STP2_MACMU
ID STP2_MACMU Reviewed; 137 AA.
AC Q9N1A3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
DE Flags: Fragment;
GN Name=TNP2;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
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; AF215720; AAF35859.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N1A3; -.
DR STRING; 9544.ENSMMUP00000014367; -.
DR eggNOG; KOG4566; Eukaryota.
DR InParanoid; Q9N1A3; -.
DR Proteomes; UP000006718; 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; Reference proteome;
KW Spermatogenesis; Zinc.
FT CHAIN 1..>137
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191427"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..124
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT COMPBIAS 1..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..137
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 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT NON_TER 137
SQ SEQUENCE 137 AA; 15414 MW; B9D947A4B5944C25 CRC64;
MDTKTHSLPI THTQLHSNSR PQSRTCSQCT CTHHRQTFSQ SCRQSQRGSR SRSSSQSPAT
HQNPTGAHSS SGLQSQSPNA SPPPKRHKKT MNSHHSPTRP TILHSSCPKN RKNLEGKLNK
KKMAKRIQQV YKTKKRS