TSH3_RAT
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 25-MAY-2022, entry version 81.
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; D3ZKB9; -.
DR GeneID; 308523; -.
DR KEGG; rno:308523; -.
DR UCSC; RGD:1306322; rat.
DR CTD; 57616; -.
DR RGD; 1306322; Tshz3.
DR eggNOG; ENOG502RJS7; Eukaryota.
DR InParanoid; D3ZKB9; -.
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 transcription, DNA-templated; 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 InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR026810; Tshz3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF5; PTHR12487:SF5; 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
