MYT1L_RAT
ID MYT1L_RAT Reviewed; 1187 AA.
AC P70475; D4A9W2; P70589;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Myelin transcription factor 1-like protein;
DE Short=MyT1-L;
DE Short=MyT1L;
DE AltName: Full=Neural zinc finger factor 1 {ECO:0000303|PubMed:8631881};
DE Short=NZF-1 {ECO:0000303|PubMed:8631881};
GN Name=Myt1l; Synonyms=Nzf1 {ECO:0000303|PubMed:8631881};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8631881; DOI=10.1074/jbc.271.18.10723;
RA Jiang Y., Yu V.C., Buchholz F., O'Connell S., Rhodes S.J., Candeloro C.,
RA Xia Y.-R., Lusis A.J., Rosenfeld M.G.;
RT "A novel family of Cys-Cys, His-Cys zinc finger transcription factors
RT expressed in developing nervous system and pituitary gland.";
RL J. Biol. Chem. 271:10723-10730(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 371-1187.
RX PubMed=8980226; DOI=10.1016/s0092-8674(00)81815-2;
RA Bellefroid E.J., Bourguignon C., Hollemann T., Ma Q., Anderson D.J.,
RA Kintner C., Pieler T.;
RT "X-MyT1, a Xenopus C2HC-type zinc finger protein with a regulatory function
RT in neuronal differentiation.";
RL Cell 87:1191-1202(1996).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9373037;
RX DOI=10.1002/(sici)1097-4547(19971015)50:2<272::aid-jnr16>3.0.co;2-a;
RA Kim J.G., Armstrong R.C., Agoston D.V., Robinsky A., Wiese C., Nagle J.,
RA Hudson L.D.;
RT "Myelin transcription factor 1 (Myt1) of the oligodendrocyte lineage, along
RT with a closely related CCHC zinc finger, is expressed in developing neurons
RT in the mammalian central nervous system.";
RL J. Neurosci. Res. 50:272-290(1997).
RN [5]
RP STRUCTURE BY NMR OF 487-548.
RX PubMed=14744132; DOI=10.1021/bi035159d;
RA Berkovits-Cymet H.J., Amann B.T., Berg J.M.;
RT "Solution structure of a CCHHC domain of neural zinc finger factor-1 and
RT its implications for DNA binding.";
RL Biochemistry 43:898-903(2004).
CC -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC differentiation (PubMed:9373037). Acts by specifically repressing
CC expression of non-neuronal genes during neuron differentiation (By
CC similarity). In contrast to other transcription repressors that inhibit
CC specific lineages, mediates repression of multiple differentiation
CC programs (By similarity). Also represses expression of negative
CC regulators of neurogenesis, such as members of the Notch signaling
CC pathway, including HES1 (By similarity). The combination of three
CC transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to
CC reprogram fibroblasts and other somatic cells into induced neuronal
CC (iN) cells in vitro (By similarity). Directly binds the 5'-AAGTT-3'
CC core motif present on the promoter of target genes and represses
CC transcription by recruiting a multiprotein complex containing SIN3B (By
CC similarity). The 5'-AAGTT-3' core motif is absent from the promoter of
CC neural genes (By similarity). {ECO:0000250|UniProtKB:P97500,
CC ECO:0000269|PubMed:9373037}.
CC -!- SUBUNIT: Interacts with SIN3B. {ECO:0000250|UniProtKB:P97500}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9373037}. Chromosome
CC {ECO:0000250|UniProtKB:P97500}. Note=Preferentially binds to DNA
CC binding sites that are in an open chromatin configuration.
CC {ECO:0000250|UniProtKB:P97500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P70475-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70475-2; Sequence=Not described;
CC Name=3;
CC IsoId=P70475-3; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Brain, testis and pituitary gland. Expression is
CC higher in the brain than in the testis and pituitary gland. Highest
CC level expression seen in the developing CNS.
CC {ECO:0000269|PubMed:8631881, ECO:0000269|PubMed:9373037}.
CC -!- DEVELOPMENTAL STAGE: Detected at E11.5 and expression is seen
CC throughout the proliferating cortex neuroepithelium, developing
CC medulla, and spinal cord. At E12.5 found in the nasal epithelium and at
CC E13.5 detected in the trigeminal ganglia, dorsal root ganglia and the
CC ganglion cell layer of the retina. At E14-E15 expressed at high levels
CC in the brain and spinal cord and then levels subsequently decrease.
CC {ECO:0000269|PubMed:8631881, ECO:0000269|PubMed:9373037}.
CC -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AABR07063792; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AABR07063793; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AABR07063794; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AABR07063795; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AABR07063796; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AABR07063797; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC52728.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U48809; AAC52728.1; ALT_FRAME; mRNA.
DR EMBL; AABR07063792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07063793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07063794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07063795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07063796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07063797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U67081; AAB40718.1; -; mRNA.
DR PIR; T46637; T46637.
DR RefSeq; NP_446340.1; NM_053888.1. [P70475-1]
DR PDB; 1PXE; NMR; -; A=487-548.
DR PDBsum; 1PXE; -.
DR AlphaFoldDB; P70475; -.
DR SMR; P70475; -.
DR BioGRID; 250552; 1.
DR STRING; 10116.ENSRNOP00000005905; -.
DR iPTMnet; P70475; -.
DR PhosphoSitePlus; P70475; -.
DR PaxDb; P70475; -.
DR PRIDE; P70475; -.
DR GeneID; 116668; -.
DR KEGG; rno:116668; -.
DR CTD; 23040; -.
DR RGD; 620550; Myt1l.
DR eggNOG; KOG3803; Eukaryota.
DR InParanoid; P70475; -.
DR OrthoDB; 116799at2759; -.
DR PhylomeDB; P70475; -.
DR EvolutionaryTrace; P70475; -.
DR PRO; PR:P70475; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IMP:CAFA.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR InterPro; IPR013681; Myelin_TF.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF08474; MYT1; 1.
DR Pfam; PF01530; zf-C2HC; 6.
DR SUPFAM; SSF103637; SSF103637; 6.
DR PROSITE; PS51802; ZF_CCHHC; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Coiled coil;
KW Developmental protein; Differentiation; DNA-binding; Metal-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1187
FT /note="Myelin transcription factor 1-like protein"
FT /id="PRO_0000096675"
FT ZN_FING 22..65
FT /note="CCHHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 496..539
FT /note="CCHHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 540..583
FT /note="CCHHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 895..938
FT /note="CCHHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 944..987
FT /note="CCHHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 997..1040
FT /note="CCHHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1055..1131
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 922
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 958
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 971
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1011
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 1030
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97500"
FT CONFLICT 39
FT /note="S -> T (in Ref. 1; AAC52728)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="M -> V (in Ref. 1; AAC52728)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..239
FT /note="DSD -> HSS (in Ref. 1; AAC52728)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="S -> T (in Ref. 1; AAC52728)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="T -> N (in Ref. 1; AAC52728)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="N -> H (in Ref. 3; AAB40718)"
FT /evidence="ECO:0000305"
FT CONFLICT 804
FT /note="S -> T (in Ref. 3; AAB40718)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="N -> I (in Ref. 3; AAB40718)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="G -> A (in Ref. 3; AAB40718)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092..1098
FT /note="VTITTME -> ITTMD (in Ref. 3; AAB40718)"
FT /evidence="ECO:0000305"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:1PXE"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:1PXE"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:1PXE"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:1PXE"
SQ SEQUENCE 1187 AA; 132926 MW; 10B2616415195DD1 CRC64;
MDVDAEEKRH RTRSKGVRVP VEPAIQELFS CPTPGCDGSG HVSGKYARHR SVYGCPLAKK
RKTQDKQPQE PAPKRKPFAV KADSSSVDEC YESDGTEDMD DKEEDDDEEF SEDNDEQGDD
DDEDEVDRED EEEIEEEDDE DDEDDDDGDD VEEEEDDDDE EEEEEEEEEE NEDHQMSCTR
IMQDPEKDDN NNDEYDNYDE LVAKSLLNLG KIAEDAAYRA RTESEMNSNT SNSLEDDSDK
NENLGRKSEL SLDLDSDVVR ETVDSLKLLA QGHGVVLSEN ISDRSYAEGM SQQDSRNMNY
VMLGKPMNNG LMEKMVEESD EEVCLSSLEC LRNQCFDLAR KLSETNPQDR SQPPNMSVRQ
HVRQEDDFPG RTPDRSYSDM MNLMRLEEQL SPRSRTFSSC AKEDGCHERD DDTTSVNSDR
SEEVFDMTKG NLTLLEKAIA LETERAKAMR EKMAMDAGRR DNLRSYEDQS PRQLAGEDRK
SKSSDSHVKK PYYDPSRTEK RESKCPTPGC DGTGHVTGLY PHHRSLSGCP HKDRVPPEIL
AMHENVLKCP TPGCTGRGHV NSNRNSHRSL SGCPIAAAEK LAKAQEKHQS CDVSKSNQAS
DRVLRPMCFV KQLEIPQYGY RNNVPTTTPR SNLAKELEKY SKTSFEYNSY DNHTYGKRAI
APKVQTRDIS PKGYDDAKRY CKNASPSSST TSSYAPSSSS NLSCGGGSSA SSTCSKSSFD
YTHDMEAAHM AATAILNLST RCREMPQNLS TKPQDLCTAR NPDMEVDENG TLDLSMNKQR
PRDSCCPVLT PLEPMSPQQQ AVMSSRCFQL SEGDCWDLPV DYTKMKPRRV DEEDPKEITP
EDLDPFQEAL EERRYPGEVT IPSPKPKYPQ CKESKKDLIT LSGCPLADKS IRSMLATSSQ
ELKCPTPGCD GSGHITGNYA SHRSLSGCPR AKKSGIRIAQ SKEDKEDQEP IRCPVPGCDG
QGHITGKYAS HRSASGCPLA AKRQKDGYLN GSQFSWKSVK TEGMSCPTPG CDGSGHVSGS
FLTHRSLSGC PRATSAMKKA KLSGEQMLTI KQRASNGIEN DEEIKQLDEE IKELNESNSQ
MEADMIKLRT QVTITTMESN LKTIEEENKV IEQQNESLLH ELANLSQSLI HSLANIQLPH
MDPINEQNFD AYVTTLTEMY TNQDRYQSPE NKALLENIKQ AVRGIQV
