ID   NPM2_MOUSE              Reviewed;         207 AA.
AC   Q80W85; Q8BW23;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Nucleoplasmin-2;
GN   Name=Npm2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=129S6/SvEv;
RX   PubMed=12714744; DOI=10.1126/science.1081813;
RA   Burns K.H., Viveiros M.M., Ren Y., Wang P., DeMayo F.J., Frail D.E.,
RA   Eppig J.J., Matzuk M.M.;
RT   "Roles of NPM2 in chromatin and nucleolar organization in oocytes and
RT   embryos.";
RL   Science 300:633-636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Core histones chaperone involved in chromatin reprogramming,
CC       specially during fertilization and early embryonic development.
CC       Probably involved in sperm DNA decondensation during fertilization.
CC   -!- SUBUNIT: Homopentamer, when bound to H2A-H2B dimers only. Homodecamer
CC       of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4
CC       tetramers simultaneously (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12714744}. Note=Found
CC       in the oocyte nucleus before nuclear membrane breakdown, after which it
CC       is redistributed to the cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ovary specific. {ECO:0000269|PubMed:12714744}.
CC   -!- DOMAIN: The acidic tract A2 mediates histone binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY262112; AAP33133.1; -; mRNA.
DR   EMBL; AK054533; BAC35815.1; -; mRNA.
DR   CCDS; CCDS27261.1; -.
DR   RefSeq; NP_851990.2; NM_181345.3.
DR   RefSeq; XP_006519206.1; XM_006519143.2.
DR   RefSeq; XP_006519208.1; XM_006519145.3.
DR   RefSeq; XP_006519209.1; XM_006519146.3.
DR   RefSeq; XP_006519210.1; XM_006519147.2.
DR   RefSeq; XP_011243393.1; XM_011245091.2.
DR   RefSeq; XP_017171550.1; XM_017316061.1.
DR   AlphaFoldDB; Q80W85; -.
DR   SMR; Q80W85; -.
DR   BioGRID; 236605; 1.
DR   STRING; 10090.ENSMUSP00000057365; -.
DR   iPTMnet; Q80W85; -.
DR   PhosphoSitePlus; Q80W85; -.
DR   REPRODUCTION-2DPAGE; Q80W85; -.
DR   PaxDb; 10090-ENSMUSP00000057365; -.
DR   ProteomicsDB; 293713; -.
DR   Antibodypedia; 22452; 123 antibodies from 23 providers.
DR   DNASU; 328440; -.
DR   Ensembl; ENSMUST00000062629.5; ENSMUSP00000057365.5; ENSMUSG00000047911.7.
DR   GeneID; 328440; -.
DR   KEGG; mmu:328440; -.
DR   UCSC; uc007uot.2; mouse.
DR   AGR; MGI:1890811; -.
DR   CTD; 10361; -.
DR   MGI; MGI:1890811; Npm2.
DR   VEuPathDB; HostDB:ENSMUSG00000047911; -.
DR   eggNOG; ENOG502S0N8; Eukaryota.
DR   GeneTree; ENSGT00940000161418; -.
DR   HOGENOM; CLU_058838_2_0_1; -.
DR   InParanoid; Q80W85; -.
DR   OMA; GQECYES; -.
DR   OrthoDB; 4640673at2759; -.
DR   PhylomeDB; Q80W85; -.
DR   TreeFam; TF327704; -.
DR   BioGRID-ORCS; 328440; 1 hit in 82 CRISPR screens.
DR   ChiTaRS; Npm2; mouse.
DR   PRO; PR:Q80W85; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q80W85; Protein.
DR   Bgee; ENSMUSG00000047911; Expressed in primary oocyte and 72 other cell types or tissues.
DR   ExpressionAtlas; Q80W85; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0061995; F:ATP-dependent protein-DNA complex displacement activity; TAS:Reactome.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR   GO; GO:0009994; P:oocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0051054; P:positive regulation of DNA metabolic process; ISO:MGI.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR   GO; GO:0045836; P:positive regulation of meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0007096; P:regulation of exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR   Gene3D; 2.60.120.340; Nucleoplasmin core domain; 1.
DR   InterPro; IPR004301; Nucleoplasmin.
DR   InterPro; IPR024057; Nucleoplasmin_core_dom.
DR   InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR   PANTHER; PTHR22747; NUCLEOPLASMIN; 1.
DR   PANTHER; PTHR22747:SF14; NUCLEOPLASMIN-2; 1.
DR   Pfam; PF03066; Nucleoplasmin; 1.
DR   SUPFAM; SSF69203; Nucleoplasmin-like core domain; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Chromatin regulator; Developmental protein; Fertilization;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..207
FT                   /note="Nucleoplasmin-2"
FT                   /id="PRO_0000219488"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..152
FT                   /note="Acidic tract A2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           165..180
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        121..146
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..198
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"
FT   SITE            84
FT                   /note="Interaction between pentamers"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        196
FT                   /note="S -> F (in Ref. 2; BAC35815)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  23309 MW;  8B8A8931F85032EE CRC64;
     MSRHSTSSVT ETTAKNMLWG SELNQEKQTC TFRGQGEKKD SCKLLLSTIC LGEKAKEEVN
     RVEVLSQEGR KPPITIATLK ASVLPMVTVS GIELSPPVTF RLRTGSGPVF LSGLECYETS
     DLTWEDDEEE EEEEEEEDED EDADISLEEI PVKQVKRVAP QKQMSIAKKK KVEKEEDETV
     VRPSPQDKSP WKKEKSTPRA KKPVTKK
//