ID   TSH1A_XENLA             Reviewed;        1078 AA.
AC   Q2HNT2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Teashirt homolog 1-A;
DE   AltName: Full=Teashirt 1A;
GN   Name=tshz1-a; Synonyms=tsh1, Xtsh1a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=16916510; DOI=10.1016/j.ydbio.2006.06.041;
RA   Koebernick K., Kashef J., Pieler T., Wedlich D.;
RT   "Xenopus Teashirt1 regulates posterior identity in brain and cranial neural
RT   crest.";
RL   Dev. Biol. 298:312-326(2006).
CC   -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC       processes. May act as a transcriptional repressor (Potential). Involved
CC       in two major neuronal regionalization processes: primary
CC       anteroposterior (AP) axis patterning of the CNS and segmentation of the
CC       cranial neuronal crest (CNS) development. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16916510}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in early blastula stage embryos with a
CC       decrease during gastrulation. Expressed at early neurula stage in two
CC       broad wedge-shaped domains within the neuroectoderm flanking the
CC       midline. Throughout neurula stages, the anterior limit of its
CC       expression is maintained at a position posterior to hindbrain
CC       rhombomere 5. Confined to the trunk region of the prospective CNS. At
CC       stage 26, expressed in a gradient spanning the presumptive
CC       hindbrain/spinal cord boundary, the diencephalon, the pronephros and
CC       the presumptive olfactory placodes. From late neurula stage on, its
CC       expression becomes detectable in a distinct population of emigrating
CC       cranial neural crest (CNC) cells of the third branchial arch. At stage
CC       26, expressed in the entire hyoid and branchial arch region and
CC       strongly reduced in this domain at tailbud stage.
CC   -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY854806; AAX48758.1; -; mRNA.
DR   RefSeq; NP_001165936.1; NM_001172465.1.
DR   AlphaFoldDB; Q2HNT2; -.
DR   SMR; Q2HNT2; -.
DR   GeneID; 100379090; -.
DR   KEGG; xla:100379090; -.
DR   CTD; 100379090; -.
DR   Xenbase; XB-GENE-6465500; tshz1.S.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 100379090; Expressed in neurula embryo and 18 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR027008; Teashirt_fam.
DR   InterPro; IPR026808; Tshz1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12487; PTHR12487; 1.
DR   PANTHER; PTHR12487:SF6; PTHR12487:SF6; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Homeobox; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1078
FT                   /note="Teashirt homolog 1-A"
FT                   /id="PRO_0000399474"
FT   ZN_FING         248..272
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         309..333
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         418..442
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   DNA_BIND        885..955
FT                   /note="Homeobox"
FT   ZN_FING         970..992
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1038..1061
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1078 AA;  119161 MW;  D37A011FE1EBAFFE CRC64;
     MPRRKQQAPR RSAAYVPEEE LKAADIEEDN LEDDGLSLDV QDSEYLYNDE HEIKETPSYQ
     NSPISSATNQ DAGYGSPFSE TSDHLADFKS TSSKEGQDKE DGQNTENVSY PTDSLAQIKA
     VYTNLLSECC WSNLALDLKK SNENSSPTTN TNKSSMSEAT GSTSDPDTPT TIPSSSCTNT
     STSISVTTSN STNSNSASGY DWHQAALAKT LQQTSYGLLP EPSLFSTVQL YRQSNKIYGS
     VFTGASRFKC KDCSAAYDTL VELTVHMNET GHYRDDNKDR DAERTKRWSK PRKRSLMEME
     GKEDAQKVLK CMYCGHSFES LQDLSVHMIK TKHYQKVPLK EPVPAITKLI PSTKKRALQD
     IALPDSPEQA GISPGASVSE SAKDPKAANP YVTPNNRYGY QNGASYTWQF EARKAQILKC
     MECGSSHDSL QQLTAHMMVT GHFLKVTNSA SKKGKQLVMD AVIEEKIQSI PLPPTTHARL
     PGSYIKKQPD SPTGSTHSEE KKDPEKEKVN NCEVEKRIKE ENEDPEKIEP ATLYQYLREE
     DLDTSPKGGL DILKSLENTV SSAISKAQNG APSWGGYPSI HAAYQLPGTV KALQPSVQSV
     QIQPSYAISV KTMTPDHNSL IHSPGSLTPP THRSNVSAME ELVEKVTGKI NIKKEEKVLE
     KEMVIPAKPP SPVAKENKEI LKAEEANGKV LKKSNEADIQ KPKKETPIEP HALNGTEPLK
     AKVTNGCSSL GIITDHSPEP SFINPLSALQ SIMNTHLGKV SKPVSPSLDP LAMLYKISNS
     MLDKPIYPTT PVKQVESIER YYYEDSDQPI DLTKSKNKPF VTSITDHVSS PLRESALMDI
     SDMVKNLTGR LTPKSSTPST VSEKSDADGS SFEEAMDELS PVHKRKGRQS NWNPQHLLIL
     QAQFASSLRE TAEGKYIMSD LGPQERVNIS KFTGLSMTTI SHWLANVKYQ LRRTGGTKFL
     KNLDTGHPVF FCNDCASQFR TASTYIGHLE THLGFSLKDL SKHSLNRIQE QQNVTKVITN
     KALSSVGGLI EEDSSSTFQC KLCNRTFASK HAVKLHLSKT HGKSPEDHVI YVTELRKQ