A33_PLEWA
ID A33_PLEWA Reviewed; 625 AA.
AC Q02084;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Zinc-binding protein A33;
OS Pleurodeles waltl (Iberian ribbed newt).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Pleurodeles.
OX NCBI_TaxID=8319;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=7679068; DOI=10.1002/j.1460-2075.1993.tb05636.x;
RA Bellini M., Lacroix J.-C., Gall J.G.;
RT "A putative zinc-binding protein on lampbrush chromosome loops.";
RL EMBO J. 12:107-114(1993).
RN [2]
RP SEQUENCE REVISION TO 15-60 AND 427-429.
RA Bellini M., Lacroix J.-C., Gall J.G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, AND MUTAGENESIS OF CYS-178;
RP CYS-202 AND HIS-267.
RX PubMed=7593179; DOI=10.1083/jcb.131.3.563;
RA Bellini M., Lacroix J.-C., Gall J.G.;
RT "A zinc-binding domain is required for targeting the maternal nuclear
RT protein PwA33 to lampbrush chromosome loops.";
RL J. Cell Biol. 131:563-570(1995).
CC -!- FUNCTION: May be a nuclear regulatory protein that is stored in the
CC germinal vesicle for use during early embryogenesis and may play a role
CC in the synthesis or processing of pre-mRNA during oogenesis. Binds 3
CC Zn(2+) ions. {ECO:0000269|PubMed:7593179}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Lampbrush chromosome
CC loops and in some nucleoplasmic particles of the germinal vesicle.
CC -!- DEVELOPMENTAL STAGE: It first appears on the chromosome loops and in
CC the nucleoplasm of the germinal vesicle (GV). It is transmitted to the
CC egg at GV breakdown and appears in embryonic nuclei at the mid-blastula
CC stage and is found in many but not all nuclei at still later stages of
CC embryogenesis. {ECO:0000269|PubMed:7679068}.
CC -!- DOMAIN: B box-type zinc binding domain is required for targeting this
CC protein to lampbrush chromosome loops and for normal functioning of
CC this protein in the oocyte.
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DR EMBL; L04190; AAA49614.2; -; mRNA.
DR PIR; S28418; S28418.
DR AlphaFoldDB; Q02084; -.
DR SMR; Q02084; -.
DR PRIDE; Q02084; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Developmental protein; Metal-binding; Nucleus;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..625
FT /note="Zinc-binding protein A33"
FT /id="PRO_0000055746"
FT DOMAIN 48..101
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 429..625
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 163..203
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 234..275
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 337..386
FT COMPBIAS 15..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 178
FT /note="C->F: No effect on intranuclear localization."
FT /evidence="ECO:0000269|PubMed:7593179"
FT MUTAGEN 202
FT /note="C->F: No effect on intranuclear localization."
FT /evidence="ECO:0000269|PubMed:7593179"
FT MUTAGEN 267
FT /note="H->N: No Zn(2+) binding. Inhibits the targeting to
FT lampbrush chromosome loops and to nucleoplasmic particles."
FT /evidence="ECO:0000269|PubMed:7593179"
SQ SEQUENCE 625 AA; 71053 MW; BCE8003BB6BF5B13 CRC64;
MANSTVAEPE KMEQSGTCEE DEEEENMEGD EDECDDDEEE NMEPAETVTI GSTYKCRRSD
NTLHAAEIIK TRKTKENAEE FYVHYVGLNR RQNEWVDKSR VLQAKQIKTE ELNNTEDETN
GVSDQSEGKA ARSNKRKIED GDGDQKKRKV DDEEDDFTED LTCPLCRSLF KEPVILECGH
NFCKHCIDKS WESASAFSCP ECKEVLTERK YTTNRVLANL VKKAAVGVKD KDVKPKEKCD
EHDERLKLFC KDDGTLACVI CRDSLKHSNH NFLPIQDAVG VYRDQLIALV SPLETTMKEN
QKLKCDQSQK ISLHRENIVD CKKHIECEFE KLHQFLREKE AKMVEDLNAE REGLLKDMEA
NLVKMTDNCE FIEEAISTTQ SRLNESDPIA FLTDIKSFIE KCCEEHRKGV PAESVLVNKE
LSQGRFKGPL QYIIWKELKS VVQPGLAPLT LDPNTAHPNL VLSEGLTSVK YTDTKQQLPD
NPKRFSQCIL VLGAEGFDSG KHYWEVEVGN KTAWDVGMAS ESSNRKGKIK LNPKNGYWAI
WLRNGNAFKA LESPSKTLNL TSKPSKIGVY LDYEGGQVSF YNADDMSPIY TFNGSFTEKL
YPYLSPFLQD SGKNAEPLKL VHTKL
