ID   TSH3_RAT                Reviewed;        1072 AA.
AC   D3ZKB9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   08-NOV-2023, entry version 85.
DE   RecName: Full=Teashirt homolog 3;
DE   AltName: Full=Zinc finger protein 537;
GN   Name=Tshz3; Synonyms=Zfp537;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   INTERACTION WITH APBB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC   -!- FUNCTION: Transcriptional regulator involved in developmental
CC       processes. Functions in association with APBB1, SET and HDAC factors as
CC       a transcriptional repressor, that inhibits the expression of CASP4.
CC       TSHZ3-mediated transcription repression involves the recruitment of
CC       histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a
CC       region surrounding the CASP4 transcriptional start site(s). Regulates
CC       the development of neurons involved in both respiratory rhythm and
CC       airflow control. Promotes maintenance of nucleus ambiguus (nA)
CC       motoneurons, which govern upper airway function, and establishes a
CC       respiratory rhythm generator (RRG) activity compatible with survival at
CC       birth. Involved in the differentiation of the proximal uretic smooth
CC       muscle cells during developmental processes. Involved in the up-
CC       regulation of myocardin, that directs the expression of smooth muscle
CC       cells in the proximal ureter (By similarity). Involved in the
CC       modulation of glutamatergic synaptic transmission and long-term
CC       synaptic potentiation (By similarity). {ECO:0000250|UniProtKB:Q8CGV9}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with HDAC1 and HDAC2; the
CC       interaction is direct. Found in a trimeric complex with APBB1 and
CC       HDAC1; the interaction between HDAC1 and APBB1 is mediated by TSHZ3 (By
CC       similarity). Interacts (via homeobox domain) with APBB1 (via PID domain
CC       1). {ECO:0000250, ECO:0000269|PubMed:19343227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:19343227}. Cell projection, growth cone
CC       {ECO:0000269|PubMed:19343227}. Note=Colocalizes with APBB1 in the
CC       nucleus (By similarity). Colocalizes with APBB1 in axonal growth cone.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in cortical neurons.
CC       {ECO:0000269|PubMed:19343227}.
CC   -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDM07600.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's first breath - Issue
CC       122 of October 2010;
CC       URL="https://web.expasy.org/spotlight/back_issues/122";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH473979; EDM07600.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_001100976.1; NM_001107506.1.
DR   AlphaFoldDB; D3ZKB9; -.
DR   SMR; D3ZKB9; -.
DR   STRING; 10116.ENSRNOP00000018931; -.
DR   PhosphoSitePlus; D3ZKB9; -.
DR   PaxDb; 10116-ENSRNOP00000018931; -.
DR   GeneID; 308523; -.
DR   KEGG; rno:308523; -.
DR   UCSC; RGD:1306322; rat.
DR   AGR; RGD:1306322; -.
DR   CTD; 57616; -.
DR   RGD; 1306322; Tshz3.
DR   eggNOG; ENOG502RJS7; Eukaryota.
DR   InParanoid; D3ZKB9; -.
DR   OrthoDB; 5407068at2759; -.
DR   PhylomeDB; D3ZKB9; -.
DR   TreeFam; TF328447; -.
DR   PRO; PR:D3ZKB9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Proteomes; UP000234681; Chromosome 1.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0060993; P:kidney morphogenesis; ISO:RGD.
DR   GO; GO:0072195; P:kidney smooth muscle cell differentiation; ISO:RGD.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0001656; P:metanephros development; ISO:RGD.
DR   GO; GO:0050881; P:musculoskeletal movement; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:RGD.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0050975; P:sensory perception of touch; ISO:RGD.
DR   GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR   GO; GO:0072193; P:ureter smooth muscle cell differentiation; ISO:RGD.
DR   GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR   GO; GO:0072105; P:ureteric peristalsis; ISO:RGD.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR027008; Teashirt_fam.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12487:SF5; TEASHIRT HOMOLOG 3; 1.
DR   PANTHER; PTHR12487; TEASHIRT-RELATED; 1.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Cell projection; Developmental protein; DNA-binding; Homeobox;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1072
FT                   /note="Teashirt homolog 3"
FT                   /id="PRO_0000399476"
FT   ZN_FING         204..228
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         265..289
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         376..400
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   DNA_BIND        882..952
FT                   /note="Homeobox; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   ZN_FING         967..989
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1032..1055
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          44..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         672
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63HK5"
SQ   SEQUENCE   1072 AA;  117463 MW;  9CB7824517771F35 CRC64;
     MAAYVSDELK AAALVEDDIE PEEQVADGEP SAKYMCPEKE LSKACPSYQN SPAAEFSSHE
     MDSESHISET SDRMADFESS SIKNEEETKE VQVPLEDTTV SDSLEQMKAV YNNFLSNSYW
     SNLNLNLHQP SSENNGGGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS QNRMLPEPSL
     FSTVQLYRQS SKLYGSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR DDNHETDNNN
     PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY QKVPLKEPVT
     PVAAKIIPAA RKKPSLELEL PSSPDSTGGT PKATLSDASD ALQKNSNPYI TPNNRYGHQN
     GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK KGKPIMETPV
     TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SVSPKLTVEI KKEVDKEKAV LDEKPKEKEK
     ASEEEEKYDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG TPSWGGYPSI
     HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKTQT LVSPPSSQTS PMPKTNFHAM
     EELVKKVTEK VAKVEEKMKE PDSKLSPPKR ATPSPCSSEQ SEPIKMEASS GSGFKSQENS
     PSPPRDVCKE ASPSAEPVEN GKELVKPLSG GSLSGSTAII TDHPPEQPFV NPLSALQSVM
     NIHLGKAAKP SLPALDPMSM LFKMSNSLAE KAAVATPPPL QAKKAEHLDR YFYHVNNDQP
     IDLTKGKSDK GCSLGSGLLS PTSTSPATSS STVTTAKTSA VVSFMSNSPL RENALSDISD
     MLKNLTESHT SKSSTPSSIS EKSDIDGATL EEAEESTPAQ KRKGRQSNWN PQHLLILQAQ
     FAASLRQTSE GKYIMSDLSP QERMHISRFT GLSMTTISHW LANVKYQLRR TGGTKFLKNL
     DTGHPVFFCN DCASQIRTPS TYISHLESHL GFRLRDLSKL STEQINNQIA QTKSPSEKMV
     TSSPEEDLGT TYQCKLCNRT FASKHAVKLH LSKTHGKSPE DHLLFVSELE KQ
//