ID H9GF57_ANOCA Unreviewed; 799 AA.
AC H9GF57;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Zinc fingers and homeoboxes 2 {ECO:0000313|Ensembl:ENSACAP00000009203.2};
GN Name=ZHX2 {ECO:0000313|Ensembl:ENSACAP00000009203.2};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000009203.2, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000009203.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009203.2};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000009203.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000256|ARBA:ARBA00007440}.
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DR RefSeq; XP_003228184.1; XM_003228136.3.
DR RefSeq; XP_008119883.1; XM_008121676.2.
DR AlphaFoldDB; H9GF57; -.
DR STRING; 28377.ENSACAP00000009203; -.
DR Ensembl; ENSACAT00000009396.2; ENSACAP00000009203.2; ENSACAG00000009402.2.
DR GeneID; 100567360; -.
DR KEGG; acs:100567360; -.
DR CTD; 22882; -.
DR eggNOG; ENOG502RHIC; Eukaryota.
DR GeneTree; ENSGT00950000182893; -.
DR HOGENOM; CLU_009147_1_0_1; -.
DR InParanoid; H9GF57; -.
DR OMA; ENHMEGT; -.
DR OrthoDB; 5350395at2759; -.
DR TreeFam; TF333363; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000009402; Expressed in dewlap and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 105..133
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 438..488
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 528..578
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 627..677
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 440..489
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 530..579
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT DNA_BIND 629..678
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 88534 MW; 131602CBF8C70D60 CRC64;
MASKRKSTTP CMVRAPEATG QGVSKDSDAA NAAPEKDMGD ELAAGKENSE NDCEVIEGKS
SPANPSKKSL GGYECKYCPY STQNLVDFTE HIDTQHPNVI LNPLYVCAEC NFTTKKYDLL
SDHNTKLHPG ENNFKLKLIK LNDQTILEQS IEVIHTSLAT EPPECEVGHL GTSGMNKAIP
IINVGKPKSE AKKISIDSHR DGIHLAEPIT CIKGAELLQD ILAHVMPSVQ LPPNINLVPK
VPVPMNITKY NSALDTNATM INSFNKFPYP TQAELSWLTA ASKHPEEQIR IWFAIQRLKH
GISWSPEEVE EARKKMFNGT IQAAPQTITV LPAHVTPAKM SQPLIQTAVP CQILSQTGLV
LTQLSNGSNV SPVTLAVAAN HKQKRSTQNQ SAVPEAKRPH VVPSEGLSKQ NTVAAPTSTT
TAPLSPVSSI PASDRKKTKE QITALKTSFL ISQFPDNAEI YRLIEITGLS RSEIKKWFSD
YRYRSQKGIV NISSESIPMD QLALAAARQG RPYSLYSDFA FHKFKGKSPE QFKILEESFL
KSSFPTQSEL ERLRSEAKMS RREVETWFNE RRKLRDNMEQ AVLDSMGSNI KNKDQGDSNG
ALTQTEKSNI SKDSTSSCKC PAFATSSQQQ SHLLKSMFAV TQWPSPQDYD ELAAQTGLTR
TEIVRWFKEN RGFLRTGKLK WFDQYQQQCV IDGYDIPEEP ISTESVKKES DAVQQPEKEH
EKLEKQNTVG MVKSQCNDQN SQNSDKNPDA GNLGFIEVTT DDGNDDDDAS DCMDNWSQPV
PESKADVDSE SLSGDNSHT
//
