TSH2_PIG
ID TSH2_PIG Reviewed; 1035 AA.
AC A5GFT6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Teashirt homolog 2;
GN Name=TSHZ2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CR974445; CAN13183.1; -; Genomic_DNA.
DR EMBL; CR956408; CAN13183.1; JOINED; Genomic_DNA.
DR EMBL; CR956408; CAN13227.1; -; Genomic_DNA.
DR EMBL; CR974445; CAN13227.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001108146.1; NM_001114674.1.
DR AlphaFoldDB; A5GFT6; -.
DR STRING; 9823.ENSSSCP00000030054; -.
DR PaxDb; A5GFT6; -.
DR PRIDE; A5GFT6; -.
DR Ensembl; ENSSSCT00030098216; ENSSSCP00030045211; ENSSSCG00030070234.
DR GeneID; 100136903; -.
DR KEGG; ssc:100136903; -.
DR CTD; 128553; -.
DR eggNOG; ENOG502QV71; Eukaryota.
DR InParanoid; A5GFT6; -.
DR OrthoDB; 106971at2759; -.
DR TreeFam; TF328447; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; A5GFT6; SS.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR027010; Tshz2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF3; PTHR12487:SF3; 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 3: Inferred from homology;
KW Coiled coil; Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1035
FT /note="Teashirt homolog 2"
FT /id="PRO_0000296391"
FT ZN_FING 216..240
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 276..300
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..405
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 842..912
FT /note="Homeobox"
FT ZN_FING 927..949
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 995..1018
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..42
FT /evidence="ECO:0000255"
FT COMPBIAS 23..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE9"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 801
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
FT CROSSLNK 821
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRE2"
SQ SEQUENCE 1035 AA; 114602 MW; B2243190681D354C CRC64;
MPRRKQQAPK RAAGYAQEEQ LKEEEEIKEE EEEEEDSGSV AQLQGSNDPG TDEELETGAE
QKGCFSYQNS PGSHLSNQDA ENESLLSDAS DQVSDIKSVC SRDASDKKAS VHPKLPTEAH
SCMDKMTAVY ANILSDSYWS GLGLGFKLSS SERRHCDTRN GSSKTDFDWH QDALSKSLQQ
NLPPRSVSKP SLFSSVQLYR QSSKMCGTVF TGASRFRCRQ CSAAYDTLVE LTVHMNETGH
YQDDNRKKDK LRPTSYSKPR KRAFQDMDKE DAQKVLKCMF CGDSFDSLQD LSVHMIKTKH
YQKVPLKEPV PTISSKMVTP AKKRVFDVNR PCSPDSTTGS FADPFPAPKN ASLQLSSNNR
YGYQNGASYT WQFEACKSQI LKCMECGSSH DTLQQLTTHM MVTGHFLKVT SSASKKGKQL
VLDPLAVEKM QSLSDAPSSD SLAPKPSSNS ASDCTASTTE LKRESKKEKP EELRTDEKVL
KSEDYEDPLQ KPLDPAMKYQ YLREEDLEDG SKGGGDILKS LENTVTTAIN KAQNGAPSWS
AYPSIHAAYQ LSEGTKPSLP MGSQVLQIRP NLANKLRPIA PKWKVMPLVS VPTSLAPYTQ
VKKEPEDKEE VAKECGQESP HEEASSFSHS EGDSFPKSEP PAESKKAEPC PLREEDKRMK
DGGEKEKAQP VEPVSSLSNG CALAAHAPAP PCVNPLSALQ SVLNNHLGKA TEPLRSPSCS
SPSSSTMAMF HKSSLGVMDK PVLSPASTRP ASVSRRYLFE NNDQPIDLTK SKSKKAESSQ
AQSCTSPPQK HALSDIADMV KVLPKATTPK PAASSRVPPV KLEMDVRRFE DVSSEVSTLH
KRKGRQSNWN PQHLLILQAQ FASSLFQTSE GKYLLSDLGP QERMQISKFT GLSMTTISHW
LANVKYQLRK TGGTKFLKNM DKGHPIFYCS DCASQFRTPS TYISHLESHL GFQMKDMTRM
AVEQQSQVEQ EISRVSSAQR SPETIAGEED TDSKFKCKLC CRTFVSKHAV KLHLSKTHSK
SPEHHAQFVT DVDEE
