ID   PRM2_MACMU              Reviewed;         102 AA.
AC   P35297;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Protamine-2;
DE   AltName: Full=Sperm histone P2;
DE   AltName: Full=Sperm protamine P2;
GN   Name=PRM2;
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=8513810; DOI=10.1111/j.1432-1033.1993.tb17960.x;
RA   Retief J.D., Dixon G.H.;
RT   "Evolution of pro-protamine P2 genes in primates.";
RL   Eur. J. Biochem. 214:609-615(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8513810.
RX   PubMed=8281927;
RA   Retief J.D., Dixon G.H.;
RL   Eur. J. Biochem. 218:1095-1095(1993).
CC   -!- FUNCTION: Protamines substitute for histones in the chromatin of sperm
CC       during the haploid phase of spermatogenesis. They compact sperm DNA
CC       into a highly condensed, stable and inactive complex.
CC       {ECO:0000250|UniProtKB:P07978}.
CC   -!- SUBUNIT: Interacts with TDRP. {ECO:0000250|UniProtKB:P07978}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07978}.
CC       Chromosome {ECO:0000250|UniProtKB:P07978}.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- PTM: Proteolytic processing into mature chains is required for histone
CC       eviction during spermatogenesis. Transition proteins (TNP1 and TNP2)
CC       are required for processing. {ECO:0000250|UniProtKB:P07978}.
CC   -!- SIMILARITY: Belongs to the protamine P2 family. {ECO:0000305}.
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DR   EMBL; X71338; CAA50478.1; -; Genomic_DNA.
DR   PIR; S33336; S33336.
DR   AlphaFoldDB; P35297; -.
DR   STRING; 9544.ENSMMUP00000014364; -.
DR   InParanoid; P35297; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0006997; P:nucleus organization; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR000492; PRM2.
DR   PANTHER; PTHR21341; PTHR21341; 1.
DR   Pfam; PF00841; Protamine_P2; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Developmental protein; Differentiation; DNA condensation;
KW   DNA-binding; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Spermatogenesis.
FT   CHAIN           1..102
FT                   /note="Protamine-2"
FT                   /id="PRO_0000191602"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..102
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11248"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11248"
SQ   SEQUENCE   102 AA;  13082 MW;  181C799303A2DEA6 CRC64;
     MVRYRMRSLS ERSHEVHGQQ VHGQDQGHNG QEEQGLNPEH VEVYERTHGH SHYRRRHCSR
     RRLHRIHRRR HRSCRRRRRR SCRHRRRHRR GCRTRRRRCR RH