ZHX2_RAT
ID ZHX2_RAT Reviewed; 836 AA.
AC Q80VX4; G3V6P3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc fingers and homeoboxes protein 2;
DE AltName: Full=Alpha-fetoprotein regulator 1;
DE Short=AFP regulator 1;
DE AltName: Full=Regulator of AFP;
DE AltName: Full=Zinc finger and homeodomain protein 2;
GN Name=Zhx2; Synonyms=Afr1, Raf;
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 {ECO:0000312|EMBL:BAC76614.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 195-358.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:BAC76614.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAC76614.1};
RX PubMed=12741956; DOI=10.1042/bj20030171;
RA Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M.,
RA Sekiguchi T., Kajitani T., Miyamoto K.;
RT "Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family,
RT functions as a transcriptional repressor.";
RL Biochem. J. 373:747-757(2003).
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}.
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DR EMBL; AABR07058000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473950; EDM16240.1; -; Genomic_DNA.
DR EMBL; AB081946; BAC76614.1; -; mRNA.
DR RefSeq; NP_001257985.1; NM_001271056.1.
DR RefSeq; XP_006241716.1; XM_006241654.3.
DR RefSeq; XP_017450346.1; XM_017594857.1.
DR AlphaFoldDB; Q80VX4; -.
DR SMR; Q80VX4; -.
DR IntAct; Q80VX4; 2.
DR STRING; 10116.ENSRNOP00000007326; -.
DR PaxDb; Q80VX4; -.
DR PeptideAtlas; Q80VX4; -.
DR Ensembl; ENSRNOT00000007326; ENSRNOP00000007326; ENSRNOG00000005417.
DR Ensembl; ENSRNOT00000095346; ENSRNOP00000077300; ENSRNOG00000005417.
DR Ensembl; ENSRNOT00000099915; ENSRNOP00000095233; ENSRNOG00000005417.
DR Ensembl; ENSRNOT00000107215; ENSRNOP00000092484; ENSRNOG00000005417.
DR GeneID; 314988; -.
DR KEGG; rno:314988; -.
DR UCSC; RGD:727926; rat.
DR CTD; 22882; -.
DR RGD; 727926; Zhx2.
DR eggNOG; ENOG502RHIC; Eukaryota.
DR GeneTree; ENSGT00950000182893; -.
DR HOGENOM; CLU_009147_1_0_1; -.
DR OMA; AKDQMAI; -.
DR OrthoDB; 518562at2759; -.
DR TreeFam; TF333363; -.
DR PRO; PR:Q80VX4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000005417; Expressed in skeletal muscle tissue and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0006402; P:mRNA catabolic process; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR CDD; cd00086; homeodomain; 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 Pfam; PF00046; Homeodomain; 3.
DR Pfam; PF18387; zf_C2H2_ZHX; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF46689; SSF46689; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
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..836
FT /note="Zinc fingers and homeoboxes protein 2"
FT /id="PRO_0000049394"
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 24..58
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 168..210
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..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C0"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C0"
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 836 AA; 92107 MW; FA6FB232BABF1200 CRC64;
MASKRKSTTP CMVRTSQVVE QDVLEEADRA KDKGLGVPPS DVSKERWAAE PEPSSKESEV
VEVRSVGESQ SKKLQGGYEC KYCPYSTQNL NEFTEHVDMQ HPNVILNPLY VCAECNFTTK
KYDSLSDHNS KFHPGETNFK LKLIKRNNQT VLEQSIEATN HVVSITASAP GSSDNDPGVS
VGKTATVKTG KQKADAKKVP KKPDEAAPDN HMEGTARLVT DTAEILSRLG SVELLHDSLG
HVMPSVQLPP NINLVPKVPV PLNTTKYNSA LDTNATMINS FNKFPYPTQA ELSWLTAASK
HPEEHIRIWF ATQRLKHGIS WSPEEVEEAR KKMFNGTIQS VPPTITVLPA QLTPTKVSQP
ILQTALPCQI LGQPSLVLTQ VTSGSTAVSC SPITLAVAGV TNHGQKRPLV TPQAAPEPKR
PHIAQVPEPP PKVANTPLTP ASDRKKTKLQ IAHLKASFLQ SQFPDDAEVY RLIEVTGLAR
SEIKKWFSDH RYRCQRGIVH ITSESLAKDQ MAITGTRHGR TYHVYPDFAA QKFKEKSQGQ
LKTLEDSFLK SSFPTQAEVE RLRVETKLSR REIDSWFSER RKLRDSMEQA VLDSMGSGKK
GSDVVAPNGA LSRLDQLSGA QLAGPLPSPS SAVVQNQEQV HLLRSTFART QWPTPQEYDQ
LAAKTGLVRT EIVRWFKENR CLLKTGTLSW LEQYQRHHLS DDHGHDVASR RATKHVAESP
KNGSEVAHQY AKDPKALGEE ESEKLVPRVK LVGDPSKDCL AGKPSEATSD RSEGSRDGQG
SEENEESGIV DFVEVTVGEE DAISEKWGSW SQRVAEGTVE RADSDSDSTP AEAGQA
