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TBX1_HUMAN
ID   TBX1_HUMAN              Reviewed;         398 AA.
AC   O43435; C6G493; C6G494; O43436; Q96RJ2;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=T-box transcription factor TBX1;
DE            Short=T-box protein 1;
DE   AltName: Full=Testis-specific T-box protein;
GN   Name=TBX1;
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 [MRNA] (ISOFORMS A AND B).
RC   TISSUE=Skeletal muscle, and Testis;
RX   PubMed=9268629; DOI=10.1006/geno.1997.4829;
RA   Chieffo C., Garvey N., Gong W., Roe B., Zhang G., Silver L., Emanuel B.S.,
RA   Budarf M.L.;
RT   "Isolation and characterization of a gene from the DiGeorge chromosomal
RT   region homologous to the mouse Tbx1 gene.";
RL   Genomics 43:267-277(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RA   Gong W., Gottlieb S., Budarf M.L.;
RT   "Mutation analysis of TBX1 in 105 patients.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=11111039; DOI=10.1016/s0378-1119(00)00417-0;
RA   Sinha S., Abraham S., Gronostajski R.M., Campbell C.E.;
RT   "Differential DNA binding and transcription modulation by three T-box
RT   proteins, T, TBX1 and TBX2.";
RL   Gene 258:15-29(2000).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [7]
RP   VARIANT CTMH/VCFS TYR-148, AND VARIANT DGS SER-310.
RX   PubMed=14585638; DOI=10.1016/s0140-6736(03)14632-6;
RA   Yagi H., Furutani Y., Hamada H., Sasaki T., Asakawa S., Minoshima S.,
RA   Ichida F., Joo K., Kimura M., Imamura S., Kamatani N., Momma K., Takao A.,
RA   Nakazawa M., Shimizu N., Matsuoka R.;
RT   "Role of TBX1 in human del22q11.2 syndrome.";
RL   Lancet 362:1366-1373(2003).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-337.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [9]
RP   VARIANT VCFS GLN-194.
RX   PubMed=17273972; DOI=10.1086/511993;
RA   Zweier C., Sticht H., Aydin-Yaylagul I., Campbell C.E., Rauch A.;
RT   "Human TBX1 missense mutations cause gain of function resulting in the same
RT   phenotype as 22q11.2 deletions.";
RL   Am. J. Hum. Genet. 80:510-517(2007).
CC   -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC       processes (By similarity). Binds to the palindromic T site 5'-
CC       TTCACACCTAGGTGTGAA-3' DNA sequence (PubMed:11111039). Is required for
CC       normal development of the pharyngeal arch arteries (By similarity).
CC       {ECO:0000250|UniProtKB:P70323, ECO:0000269|PubMed:11111039}.
CC   -!- SUBUNIT: Binds DNA as a dimer (PubMed:11111039). Interacts with DSCR6
CC       (By similarity). {ECO:0000250|UniProtKB:P70323,
CC       ECO:0000269|PubMed:11111039}.
CC   -!- INTERACTION:
CC       O43435; P57055: RIPPLY3; NbExp=2; IntAct=EBI-21460353, EBI-12092053;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=O43435-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=O43435-2; Sequence=VSP_006383;
CC       Name=C; Synonyms=TBX1C;
CC         IsoId=O43435-3; Sequence=VSP_007423;
CC   -!- DISEASE: Note=Haploinsufficiency of the TBX1 gene is responsible for
CC       most of the physical malformations present in DiGeorge syndrome (DGS)
CC       and velocardiofacial syndrome (VCFS). DGS is characterized by the
CC       association of several malformations: hypoplastic thymus and
CC       parathyroid glands, congenital conotruncal cardiopathy, and a subtle
CC       but characteristic facial dysmorphology. VCFS is marked by the
CC       association of congenital conotruncal heart defects, cleft palate or
CC       velar insufficiency, facial dysmorpholgy and learning difficulties. It
CC       is now accepted that these two syndromes represent two forms of
CC       clinical expression of the same entity manifesting at different stages
CC       of life.
CC   -!- DISEASE: DiGeorge syndrome (DGS) [MIM:188400]: A congenital syndrome
CC       characterized by a wide spectrum of characteristics including
CC       parathyroid hypoplasia resulting in hypocalcemia, thymic hypoplasia
CC       resulting in T-cell immunodeficiency, defects in the outflow tract of
CC       the heart, and craniofacial anomalies. Disturbance of cervical neural
CC       crest migration into the derivatives of the pharyngeal arches and
CC       pouches can account for the phenotype. {ECO:0000269|PubMed:14585638}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Velocardiofacial syndrome (VCFS) [MIM:192430]: A syndrome
CC       characterized by abnormal pharyngeal arch development that results in
CC       defective development of the parathyroid glands, thymus, and
CC       conotruncal region of the heart. The phenotype is highly variable, with
CC       no single clinical feature present in every patient. Affected
CC       individuals may present with structural or functional palatal
CC       abnormalities, cardiac defects, unique facial characteristics,
CC       hypernasal speech, hypotonia, and defective thymic development
CC       associated with impaired immune function. In addition, affected
CC       individuals may present with learning disabilities, overt developmental
CC       delay, and psychiatric disorders. {ECO:0000269|PubMed:14585638,
CC       ECO:0000269|PubMed:17273972}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A group
CC       of congenital heart defects involving the outflow tracts. Examples
CC       include truncus arteriosus communis, double-outlet right ventricle and
CC       transposition of great arteries. Truncus arteriosus communis is
CC       characterized by a single outflow tract instead of a separate aorta and
CC       pulmonary artery. In transposition of the great arteries, the aorta
CC       arises from the right ventricle and the pulmonary artery from the left
CC       ventricle. In double outlet of the right ventricle, both the pulmonary
CC       artery and aorta arise from the right ventricle. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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DR   EMBL; AF012130; AAB94018.1; -; mRNA.
DR   EMBL; AF012131; AAB94019.1; -; mRNA.
DR   EMBL; AF373867; AAK58955.1; -; mRNA.
DR   EMBL; FJ515849; ACS13741.1; -; Genomic_DNA.
DR   EMBL; FJ515849; ACS13742.1; -; Genomic_DNA.
DR   EMBL; CH471176; EAX03024.1; -; Genomic_DNA.
DR   EMBL; CH471176; EAX03025.1; -; Genomic_DNA.
DR   CCDS; CCDS13765.1; -. [O43435-2]
DR   CCDS; CCDS13766.1; -. [O43435-1]
DR   CCDS; CCDS13767.1; -. [O43435-3]
DR   RefSeq; NP_005983.1; NM_005992.1. [O43435-2]
DR   RefSeq; NP_542377.1; NM_080646.1. [O43435-1]
DR   RefSeq; NP_542378.1; NM_080647.1. [O43435-3]
DR   RefSeq; XP_006724375.1; XM_006724312.2. [O43435-3]
DR   RefSeq; XP_016884415.1; XM_017028926.1. [O43435-3]
DR   PDB; 4A04; X-ray; 2.58 A; A/B=109-297.
DR   PDBsum; 4A04; -.
DR   AlphaFoldDB; O43435; -.
DR   SMR; O43435; -.
DR   BioGRID; 112762; 6.
DR   IntAct; O43435; 1.
DR   STRING; 9606.ENSP00000331791; -.
DR   iPTMnet; O43435; -.
DR   PhosphoSitePlus; O43435; -.
DR   BioMuta; TBX1; -.
DR   jPOST; O43435; -.
DR   MassIVE; O43435; -.
DR   MaxQB; O43435; -.
DR   PeptideAtlas; O43435; -.
DR   PRIDE; O43435; -.
DR   ProteomicsDB; 48946; -. [O43435-1]
DR   ProteomicsDB; 48947; -. [O43435-2]
DR   ProteomicsDB; 48948; -. [O43435-3]
DR   Antibodypedia; 22982; 322 antibodies from 32 providers.
DR   DNASU; 6899; -.
DR   Ensembl; ENST00000329705.11; ENSP00000331176.7; ENSG00000184058.15. [O43435-1]
DR   Ensembl; ENST00000332710.8; ENSP00000331791.4; ENSG00000184058.15. [O43435-3]
DR   Ensembl; ENST00000359500.7; ENSP00000352483.3; ENSG00000184058.15. [O43435-2]
DR   GeneID; 6899; -.
DR   KEGG; hsa:6899; -.
DR   UCSC; uc002zqa.2; human. [O43435-1]
DR   CTD; 6899; -.
DR   DisGeNET; 6899; -.
DR   GeneCards; TBX1; -.
DR   GeneReviews; TBX1; -.
DR   HGNC; HGNC:11592; TBX1.
DR   HPA; ENSG00000184058; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; TBX1; -.
DR   MIM; 188400; phenotype.
DR   MIM; 192430; phenotype.
DR   MIM; 217095; phenotype.
DR   MIM; 602054; gene.
DR   neXtProt; NX_O43435; -.
DR   OpenTargets; ENSG00000184058; -.
DR   Orphanet; 567; 22q11.2 deletion syndrome.
DR   Orphanet; 1727; 22q11.2 duplication syndrome.
DR   Orphanet; 3303; Tetralogy of Fallot.
DR   PharmGKB; PA36355; -.
DR   VEuPathDB; HostDB:ENSG00000184058; -.
DR   eggNOG; KOG3586; Eukaryota.
DR   GeneTree; ENSGT00940000154816; -.
DR   HOGENOM; CLU_014430_9_1_1; -.
DR   InParanoid; O43435; -.
DR   OMA; HNHSSFK; -.
DR   OrthoDB; 1185429at2759; -.
DR   PhylomeDB; O43435; -.
DR   TreeFam; TF106341; -.
DR   PathwayCommons; O43435; -.
DR   SignaLink; O43435; -.
DR   SIGNOR; O43435; -.
DR   BioGRID-ORCS; 6899; 22 hits in 1102 CRISPR screens.
DR   ChiTaRS; TBX1; human.
DR   GenomeRNAi; 6899; -.
DR   Pharos; O43435; Tbio.
DR   PRO; PR:O43435; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; O43435; protein.
DR   Bgee; ENSG00000184058; Expressed in hindlimb stylopod muscle and 160 other tissues.
DR   ExpressionAtlas; O43435; baseline and differential.
DR   Genevisible; O43435; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046983; F:protein dimerization activity; TAS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR   GO; GO:0035909; P:aorta morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048844; P:artery morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR   GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR   GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR   GO; GO:0042471; P:ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:UniProtKB.
DR   GO; GO:0070166; P:enamel mineralization; ISS:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060325; P:face morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR   GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001945; P:lymph vessel development; ISS:UniProtKB.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0007498; P:mesoderm development; ISS:UniProtKB.
DR   GO; GO:0042474; P:middle ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0042693; P:muscle cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR   GO; GO:0048644; P:muscle organ morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060415; P:muscle tissue morphogenesis; ISS:UniProtKB.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
DR   GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:UniProtKB.
DR   GO; GO:0042473; P:outer ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:UniProtKB.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060017; P:parathyroid gland development; IMP:UniProtKB.
DR   GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
DR   GO; GO:0060037; P:pharyngeal system development; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:2001037; P:positive regulation of tongue muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:2000027; P:regulation of animal organ morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048752; P:semicircular canal morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR   GO; GO:0060023; P:soft palate development; IMP:UniProtKB.
DR   GO; GO:0048538; P:thymus development; IMP:UniProtKB.
DR   GO; GO:0030878; P:thyroid gland development; ISS:UniProtKB.
DR   GO; GO:0043587; P:tongue morphogenesis; ISS:UniProtKB.
DR   GO; GO:0021644; P:vagus nerve morphogenesis; ISS:UniProtKB.
DR   CDD; cd00182; TBOX; 1.
DR   Gene3D; 2.60.40.820; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR046360; T-box_DNA-bd.
DR   InterPro; IPR036960; T-box_sf.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   PANTHER; PTHR11267; PTHR11267; 1.
DR   Pfam; PF00907; T-box; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   PROSITE; PS01283; TBOX_1; 1.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Disease variant;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..398
FT                   /note="T-box transcription factor TBX1"
FT                   /id="PRO_0000184423"
FT   DNA_BIND        119..297
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          23..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         337..398
FT                   /note="GGHVLKDKEVKAETSRNTPEREVELLRDAGGCVNLGLPCPAECQPFNTQGLV
FT                   AGRTAGDRLC -> DAAEARREFQRDAGGPAVLGDPAHPPQLLARVLSPSLPGAGGAGG
FT                   LVPLPGAPGGRPSPPNPELRLEAPGASEPLHHHPYKYPAAAYDHYLGAKSRPAPYPLPG
FT                   LRGHGYHPHAHPHHHHHPVSPAAAAAAAAAAAAAAANMYSSAGAAPPGSYDYCPR (in
FT                   isoform C)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_007423"
FT   VAR_SEQ         338..398
FT                   /note="GHVLKDKEVKAETSRNTPEREVELLRDAGGCVNLGLPCPAECQPFNTQGLVA
FT                   GRTAGDRLC -> LVTEGSGLQPGLLDVLLKPPSKKSESLRPPHCKDT (in
FT                   isoform B)"
FT                   /evidence="ECO:0000303|PubMed:9268629"
FT                   /id="VSP_006383"
FT   VARIANT         148
FT                   /note="F -> Y (in CTHM and VCFS; dbSNP:rs28939675)"
FT                   /evidence="ECO:0000269|PubMed:14585638"
FT                   /id="VAR_035025"
FT   VARIANT         194
FT                   /note="H -> Q (in VCFS; dbSNP:rs74315522)"
FT                   /evidence="ECO:0000269|PubMed:17273972"
FT                   /id="VAR_035026"
FT   VARIANT         310
FT                   /note="G -> S (in DGS; dbSNP:rs41298838)"
FT                   /evidence="ECO:0000269|PubMed:14585638"
FT                   /id="VAR_034545"
FT   VARIANT         337
FT                   /note="G -> E (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036065"
FT   VARIANT         350
FT                   /note="T -> M (in dbSNP:rs4819522)"
FT                   /id="VAR_024657"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   HELIX           117..126
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          154..165
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          167..173
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   TURN            174..177
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   HELIX           203..208
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          236..245
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          260..264
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   STRAND          270..275
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   HELIX           279..288
FT                   /evidence="ECO:0007829|PDB:4A04"
FT   HELIX           290..295
FT                   /evidence="ECO:0007829|PDB:4A04"
SQ   SEQUENCE   398 AA;  43133 MW;  FAF0F3FA0CDC6176 CRC64;
     MHFSTVTRDM EAFTASSLSS LGAAGGFPGA ASPGADPYGP REPPPPPPRY DPCAAAAPGA
     PGPPPPPHAY PFAPAAGAAT SAAAEPEGPG ASCAAAAKAP VKKNAKVAGV SVQLEMKALW
     DEFNQLGTEM IVTKAGRRMF PTFQVKLFGM DPMADYMLLM DFVPVDDKRY RYAFHSSSWL
     VAGKADPATP GRVHYHPDSP AKGAQWMKQI VSFDKLKLTN NLLDDNGHII LNSMHRYQPR
     FHVVYVDPRK DSEKYAEENF KTFVFEETRF TAVTAYQNHR ITQLKIASNP FAKGFRDCDP
     EDWPRNHRPG ALPLMSAFAR SRNPVASPTQ PSGTEKGGHV LKDKEVKAET SRNTPEREVE
     LLRDAGGCVN LGLPCPAECQ PFNTQGLVAG RTAGDRLC
 
 
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