STP2_RAT
ID STP2_RAT Reviewed; 114 AA.
AC P11101; Q64390; Q64561; Q6AYX7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
GN Name=Tnp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2726489; DOI=10.1093/nar/17.9.3585;
RA Luerssen H., Maier W.-M., Hoyer-Fender S., Engel W.;
RT "The nucleotide sequence of rat transition protein 2 (TP2) cDNA.";
RL Nucleic Acids Res. 17:3585-3585(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=8954887; DOI=10.1006/prep.1996.0118;
RA Meetei A.R., Rao M.R.S.;
RT "Cloning of cDNA encoding rat spermatidal protein TP2 and expression in
RT Escherichia coli.";
RL Protein Expr. Purif. 8:409-415(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8720108;
RX DOI=10.1002/(sici)1098-2795(199601)43:1<1::aid-mrd1>3.0.co;2-w;
RA Schlueter G., Celik A.B., Obata R., Schlicker M., Hofferbert S.,
RA Schlung A., Adham I.M., Engel W.;
RT "Sequence analysis of the conserved protamine gene cluster shows that it
RT contains a fourth expressed gene.";
RL Mol. Reprod. Dev. 43:1-6(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 89-114.
RX PubMed=3307778; DOI=10.1016/s0006-291x(87)80140-7;
RA Cole K.D., Kistler W.S.;
RT "Nuclear transition protein 2 (TP2) of mammalian spermatids has a very
RT basic carboxyl terminal domain.";
RL Biochem. Biophys. Res. Commun. 147:437-442(1987).
RN [6]
RP ZINC-BINDING.
RX PubMed=1930189; DOI=10.1016/0006-291x(91)91741-t;
RA Baskaran R., Rao M.R.S.;
RT "Mammalian spermatid specific protein, TP2, is a zinc metalloprotein with
RT two finger motifs.";
RL Biochem. Biophys. Res. Commun. 179:1491-1499(1991).
RN [7]
RP ZINC-BINDING.
RX PubMed=8076694; DOI=10.1016/0014-5793(94)00799-3;
RA Kundu T.K., Rao M.R.S.;
RT "Characterization of the zinc-metalloprotein nature of rat spermatidal
RT protein TP2.";
RL FEBS Lett. 351:6-10(1994).
RN [8]
RP MUTAGENESIS, AND SUBCELLULAR LOCATION.
RX PubMed=10961985; DOI=10.1074/jbc.m002734200;
RA Meetei A.R., Ullas K.S., Rao M.R.S.;
RT "Identification of two novel zinc finger modules and nuclear localization
RT signal in rat spermatidal protein TP2 by site-directed mutagenesis.";
RL J. Biol. Chem. 275:38500-38507(2000).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-101 AND SER-109, AND
RP MUTAGENESIS OF SER-68; SER-90; THR-101; SER-108 AND SER-109.
RX PubMed=11772016; DOI=10.1021/bi0117652;
RA Meetei A.R., Ullas K.S., Vasupradha V., Rao M.R.S.;
RT "Involvement of protein kinase A in the phosphorylation of spermatidal
RT protein TP2 and its effect on DNA condensation.";
RL Biochemistry 41:185-195(2002).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14514679; DOI=10.1074/jbc.m308365200;
RA Ullas K.S., Rao M.R.S.;
RT "Phosphorylation of rat spermatidal protein TP2 by sperm-specific protein
RT kinase A and modulation of its transport into the haploid nucleus.";
RL J. Biol. Chem. 278:52673-52680(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17682055; DOI=10.1128/mcb.00519-07;
RA Pradeepa M.M., Manjunatha S., Sathish V., Agrawal S., Rao M.R.;
RT "Involvement of importin-4 in the transport of transition protein 2 into
RT the spermatid nucleus.";
RL Mol. Cell. Biol. 28:4331-4341(2008).
CC -!- FUNCTION: Plays a key role in the replacement of histones to protamine
CC in the elongating spermatids of mammals (PubMed:11772016). In
CC condensing spermatids, loaded onto the nucleosomes, where it promotes
CC the recruitment and processing of protamines, which are responsible for
CC histone eviction (By similarity). {ECO:0000250|UniProtKB:P11378,
CC ECO:0000269|PubMed:11772016}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10961985,
CC ECO:0000269|PubMed:14514679, ECO:0000269|PubMed:17682055}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10961985, ECO:0000269|PubMed:14514679}.
CC Chromosome {ECO:0000269|PubMed:14514679}. Note=Loaded onto the
CC nucleosomes of condensing spermatids (By similarity). Nuclear import is
CC mediated by IPO4 (PubMed:17682055). Nucleolar localization requires the
CC protein to be phosphorylated (PubMed:14514679).
CC {ECO:0000250|UniProtKB:P11378, ECO:0000269|PubMed:14514679,
CC ECO:0000269|PubMed:17682055}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:11772016,
CC ECO:0000269|PubMed:14514679}.
CC -!- DEVELOPMENTAL STAGE: Expressed during stages 12-15 of spermiogenesis.
CC {ECO:0000269|PubMed:14514679}.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X14776; CAA32882.1; -; mRNA.
DR EMBL; U52958; AAB02693.1; -; mRNA.
DR EMBL; Z46939; CAA87064.1; -; Genomic_DNA.
DR EMBL; BC078849; AAH78849.1; -; mRNA.
DR PIR; S04094; S04094.
DR PIR; S57667; S57667.
DR RefSeq; NP_058753.2; NM_017057.2.
DR AlphaFoldDB; P11101; -.
DR BioGRID; 246958; 3.
DR STRING; 10116.ENSRNOP00000003455; -.
DR iPTMnet; P11101; -.
DR PhosphoSitePlus; P11101; -.
DR PaxDb; P11101; -.
DR GeneID; 24840; -.
DR KEGG; rno:24840; -.
DR UCSC; RGD:3885; rat.
DR CTD; 7142; -.
DR RGD; 3885; Tnp2.
DR eggNOG; KOG4566; Eukaryota.
DR InParanoid; P11101; -.
DR PRO; PR:P11101; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0007340; P:acrosome reaction; ISO:RGD.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0007341; P:penetration of zona pellucida; ISO:RGD.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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; 2.
DR PROSITE; PS00970; TP2_1; 1.
DR PROSITE; PS00971; TP2_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Metal-binding; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis; Zinc.
FT CHAIN 1..114
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191433"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:10961985,
FT ECO:0000269|PubMed:17682055"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..114
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:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:1930189,
FT ECO:0000269|PubMed:8076694"
FT MOD_RES 101
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:11772016"
FT MOD_RES 109
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:11772016"
FT MUTAGEN 12
FT /note="H->Q: 50% loss of zinc binding; when associated with
FT Q-14; Q-16 and Q-24."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 14
FT /note="H->Q: 50% loss of zinc binding; when associated with
FT Q-12; Q-16 and Q-24."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 16
FT /note="H->Q: 50% loss of zinc binding; when associated with
FT Q-12; Q-14 and Q-24."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 24
FT /note="H->Q: 50% loss of zinc binding; when associated with
FT Q-12; Q-14 and Q-16."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 29
FT /note="C->A: 50% loss of zinc binding and loss of nucleolar
FT localization; when associated with A-31; A-35 and A-38."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 31
FT /note="C->A: 50% loss of zinc binding and loss of nucleolar
FT localization; when associated with A-29; A-35 and A-38."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 35
FT /note="C->A: 50% loss of zinc binding and loss of nucleolar
FT localization; when associated with A-29; A-31 and A-38."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 38
FT /note="C->A: 50% loss of zinc binding and loss of nucleolar
FT localization; when associated with A-29; A-31 and A-35."
FT /evidence="ECO:0000269|PubMed:10961985"
FT MUTAGEN 68
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:11772016"
FT MUTAGEN 90
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:11772016"
FT MUTAGEN 101
FT /note="T->A: Slight decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:11772016"
FT MUTAGEN 108
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:11772016"
FT MUTAGEN 109
FT /note="S->A: Large decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:11772016"
FT CONFLICT 1..8
FT /note="MDTKMQSL -> MGGHTRRGRA (in Ref. 1; CAA32882)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> S (in Ref. 4; AAH78849)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="S -> SV (in Ref. 3; CAA87064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 114 AA; 12848 MW; E9EFAF3BE3FC1A7C CRC64;
MDTKMQSLPT THPHPHSSSR PQSHTNNQCA CSHHCRSCSQ AGHPSSSSSP SPGPPTKHPK
TPMHSRYSPS RPSHRGSCPK NRKTLEGKVS KRKAVRRRKR THRAKRRSSG RRYK
