STP2_PIG
ID STP2_PIG Reviewed; 137 AA.
AC P29258;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
GN Name=TNP2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1627265; DOI=10.1515/bchm3.1992.373.1.261;
RA Keime S., Heitland K., Kumm S., Schloesser M., Hroch N., Holtz W.,
RA Engel W.;
RT "Characterization of four genes encoding basic proteins of the porcine
RT spermatid nucleus and close linkage of three of them.";
RL Biol. Chem. Hoppe-Seyler 373:261-270(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1380212; DOI=10.1111/j.1365-2052.1992.tb00161.x;
RA Keime S., Kumm S., Luerssen H., Engel W.;
RT "The nucleotide sequence of boar transition protein 2 (TNP2) cDNA and
RT haploid expression of the gene during spermatogenesis.";
RL Anim. Genet. 23:373-378(1992).
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. Expression is restricted to haploid germ
CC cells. {ECO:0000269|PubMed:1380212}.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC {ECO:0000305}.
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DR EMBL; M80677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X57989; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S21671; BGPG2.
DR AlphaFoldDB; P29258; -.
DR SMR; P29258; -.
DR STRING; 9823.ENSSSCP00000025815; -.
DR PaxDb; P29258; -.
DR PeptideAtlas; P29258; -.
DR PRIDE; P29258; -.
DR eggNOG; KOG4566; Eukaryota.
DR InParanoid; P29258; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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..137
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191431"
FT REGION 1..137
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..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..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 24
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 BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 38
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 CONFLICT 20..21
FT /note="GP -> TGF (in Ref. 2; X57989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15301 MW; 81842E3F93FD620D CRC64;
MDTKTQSLPN AHTQPHSNSG PQSHACNQCS CSHHCQNCSQ SCDRSQSCSR SRSSSQSPTG
HRSLPGHQSQ SLSPSPSPRH RKRAMHSHRC PSRPGTRSCS HSKKRKNVEG KANKRKGIKR
SQQVYKTKRR SSGRKYN
