GT2D1_MOUSE
ID GT2D1_MOUSE Reviewed; 1104 AA.
AC Q9JI57; Q547E0; Q80WJ8; Q80WJ9; Q80WK0; Q80WK1; Q8R4X5; Q8R4X6; Q8R4X7;
AC Q8R4X8; Q8VHD5; Q8VI58; Q9EQE7; Q9ESZ6; Q9ESZ7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=General transcription factor II-I repeat domain-containing protein 1;
DE Short=GTF2I repeat domain-containing protein 1;
DE AltName: Full=Binding factor for early enhancer;
GN Name=Gtf2ird1; Synonyms=Ben;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Swiss Webster / NIH;
RX PubMed=10861001; DOI=10.1073/pnas.97.13.7342;
RA Bayarsaihan D., Ruddle F.H.;
RT "Isolation and characterization of BEN, a member of the TFII-I family of
RT DNA-binding proteins containing distinct helix-loop-helix domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7342-7347(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=11352562; DOI=10.1006/geno.2001.6507;
RA Durkin M.E., Keck-Waggoner C.L., Popescu N.C., Thorgeirsson S.S.;
RT "Integration of a c-myc transgene results in disruption of the mouse
RT Gtf2ird1 gene, the homologue of the human GTF2IRD1 gene hemizygously
RT deleted in Williams-Beuren syndrome.";
RL Genomics 73:20-27(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=129/SvJ;
RX PubMed=11827466; DOI=10.1006/geno.2001.6674;
RA Bayarsaihan D., Dunai J., Greally J.M., Kawasaki K., Sumiyama K.,
RA Enkhmandakh B., Shimizu N., Ruddle F.H.;
RT "Genomic organization of the genes Gtf2ird1, Gtf2i, and Ncf1 at the mouse
RT chromosome 5 region syntenic to the human chromosome 7q11.23 Williams
RT syndrome critical region.";
RL Genomics 79:137-143(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9 AND 10), AND
RP SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ, and C57BL/6 X DBA/2; TISSUE=Skeletal muscle;
RX PubMed=12780350; DOI=10.1042/bj20030189;
RA Tay E.S.E., Guven K.L., Subramaniam N., Polly P., Issa L.L., Gunning P.W.,
RA Hardeman E.C.;
RT "Regulation of alternative splicing of Gtf2ird1 and its impact on slow
RT muscle promoter activity.";
RL Biochem. J. 374:359-367(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RC STRAIN=129/Sv;
RA Green E.D.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=11438732; DOI=10.1073/pnas.141222298;
RA Tussie-Luna M.I., Bayarsaihan D., Ruddle F.H., Roy A.L.;
RT "Repression of TFII-I-dependent transcription by nuclear exclusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7789-7794(2001).
CC -!- FUNCTION: May be a transcription regulator involved in cell-cycle
CC progression and skeletal muscle differentiation. May repress GTF2I
CC transcriptional functions, by preventing its nuclear residency, or by
CC inhibiting its transcriptional activation. May contribute to slow-
CC twitch fiber type specificity during myogenesis and in regenerating
CC muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds
CC specifically and with high affinity to the EFG sequences derived from
CC the early enhancer of HOXC8. {ECO:0000269|PubMed:11438732}.
CC -!- SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its C-
CC terminus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00484,
CC ECO:0000269|PubMed:12780350}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=2; Synonyms=Beta, 3b7;
CC IsoId=Q9JI57-1; Sequence=Displayed;
CC Name=1; Synonyms=Alpha, 3a7;
CC IsoId=Q9JI57-2; Sequence=VSP_003876;
CC Name=3; Synonyms=Gamma, 1a1;
CC IsoId=Q9JI57-3; Sequence=VSP_003874, VSP_003875, VSP_003876;
CC Name=4; Synonyms=1b1;
CC IsoId=Q9JI57-4; Sequence=VSP_003874, VSP_003875;
CC Name=5; Synonyms=3b5;
CC IsoId=Q9JI57-5; Sequence=VSP_003874;
CC Name=6; Synonyms=3b3;
CC IsoId=Q9JI57-6; Sequence=VSP_021376, VSP_003874;
CC Name=7; Synonyms=3a3;
CC IsoId=Q9JI57-7; Sequence=VSP_021376, VSP_003874, VSP_003876;
CC Name=8; Synonyms=1b4;
CC IsoId=Q9JI57-8; Sequence=VSP_003875;
CC Name=9; Synonyms=2a5;
CC IsoId=Q9JI57-9; Sequence=VSP_021377, VSP_003876;
CC Name=10; Synonyms=1a4;
CC IsoId=Q9JI57-10; Sequence=VSP_003875, VSP_003876;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed in somites, neural tube and brain at 8-
CC 8.5 dpc. Expression remains constant from 9.5-12.5 dpc with highest
CC expression levels in the limb buds, branchial arches, crainofacial
CC area, brain and spinal cord.
CC -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000255|PROSITE-
CC ProRule:PRU00484}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78367.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF260133; AAF78367.1; ALT_FRAME; mRNA.
DR EMBL; AF257475; AAG44655.1; -; mRNA.
DR EMBL; AY030287; AAK49782.1; -; mRNA.
DR EMBL; AY030288; AAK49783.1; -; mRNA.
DR EMBL; AY030289; AAK49784.1; -; mRNA.
DR EMBL; AF247161; AAL68980.1; -; mRNA.
DR EMBL; AF343348; AAM02920.1; -; mRNA.
DR EMBL; AF343349; AAM02921.1; -; mRNA.
DR EMBL; AF343350; AAM02922.1; -; mRNA.
DR EMBL; AF343351; AAM02923.1; -; mRNA.
DR EMBL; AF497637; AAP30728.1; -; mRNA.
DR EMBL; AF497638; AAP30729.1; -; mRNA.
DR EMBL; AF497639; AAP30730.1; -; mRNA.
DR EMBL; AF497640; AAP30731.1; -; mRNA.
DR EMBL; AF497641; AAP30732.1; -; mRNA.
DR EMBL; AF497642; AAP30733.1; -; mRNA.
DR EMBL; AF289666; AAF99337.1; -; Genomic_DNA.
DR EMBL; AF289667; AAF99339.1; -; Genomic_DNA.
DR CCDS; CCDS39302.1; -. [Q9JI57-7]
DR CCDS; CCDS39303.1; -. [Q9JI57-9]
DR CCDS; CCDS39305.1; -. [Q9JI57-2]
DR CCDS; CCDS39306.1; -. [Q9JI57-5]
DR CCDS; CCDS39307.1; -. [Q9JI57-1]
DR CCDS; CCDS51657.1; -. [Q9JI57-8]
DR CCDS; CCDS80420.1; -. [Q9JI57-10]
DR CCDS; CCDS84967.1; -. [Q9JI57-6]
DR RefSeq; NP_001074931.1; NM_001081462.2. [Q9JI57-1]
DR RefSeq; NP_001074932.1; NM_001081463.2. [Q9JI57-5]
DR RefSeq; NP_001074935.1; NM_001081466.2. [Q9JI57-7]
DR RefSeq; NP_001074936.1; NM_001081467.2. [Q9JI57-8]
DR RefSeq; NP_001074938.1; NM_001081469.2. [Q9JI57-10]
DR RefSeq; NP_001074939.1; NM_001081470.2. [Q9JI57-3]
DR RefSeq; NP_001231865.1; NM_001244936.1. [Q9JI57-4]
DR RefSeq; NP_001334417.1; NM_001347488.1. [Q9JI57-6]
DR RefSeq; NP_065064.2; NM_020331.3. [Q9JI57-2]
DR RefSeq; XP_017176527.1; XM_017321038.1. [Q9JI57-1]
DR RefSeq; XP_017176528.1; XM_017321039.1. [Q9JI57-5]
DR AlphaFoldDB; Q9JI57; -.
DR SMR; Q9JI57; -.
DR IntAct; Q9JI57; 2.
DR MINT; Q9JI57; -.
DR STRING; 10090.ENSMUSP00000098217; -.
DR iPTMnet; Q9JI57; -.
DR PhosphoSitePlus; Q9JI57; -.
DR MaxQB; Q9JI57; -.
DR PaxDb; Q9JI57; -.
DR PRIDE; Q9JI57; -.
DR ProteomicsDB; 271358; -. [Q9JI57-1]
DR ProteomicsDB; 271359; -. [Q9JI57-2]
DR ProteomicsDB; 271360; -. [Q9JI57-3]
DR ProteomicsDB; 271361; -. [Q9JI57-4]
DR ProteomicsDB; 271362; -. [Q9JI57-5]
DR ProteomicsDB; 271363; -. [Q9JI57-6]
DR ProteomicsDB; 271364; -. [Q9JI57-7]
DR ProteomicsDB; 271365; -. [Q9JI57-8]
DR ProteomicsDB; 271366; -. [Q9JI57-9]
DR ProteomicsDB; 271367; -. [Q9JI57-10]
DR Antibodypedia; 14624; 394 antibodies from 32 providers.
DR DNASU; 57080; -.
DR Ensembl; ENSMUST00000073161; ENSMUSP00000072904; ENSMUSG00000023079. [Q9JI57-2]
DR Ensembl; ENSMUST00000074114; ENSMUSP00000073752; ENSMUSG00000023079. [Q9JI57-8]
DR Ensembl; ENSMUST00000100650; ENSMUSP00000098215; ENSMUSG00000023079. [Q9JI57-5]
DR Ensembl; ENSMUST00000100652; ENSMUSP00000098217; ENSMUSG00000023079. [Q9JI57-1]
DR Ensembl; ENSMUST00000100654; ENSMUSP00000098219; ENSMUSG00000023079. [Q9JI57-9]
DR Ensembl; ENSMUST00000111245; ENSMUSP00000106876; ENSMUSG00000023079. [Q9JI57-7]
DR Ensembl; ENSMUST00000167084; ENSMUSP00000132882; ENSMUSG00000023079. [Q9JI57-10]
DR Ensembl; ENSMUST00000200944; ENSMUSP00000143848; ENSMUSG00000023079. [Q9JI57-10]
DR Ensembl; ENSMUST00000202554; ENSMUSP00000143809; ENSMUSG00000023079. [Q9JI57-6]
DR GeneID; 57080; -.
DR KEGG; mmu:57080; -.
DR UCSC; uc008zvv.2; mouse. [Q9JI57-2]
DR UCSC; uc008zvw.2; mouse. [Q9JI57-7]
DR UCSC; uc008zvx.2; mouse. [Q9JI57-3]
DR UCSC; uc008zvy.2; mouse. [Q9JI57-10]
DR UCSC; uc008zvz.2; mouse. [Q9JI57-9]
DR UCSC; uc008zwa.2; mouse. [Q9JI57-8]
DR UCSC; uc008zwb.2; mouse. [Q9JI57-6]
DR UCSC; uc008zwc.2; mouse. [Q9JI57-4]
DR UCSC; uc008zwd.2; mouse. [Q9JI57-5]
DR UCSC; uc008zwe.2; mouse. [Q9JI57-1]
DR CTD; 9569; -.
DR MGI; MGI:1861942; Gtf2ird1.
DR VEuPathDB; HostDB:ENSMUSG00000023079; -.
DR eggNOG; ENOG502QPVX; Eukaryota.
DR GeneTree; ENSGT00940000159414; -.
DR HOGENOM; CLU_014412_0_0_1; -.
DR InParanoid; Q9JI57; -.
DR OMA; SNQIPVM; -.
DR OrthoDB; 115381at2759; -.
DR PhylomeDB; Q9JI57; -.
DR TreeFam; TF352524; -.
DR BioGRID-ORCS; 57080; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Gtf2ird1; mouse.
DR PRO; PR:Q9JI57; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JI57; protein.
DR Bgee; ENSMUSG00000023079; Expressed in saccule of membranous labyrinth and 269 other tissues.
DR ExpressionAtlas; Q9JI57; baseline and differential.
DR Genevisible; Q9JI57; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0014886; P:transition between slow and fast fiber; IDA:MGI.
DR Gene3D; 3.90.1460.10; -; 6.
DR InterPro; IPR004212; GTF2I.
DR InterPro; IPR036647; GTF2I-like_rpt_sf.
DR InterPro; IPR016659; TF_II-I.
DR Pfam; PF02946; GTF2I; 6.
DR PIRSF; PIRSF016441; TF_II-I; 1.
DR SUPFAM; SSF117773; SSF117773; 6.
DR PROSITE; PS51139; GTF2I; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1104
FT /note="General transcription factor II-I repeat domain-
FT containing protein 1"
FT /id="PRO_0000083871"
FT REPEAT 119..213
FT /note="GTF2I-like 1"
FT REPEAT 342..436
FT /note="GTF2I-like 2"
FT REPEAT 556..650
FT /note="GTF2I-like 3"
FT REPEAT 681..775
FT /note="GTF2I-like 4"
FT REPEAT 805..899
FT /note="GTF2I-like 5"
FT REPEAT 908..1002
FT /note="GTF2I-like 6"
FT REGION 509..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1012..1019
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 543..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 669
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 717
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 757
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 759
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 841
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT CROSSLNK 901
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHL9"
FT VAR_SEQ 657..675
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12780350"
FT /id="VSP_021376"
FT VAR_SEQ 703..800
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:12780350"
FT /id="VSP_021377"
FT VAR_SEQ 774..800
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11827466,
FT ECO:0000303|PubMed:12780350"
FT /id="VSP_003874"
FT VAR_SEQ 864..966
FT /note="Missing (in isoform 3, isoform 4, isoform 8 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:11827466,
FT ECO:0000303|PubMed:12780350"
FT /id="VSP_003875"
FT VAR_SEQ 1051..1104
FT /note="VKSRGSELHPNSVWPLPLPRAGPSTAPGTGRHWALRGTQPTTEGQAHPLVLP
FT TR -> QWPVYMVDYSGLNVQLPGPLDY (in isoform 1, isoform 3,
FT isoform 7, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10861001,
FT ECO:0000303|PubMed:11827466, ECO:0000303|PubMed:12780350"
FT /id="VSP_003876"
FT CONFLICT 79
FT /note="E -> V (in Ref. 4; AAM02923)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="N -> D (in Ref. 1; AAF78367)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="E -> K (in Ref. 4; AAM02920)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> F (in Ref. 1; AAF78367)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="Y -> H (in Ref. 1; AAF78367)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> L (in Ref. 1; AAF78367)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="D -> G (in Ref. 1; AAF78367)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="K -> R (in Ref. 4; AAL68980)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="L -> F (in Ref. 4; AAM02920/AAP30731)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="H -> Y (in Ref. 4; AAM02923)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="L -> P (in Ref. 4; AAP30733/AAM02922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 123483 MW; C76B2AF3CD1BCD73 CRC64;
MALLGKHCDI PTNGCGSERW NSTFARKDEL INSLVSALDS MCSALSKLNT EVACVAVHNE
SVFVMGTEKG RVFLNTRKEL QSDFLRFCRG PLWNDPEAGH PKKVQRCEGG GRSLPRSSLE
QCSDVYLLQK MVEEVFDVLY SEAMGRATVV PLPYERLLRE PGLLAVQGLP EGLAFRRPAE
YDPKALMAIL EHSHRIRFKL RRPPDDGGQD TKALVEMNGI SLLPKGSRDC GLHGQASKVA
PQDLTPTATP SSMANFLYST SMPNHTIREL KQEVPTCPLT PSDLGMGWPV PEPHVPSTQD
FSDCCGQTPA GPAGPLIQNV HASKRILFSI VHDKSEKWDP FIKEMEDINT LRECVQILFN
SRYAEALGLD HMVPVPYRKI ACDPEAVEIV GIPDKIPFKR PCTYGVPKLK RILEERHSIH
FIIKRMFDER IFTGNKFTKD PMKLEPASPP EDTSTEVCRD SMLDLAGTAW SDMSSVSEDC
GPGTSGEIAM LRPIKIEPEE LDIIQVTVSD PSPTSEEMTD SLPGHLPSED SGYGMEMPAD
KGPSEEPWSE ERPAEESPGD VIRPLRKQVE MLFNTKYAKA IGTSEPVKVP YSKFLMHPEE
LFVLGLPEGI SLRRPNCFGI AKLRKILEAS NSIQFVIKRP ELLTDGVKEP VLDTQERDSW
DRLVDETPKR QGLQENYNTR LSRIDIANTL REQVQDLFNK KYGEALGIKY PVQVPYKRIK
SNPGSVIIEG LPPGIPFRKP CTFGSQNLER ILSVADKIKF TVTRPFQGLI PKPETKILTT
GHEAGKTTRP RRLQQDTWQP DEDDANRLGE KVILREQVKE LFNEKYGEAL GLNRPVLVPY
KLIRDSPDAV EVKGLPDDIP FRNPNTYDIH RLEKILKARE HVRMVIINQL QPFAEVCNDP
KVPEEDDSNK LGKKVILREQ VKELFNEKYG EALGLNRPVL VPYKLIRDSP DAVEVKGLPD
DIPFRNPNTY DIHRLEKILK AREHVRMVII NQLQPFGDVC NNAKVPAKDN IPKRKRKRVS
EGNSVSSSSS SSSSSSNPES VASTNQISLV VKSRGSELHP NSVWPLPLPR AGPSTAPGTG
RHWALRGTQP TTEGQAHPLV LPTR
