ID   STP2_GORGO              Reviewed;         133 AA.
AC   Q9N1A5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Nuclear transition protein 2;
DE            Short=TP-2;
DE            Short=TP2;
DE   Flags: Fragment;
GN   Name=TNP2;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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; AF215718; AAF35857.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9N1A5; -.
DR   STRING; 9593.ENSGGOP00000023058; -.
DR   PRIDE; Q9N1A5; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   HOGENOM; CLU_152028_0_0_1; -.
DR   InParanoid; Q9N1A5; -.
DR   Proteomes; UP000001519; 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:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0007340; P:acrosome reaction; IBA:GO_Central.
DR   GO; GO:0007341; P:penetration of zona pellucida; IBA:GO_Central.
DR   GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
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..>133
FT                   /note="Nuclear transition protein 2"
FT                   /id="PRO_0000191424"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           111..119
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..124
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         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
FT   NON_TER         133
SQ   SEQUENCE   133 AA;  15052 MW;  26DED78CA92688E2 CRC64;
     MDTKTHSLPI THTQLHSNSQ PQSRTCTRHC QTFSQSCRQS HRGSRSRSSS QSPASHRNPT
     GAHSSSGHQS QSPNTSPPPK RHKKTMNSHH SPRRPTILHC SCPKNRKNLE GKLKKKKMAK
     RIQQVYKTKT RSS