ID   STP2_PANPA              Reviewed;         133 AA.
AC   Q9N1A6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Nuclear transition protein 2;
DE            Short=TP-2;
DE            Short=TP2;
DE   Flags: Fragment;
GN   Name=TNP2;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10659848; DOI=10.1038/35002070;
RA   Wyckoff G.J., Wang W., Wu C.-I.;
RT   "Rapid evolution of male reproductive genes in the descent of man.";
RL   Nature 403:304-309(2000).
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; AF215717; AAF35856.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9N1A6; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   Proteomes; UP000240080; Unplaced.
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.
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..>133
FT                   /note="Nuclear transition protein 2"
FT                   /id="PRO_0000191429"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           110..118
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        109..123
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         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   NON_TER         133
SQ   SEQUENCE   133 AA;  14925 MW;  D2D624DD296F9BCF CRC64;
     MDTKTHSLPI THTQLHSNSQ PQSCTCTHHR QTFSQSCRQS HRGSRSRSSS QSPASHRNPT
     GAHSSSGHQS QSPNTSPPPK RHKKTMNSHH SPMRPTLHCS CPKNRKNLEG KLKTKKMAKR
     IQQVYKTKTR SSG