ID   STP2_MACFA              Reviewed;         141 AA.
AC   Q8WNV1; Q4R607;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Nuclear transition protein 2;
DE            Short=TP-2;
DE            Short=TP2;
GN   Name=TNP2; ORFNames=QtsA-11347, QtsA-19461;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a key role in the replacement of histones to protamine
CC       in the elongating spermatids of mammals. In condensing spermatids,
CC       loaded onto the nucleosomes, where it promotes the recruitment and
CC       processing of protamines, which are responsible for histone eviction.
CC       {ECO:0000250|UniProtKB:P11378}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11101}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P11101}. Chromosome
CC       {ECO:0000250|UniProtKB:P11101}. Note=Loaded onto the nucleosomes of
CC       condensing spermatids (By similarity). Nuclear import is mediated by
CC       IPO4. Nucleolar localization requires the protein to be phosphorylated
CC       (By similarity). {ECO:0000250|UniProtKB:P11101,
CC       ECO:0000250|UniProtKB:P11378}.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AB064994; BAB83536.1; -; mRNA.
DR   EMBL; AB169384; BAE01468.1; -; mRNA.
DR   RefSeq; NP_001274665.1; NM_001287736.1.
DR   AlphaFoldDB; Q8WNV1; -.
DR   STRING; 9541.XP_005591318.1; -.
DR   Ensembl; ENSMFAT00000005419; ENSMFAP00000031205; ENSMFAG00000036693.
DR   GeneID; 102135039; -.
DR   CTD; 7142; -.
DR   VEuPathDB; HostDB:ENSMFAG00000036693; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   GeneTree; ENSGT00390000008176; -.
DR   OMA; RPQSHTC; -.
DR   OrthoDB; 1586614at2759; -.
DR   Proteomes; UP000233100; Chromosome 20.
DR   Bgee; ENSMFAG00000036693; Expressed in multicellular organism.
DR   GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR   GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR   InterPro; IPR000678; TP2.
DR   PANTHER; PTHR17488; PTHR17488; 1.
DR   Pfam; PF01254; TP2; 1.
DR   PROSITE; PS00970; TP2_1; 1.
DR   PROSITE; PS00971; TP2_2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Developmental protein; Differentiation; DNA-binding;
KW   Metal-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Spermatogenesis; Zinc.
FT   CHAIN           1..141
FT                   /note="Nuclear transition protein 2"
FT                   /id="PRO_0000191426"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           114..122
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   COMPBIAS        1..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..141
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
SQ   SEQUENCE   141 AA;  15777 MW;  0B4958AC7CCC11B9 CRC64;
     MDTKTHSLPI THTQLHSNSR PQSRSQCTCT HHCQTFSQSC RQSQRGSRSR SSSQSPATHQ
     NPTGAHSSSG CQSQSPNASP PPKRHKKTMN SHHSPTRPTI LHSSCPKNRK NLEGKLNKKK
     MAKRIQQVYK TKKRSSGRKS N