NPM_RHIMB
ID NPM_RHIMB Reviewed; 198 AA.
AC Q1HTZ8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Nucleoplasmin {ECO:0000305};
GN Name=np {ECO:0000312|EMBL:ABC69370.1};
OS Rhinella marina (Cane toad) (Bufo marinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX NCBI_TaxID=8386 {ECO:0000312|EMBL:ABC69370.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16646973; DOI=10.1186/1471-2164-7-99;
RA Frehlick L.J., Eirin-Lopez J.M., Jeffery E.D., Hunt D.F., Ausio J.;
RT "The characterization of amphibian nucleoplasmins yields new insight into
RT their role in sperm chromatin remodeling.";
RL BMC Genomics 7:99-99(2006).
CC -!- FUNCTION: Acts as a chaperone for histones, such as histone H2A-H2B,
CC and thus regulates the assembly of nucleosome cores. Involved in
CC chromatin remodeling, especially during fertilization and early
CC embryonic development. May be involved in sperm chromatin
CC decondensation during fertilization. {ECO:0000250|UniProtKB:P05221,
CC ECO:0000250|UniProtKB:Q86SE8}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000305|PubMed:16646973}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16646973}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes.
CC {ECO:0000269|PubMed:16646973}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; DQ340657; ABC69370.1; -; mRNA.
DR AlphaFoldDB; Q1HTZ8; -.
DR SMR; Q1HTZ8; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chromatin regulator; Developmental protein; Fertilization;
KW Nucleus.
FT CHAIN 1..198
FT /note="Nucleoplasmin"
FT /id="PRO_0000430717"
FT REGION 35..38
FT /note="Acidic tract A1"
FT /evidence="ECO:0000305"
FT REGION 125..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..145
FT /note="Acidic tract A2"
FT /evidence="ECO:0000305"
FT REGION 172..174
FT /note="Acidic tract A3"
FT /evidence="ECO:0000305"
FT MOTIF 152..167
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P05221"
FT COMPBIAS 125..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250|UniProtKB:P05221"
FT SITE 82
FT /note="Interaction between pentamers"
FT /evidence="ECO:0000250|UniProtKB:P05221"
SQ SEQUENCE 198 AA; 21674 MW; 6A8F94DF3C174DB7 CRC64;
MASTASNTSK LEKPVSLIWG CELNEQNKTF VFKVSDEDKS EHQLALRTVC LGDKAKDEFH
VVEIVPQVEG SDVQPVPIAS LKPSILPMAT MVGIELTPPV TFRLKAGSGP VYISGQHIAL
EEDYSWAEEE GEEEVEEEEE EEDPESPPKA VKRPAASKKG SQAKKKKMDK DEEESSEEDS
PVKKGKGAGR GRKPAAKK
