TSH1_MOUSE
ID TSH1_MOUSE Reviewed; 1084 AA.
AC Q5DTH5; Q6PE60; Q8VD19; Q9JLD5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Teashirt homolog 1;
DE AltName: Full=Serologically defined colon cancer antigen 3 homolog;
GN Name=Tshz1; Synonyms=Kiaa4206, Sdccag33, Tsh1;
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 [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-1084.
RC TISSUE=Limb bud;
RX PubMed=10704881; DOI=10.1016/s0925-4773(99)00318-4;
RA Caubit X., Core N., Boned A., Kerridge S., Djabali M., Fasano L.;
RT "Vertebrate orthologues of the Drosophila region-specific patterning gene
RT teashirt.";
RL Mech. Dev. 91:445-448(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-1084.
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP POSSIBLE FUNCTION.
RX PubMed=14973285; DOI=10.1242/dev.00977;
RA Manfroid I., Caubit X., Kerridge S., Fasano L.;
RT "Three putative murine Teashirt orthologues specify trunk structures in
RT Drosophila in the same way as the Drosophila teashirt gene.";
RL Development 131:1065-1073(2004).
RN [5]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17586487; DOI=10.1016/j.ydbio.2007.05.038;
RA Core N., Caubit X., Metchat A., Boned A., Djabali M., Fasano L.;
RT "Tshz1 is required for axial skeleton, soft palate and middle ear
RT development in mice.";
RL Dev. Biol. 308:407-420(2007).
RN [6]
RP INTERACTION WITH APBB1.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric junction
RT obstruction.";
RL Nephrol. Dial. Transplant. 25:54-60(2010).
CC -!- FUNCTION: Probable transcriptional regulator involved in developmental
CC processes. May act as a transcriptional repressor (Potential).
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID domain 1).
CC {ECO:0000269|PubMed:19343227}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: From 12.5 dpc, expressed in the mesenchyme of the
CC developing middle ear, within areas surrounding the condensing malleus
CC and tympanic ring and on both sides of the external acoustic meatus. At
CC 12.5 dpc, borders and surrounds the future cartilages, but excluded
CC from cartilaginous condensations. Not detected in mesenchymal cells in
CC proximal ureters at 14 dpc. {ECO:0000269|PubMed:17586487,
CC ECO:0000269|PubMed:19745106}.
CC -!- DISRUPTION PHENOTYPE: Normal Mendelian ratio at birth, but none of the
CC mutant animals survive beyond P0. Newborn mutant mice exhibit a strong
CC defect of the soft palate, vertebral malformations in the cervical and
CC thoracic regions of the axial skeleton and malformations in the middle
CC ear components. {ECO:0000269|PubMed:17586487}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63158.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH58264.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220545; BAD90534.1; ALT_INIT; mRNA.
DR EMBL; AF191309; AAF63158.1; ALT_FRAME; mRNA.
DR EMBL; BC017636; AAH17636.1; -; mRNA.
DR EMBL; BC058264; AAH58264.1; ALT_INIT; mRNA.
DR CCDS; CCDS37876.1; -.
DR RefSeq; NP_001074769.1; NM_001081300.1.
DR AlphaFoldDB; Q5DTH5; -.
DR SMR; Q5DTH5; -.
DR STRING; 10090.ENSMUSP00000089388; -.
DR iPTMnet; Q5DTH5; -.
DR PhosphoSitePlus; Q5DTH5; -.
DR jPOST; Q5DTH5; -.
DR MaxQB; Q5DTH5; -.
DR PaxDb; Q5DTH5; -.
DR PeptideAtlas; Q5DTH5; -.
DR PRIDE; Q5DTH5; -.
DR ProteomicsDB; 297661; -.
DR Antibodypedia; 1827; 194 antibodies from 30 providers.
DR Ensembl; ENSMUST00000060303; ENSMUSP00000089388; ENSMUSG00000046982.
DR GeneID; 110796; -.
DR KEGG; mmu:110796; -.
DR UCSC; uc008ful.1; mouse.
DR CTD; 10194; -.
DR MGI; MGI:1346031; Tshz1.
DR VEuPathDB; HostDB:ENSMUSG00000046982; -.
DR eggNOG; ENOG502RJS7; Eukaryota.
DR GeneTree; ENSGT00950000183051; -.
DR HOGENOM; CLU_010469_0_0_1; -.
DR InParanoid; Q5DTH5; -.
DR OMA; TNQEAGY; -.
DR OrthoDB; 106971at2759; -.
DR PhylomeDB; Q5DTH5; -.
DR TreeFam; TF328447; -.
DR BioGRID-ORCS; 110796; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tshz1; mouse.
DR PRO; PR:Q5DTH5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q5DTH5; protein.
DR Bgee; ENSMUSG00000046982; Expressed in rostral migratory stream and 287 other tissues.
DR ExpressionAtlas; Q5DTH5; baseline and differential.
DR Genevisible; Q5DTH5; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060023; P:soft palate development; IMP:MGI.
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 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1084
FT /note="Teashirt homolog 1"
FT /id="PRO_0000047063"
FT ZN_FING 246..270
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..331
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..440
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 891..961
FT /note="Homeobox; atypical"
FT ZN_FING 976..998
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1044..1067
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 49..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSZ6"
FT CONFLICT 31
FT /note="A -> S (in Ref. 2; AAF63158)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="N -> S (in Ref. 2; AAF63158)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="G -> A (in Ref. 2; AAF63158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1084 AA; 118567 MW; 22EB9A9132E62DC8 CRC64;
MPRRKQQAPR RSAAYVPEEE LKAAEIDEEH AEDGGLSLDI QESEFACNEE TEIKEAQSYQ
NSPVSTATNQ DAGYGSPFSE GSDQLAHFKS SSSREEKEES QCPDSVSYPQ DSLAQIKAVY
ANLFSESCWS SLALDLKKSN SATSNNDASQ KESSTPTPTP PTSTASTACT TATTAITSCS
TSTSHSSTTS NSSSSGYDWH QAALAKTLQQ TSSYGLLPEP SLFSTVQLYR QNNKLYGSVF
TGASKFRCKD CSAAYDTLVE LTVHMNETGH YRDDNRDKDS EKTKRWSKPR KRSLMEMEGK
EDAQKVLKCM YCGHSFESLQ DLSVHMIKTK HYQKVPLKEP VPAITKLVPS TKKRALQDLA
SPCSPEPTGV ATEVALSESA KDQKTANPYV TPNNRYGYQN GASYTWQFEA RKAQILKCME
CGSSHDTLQQ LTAHMMVTGH FLKVTTSASK KGKQLVLDPV VEEKIQSIPL PPTTHTRLPA
SSIKKQPDSP AGSVASEEKK EPEKEKEKEK APPAAGDAER KIKEETEDAT EKFEPTALYQ
YLREEDLDDS PKGGVDILKS LENTVSTAIS KAQNGAPSWG GYPSIHAAYQ LPGTVKPLQS
AVQSVQIQPS YASSVKSLSS TEHNALLHSP GSLTPPPHKS NVSAMEELVE KVTGKVSIKK
EERPTEKEKS SPVKAISPVA KENKDLPKTE ETGSKPQKKG SDSETGKAKK ESTLDAHTPN
GTEPLKAKVT NGCGHLGIIT DHSPEPSFIN PLSALQSIMN THLGKVSKPV SPSLDPLAML
YKISNSMLDK PVYPTTPAKQ ADAIDRYYYE NSDQPIDLTK SKNKPLVSGV ADAVSSPLRE
SALMDISDMV KNLTGRLTPK SSTPSTVSEK SDADGSSFEE ALDELSPVHK RKGRQSNWNP
QHLLILQAQF ASSLRETAEG KYIMSDLGPQ ERVHISKFTG LSMTTISHWL ANVKYQLRRT
GGTKFLKNLD TGHPVFFCND CASQFRTAST YVSHLETHLG FSLKDLSKLP LSQIQEQQSV
VSKALTNKTL GPLGSSEEDL GSTFQCKLCN RTFASKHAVK LHLSKTHGKS PEDHLIYVTE
LEKQ
