REQUA_XENLA
ID REQUA_XENLA Reviewed; 388 AA.
AC Q9W638; Q9PWJ6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Zinc finger protein ubi-d4 A;
DE AltName: Full=Apoptosis response zinc finger protein A;
DE AltName: Full=Protein requiem A;
DE Short=xReq A;
GN Name=req-a; Synonyms=req1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10209271; DOI=10.1016/s0167-4781(99)00031-7;
RA Konishi M., Hiraoka Y., Ogawa M., Sakai Y., Ishii H., Aiso S.;
RT "Molecular cloning and expression of Xenopus laevis Requiem cDNA.";
RL Biochim. Biophys. Acta 1445:172-176(1999).
CC -!- FUNCTION: May be a transcription factor required for the apoptosis
CC response following survival factor withdrawal from myeloid cells. Might
CC also have a role in the development and maturation of lymphoid cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; AB021741; BAA77574.1; -; mRNA.
DR EMBL; AB021737; BAA77570.1; -; mRNA.
DR RefSeq; NP_001079117.1; NM_001085648.1.
DR RefSeq; XP_018111885.1; XM_018256396.1.
DR AlphaFoldDB; Q9W638; -.
DR SMR; Q9W638; -.
DR GeneID; 373651; -.
DR KEGG; xla:373651; -.
DR CTD; 373651; -.
DR Xenbase; XB-GENE-945342; dpf2.L.
DR OMA; GPXRILE; -.
DR OrthoDB; 708781at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 373651; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..388
FT /note="Zinc finger protein ubi-d4 A"
FT /id="PRO_0000168152"
FT ZN_FING 205..228
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 269..329
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 326..376
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 60..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 339..340
FT /note="Missing (in Ref. 1; BAA77570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 43907 MW; 49788CAFBBE08558 CRC64;
MAAAVEKILG EQYYKDAMEQ CHNYNARLCA ERSVRLPFLD SQTRVAQSNC YIWMEKRHRG
PGSAPGQLYT YPSRRWRKKR RAHPPEDPRL SFPSLKPDPE QMLKKEGVIP PDGSSLEALL
RSDPIEKRIM PDSRDDDSLT EFPPLSRSAR KRILEPDDFL DDLDDEDYEE DTPKKRGKGK
AKGKGIGSAR KKLDAAALDD RDKPYACDIC GKRYKNRPGL SYHYAHSHLV DEEGAGAEDK
EDSQPPTPIM HRPEEQKSKK GPDGIALPNN YCDFCLGDSK INKKTNQSEE LVSCSDCGRS
GHPSCLQFTA VMMAAVKTYR WQCIECKCCN ICGTSENDDQ LLFCDDCDRG YHMYCLVPPV
AEPPEGSWSC HLCLDLLKDK ASIYQNQS