STP2_BOVIN
ID STP2_BOVIN Reviewed; 132 AA.
AC P26377; Q32L25;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
GN Name=TNP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1716912; DOI=10.1515/bchm3.1991.372.1.431;
RA Reinhart N., Kremling H., Luerssen H., Adham I.M., Engel W.;
RT "Characterization of a gene encoding a basic protein of the spermatid
RT nucleus, TNP2, and its close linkage to the protamine genes in the bull.";
RL Biol. Chem. Hoppe-Seyler 372:431-436(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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. {ECO:0000269|PubMed:1716912}.
CC -!- DEVELOPMENTAL STAGE: Haploid stage of the germ cells.
CC {ECO:0000269|PubMed:1716912}.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X56400; CAA39810.1; -; Genomic_DNA.
DR EMBL; X56401; CAA39811.1; -; Genomic_DNA.
DR EMBL; BC109800; AAI09801.1; -; mRNA.
DR PIR; S16134; BGBO2.
DR RefSeq; NP_776625.1; NM_174200.1.
DR AlphaFoldDB; P26377; -.
DR STRING; 9913.ENSBTAP00000048966; -.
DR PaxDb; P26377; -.
DR Ensembl; ENSBTAT00000054025; ENSBTAP00000048966; ENSBTAG00000032884.
DR GeneID; 281538; -.
DR KEGG; bta:281538; -.
DR CTD; 7142; -.
DR VEuPathDB; HostDB:ENSBTAG00000032884; -.
DR VGNC; VGNC:36198; TNP2.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00390000008176; -.
DR HOGENOM; CLU_152028_0_0_1; -.
DR InParanoid; P26377; -.
DR OMA; RPQSHTC; -.
DR OrthoDB; 1586614at2759; -.
DR TreeFam; TF338516; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000032884; Expressed in semen and 25 other tissues.
DR ExpressionAtlas; P26377; baseline and differential.
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..132
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191422"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..113
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..132
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 MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT CONFLICT 62
FT /note="R -> H (in Ref. 1; CAA39810/CAA39811)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..86
FT /note="QSPGPSPPLRRHRHTMHSHQCP -> RARPQPSSEAPQTHHALPPVS (in
FT Ref. 1; CAA39810/CAA39811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 15241 MW; F6205ABC2CB46275 CRC64;
MDTKTQSLPN THAQPHSNSR PQSHACHHCS CSQHCQSRSR SRSCRSRSSS RRPRSHRSPT
GRQGQSPGPS PPLRRHRHTM HSHQCPSRPV THSCSHSKNR KNLEGKVIKR KQVKRSKQVY
KRKRQSSGRK YN
