ID   STP2_CANLF              Reviewed;         129 AA.
AC   O77645;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Nuclear transition protein 2;
DE            Short=TP-2;
DE            Short=TP2;
GN   Name=TNP2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shibuya H., Nonneman D., Liu P.-C., Johnson G.S.;
RT   "Polymorphisms in the canine transition protein 2 gene.";
RL   Submitted (JUN-1998) 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; AF071208; AAC23891.1; -; Genomic_DNA.
DR   RefSeq; NP_001013436.1; NM_001013418.1.
DR   AlphaFoldDB; O77645; -.
DR   STRING; 9615.ENSCAFP00000047443; -.
DR   GeneID; 479849; -.
DR   KEGG; cfa:479849; -.
DR   CTD; 7142; -.
DR   InParanoid; O77645; -.
DR   OrthoDB; 1586614at2759; -.
DR   Proteomes; UP000002254; Chromosome 6.
DR   Bgee; ENSCAFG00000031312; Expressed in testis and 19 other tissues.
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..129
FT                   /note="Nuclear transition protein 2"
FT                   /id="PRO_0000191423"
FT   REGION          1..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           104..112
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..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..129
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         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11101"
SQ   SEQUENCE   129 AA;  14567 MW;  AC25DAD6BF3A1F9D CRC64;
     MDTKTQSLPI THTQPHSNSR PQGHTCSQCT CSSHCQTCSQ SCSQSRSSSQ SPTGHHSSSG
     HQSQSPHPTL PPRHQKHTRH SHHCPPRPTT HSCSYPKNRK NFEGKVNKRK VVKRSQQVYK
     TKRRNSGRK