYIDFLHLSE ERRRQLKKQY YFDCSCEHCQ KGLKDDLFLA AKEDPKPSQE
VVKEMIQFSK DTLEKIDKAR SEGLYHEVVK LCRECLEKQE PVFADTNLYV LRLLSIASEV
LSYLQAYEEA SHYARRMVDG YMKLYHHNNA QLGMAVMRAG LTNWHAGHIE VGHGMICKAY
AILLVTHGPS HPITKDLEAM RMQTEMELRM FRQNEFMYHK MREAALNNQP MQVMAEPSNE
PAPALFHKKQ
