ID ZHX2_PONAB Reviewed; 837 AA.
AC Q5R7F2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 87.
DE RecName: Full=Zinc fingers and homeoboxes protein 2;
DE AltName: Full=Zinc finger and homeodomain protein 2;
GN Name=ZHX2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a transcriptional repressor. Represses the promoter
CC activity of the CDC25C gene stimulated by NFYA. May play a role in
CC retinal development where it regulates the composition of bipolar cell
CC populations, by promoting differentiation of bipolar OFF-type cells. In
CC the brain, may promote maintenance and suppress differentiation of
CC neural progenitor cells in the developing cortex.
CC {ECO:0000250|UniProtKB:Q8C0C0, ECO:0000250|UniProtKB:Q9Y6X8}.
CC -!- SUBUNIT: Homodimer (via homeobox domain 1). Heterodimer with ZHX1 (via
CC homeobox domain 1). Heterodimer with ZHX3 (via homeobox domain 1).
CC Heterodimerization with ZHX1 is not necessary for repressor activity.
CC Interacts (via homeobox domain) with NFYA (via N-terminus). Interacts
CC with EFNB1 intracellular domain peptide; the interaction enhances ZHX2
CC transcriptional repression activity. {ECO:0000250|UniProtKB:Q8C0C0,
CC ECO:0000250|UniProtKB:Q9Y6X8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC Note=Colocalizes with EFNB1 intracellular domain in the nucleus.
CC {ECO:0000250|UniProtKB:Q8C0C0}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}.
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; CR860166; CAH92308.1; -; mRNA.
DR RefSeq; NP_001126352.1; NM_001132880.1.
DR AlphaFoldDB; Q5R7F2; -.
DR SMR; Q5R7F2; -.
DR GeneID; 100173333; -.
DR KEGG; pon:100173333; -.
DR CTD; 22882; -.
DR InParanoid; Q5R7F2; -.
DR OrthoDB; 5350395at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00086; homeodomain; 4.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR041057; ZHX_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15467:SF5; ZINC FINGERS AND HOMEOBOXES PROTEIN 2; 1.
DR PANTHER; PTHR15467; ZINC-FINGERS AND HOMEOBOXES RELATED; 1.
DR Pfam; PF00046; Homeodomain; 3.
DR Pfam; PF18387; zf_C2H2_ZHX; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 4.
DR PROSITE; PS50071; HOMEOBOX_2; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Differentiation; DNA-binding; Homeobox; Isopeptide bond; Metal-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..837
FT /note="Zinc fingers and homeoboxes protein 2"
FT /id="PRO_0000049393"
FT ZN_FING 78..101
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 110..133
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 263..324
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 439..501
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 530..591
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 628..690
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..77
FT /note="Interaction with EFNB1"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C0"
FT REGION 167..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..358
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT REGION 263..497
FT /note="Required for interaction with NFYA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT REGION 263..446
FT /note="Required for repressor activity"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT REGION 317..446
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT REGION 404..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C0"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C0"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X8"
SQ SEQUENCE 837 AA; 92154 MW; 7415145C2F1ECE12 CRC64;
MASKRKSTTP CMVRTSQVVE QDVPEEVDRA KEKGIGTPQP DVAKDCWAAE LENSSKENEV
IEVKSMGESQ SKKLQGGYEC KYCPYSTQNL NEFTEHVDMQ HPNVILNPLY VCAECNFTTK
KYDSLSDHNS KFHPGEANFK LKLIKRNNQT VLEQSIEATN HVVSITTSGP GTGDSDSGIS
VSKTPIMKPG KPKADAKKVP KKPEEIAPEN HVEGTARLVT DTAEILSRLG GVELLQDTLG
HVMPSVQLPP NINLVPKVPV PLNTTKYNSA LDTNATMINS FNKFPYPTQA ELSWLTAASK
HPEEHIRIWF ATQRLKHGIS WSPEEVEEAR KKMFNGTIQS VPPTITVLPA QLAPTKVTQP
ILQTALPCQI LGQTSLVLTP VTSGSTTVSC SPITLAVAGV TNHGQKRPLV TPQAAPEPKR
PHIAQVPEPP PKVANPPLTP ASDRKKTKEQ IAHLKASFLQ SQFPDDAEVY RLIEVTGLAR
SEIKKWFSDH RYRCQRGIVH ITSGSLAKEQ LAIAASRHGR TYHAYPDFAP QKFKEKTQGQ
VKILEDSFLK SSFPTQAELD RLRVETKLSR REIDSWFSER RKLRDSMEQA VLDSMGSGKK
GQDVGAPNGA LSRLDQLSGA QLTSSLPSPS PAIAKSQEQV HLLRSTFART QWPTPQEYDQ
LAAKTGLVRT EIVRWFKENR CLLKTGTVKW MEQYQHQPVA DDHGYDAVAR KATKPMAESP
KNGGDMVPQY YKDPKKLCEE DLEKLVPRVK VGSEPAKDCL PAKPSEATSD RSEGSSRDGQ
GSDENEESSV VDYVEVTVGE EDAISDRSDS WSQAAAEGVA ELAESDSDCV PAEAGQA
//
