ID   TSH1B_XENLA             Reviewed;        1077 AA.
AC   Q2HNT1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Teashirt homolog 1-B;
DE   AltName: Full=Teashirt 1B;
GN   Name=tshz1-b; Synonyms=tsh1, Xtsh1b;
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 DEVELOPMENTAL STAGE.
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.
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       {ECO:0000269|PubMed:16916510}.
CC   -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY854807; AAX48759.1; -; mRNA.
DR   RefSeq; NP_001165937.1; NM_001172466.1.
DR   AlphaFoldDB; Q2HNT1; -.
DR   SMR; Q2HNT1; -.
DR   PRIDE; Q2HNT1; -.
DR   GeneID; 100379091; -.
DR   KEGG; xla:100379091; -.
DR   CTD; 100379091; -.
DR   Xenbase; XB-GENE-6461981; tshz1.L.
DR   OrthoDB; 106971at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 100379091; Expressed in pancreas and 14 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; IPR036236; Znf_C2H2_sf.
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   SUPFAM; SSF57667; SSF57667; 1.
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..1077
FT                   /note="Teashirt homolog 1-B"
FT                   /id="PRO_0000399475"
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         1037..1060
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          142..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..75
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..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1077 AA;  118795 MW;  54A74697776477D0 CRC64;
     MPRRKQQAPR RSAAYVPAEE LKAAETEEDN LEDDGLSLDV QDSEYLYNDE HEIKETQSYQ
     NSPISSATNP DAGYGSPFSE ASDHLADFKS TSSKEGQDKE DGQSTENASY PTDSLAQIKA
     VYTNLLSECC WSNLALDLKK SNEKASPTTN TDKSSKSEAS GPTSDPGTPT TITSSSCTNT
     STSICVTTSN SAISNTASGY DWHQAALAKT LQQTSYGLLP EPSLFSTVQL YRQSNKLYGS
     VFTGASKFRC KDCSAAYDTL VELTVHMNET GHYRDDNRDR EAERTKRWSK PRKRSLMEME
     GKEDAQKVLK CMYCGHSFES LQDLSVHMIK TKHYQKVPLK EPVPAITKLV PSTKKRALQD
     IALPDSPEQA GISPGASVSE SAKDPKAANP YVTPNNRYGY QNGASYTWQF EARKAQILKC
     MECGSSHDTL QQLTAHMMVT GHFLKVTNSA SKKGKQLVMD AVLEEKIQSI PLPPTTHARL
     PATYIKKPPD SPTGSTHSEE KKDPEKEKVN IGEVEKKIKE ENEDPEKIEP ATLYQYLREE
     DLDDSPKGGL DILKSLENTV SSAISKAQNG APSWGGYPSI HAAYQLPGTI KALQPSVQSV
     QIQPSYASSV KTMSSDHNAL IHSPGSLTPP PHKSNVSAME ELVEKVTGKI NVKKEEKVLE
     KEKVISAKPP SPMAKENKEI LKPEEANSKT LKKHNEAEIQ KPKKETPIES HALNGTEPLK
     AKVTNGCTSL GIITDHSPEQ SFINPLSALQ SIMNTHLGKV SKPVSPSLDP LAMLYKISNS
     MLDKPIYPTT PMKQVESIDR YYYEDSDQPI DLTKSKNKPL VTSITDPVSS PLRESALMDI
     SDMVKNLTGR LTPKSSTPST VSEKSDADGS SFEEALDELS PVHKRKGRQS NWNPQHLLIL
     QAQFASSLRE TAEGKYIMSD LGPQERVHIS KFTGLSMTTI SHWLANVKYQ LRRTGGTKFL
     KNLDTGHPVF FCNDCASQFR TASTYIGHLE THLGFSLKDL SKLSLNQIQE QQNVTKVITN
     KALSSVGLIE EDSGSTFQCK LCNRTFASKH AVKLHLSKTH GKSPEDHVIY VTELEKQ