ID   PRM2_CALJA              Reviewed;         104 AA.
AC   Q28337;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protamine-2;
DE   AltName: Full=Sperm histone P2;
DE   AltName: Full=Sperm protamine P2;
GN   Name=PRM2;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=8940659; DOI=10.1111/j.1365-2605.1996.tb00465.x;
RA   Saunders P.T.K., Gaughan J., Saxty B.A., Kerr L.E., Millar M.R.;
RT   "Expression of protamine P2 in the testis of the common marmoset and man
RT   visualized using non-radioactive in-situ hybridization.";
RL   Int. J. Androl. 19:212-219(1996).
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; X85371; CAA59687.1; -; mRNA.
DR   PIR; S53118; S53118.
DR   RefSeq; NP_001244185.1; NM_001257256.1.
DR   AlphaFoldDB; Q28337; -.
DR   STRING; 9483.ENSCJAP00000029529; -.
DR   Ensembl; ENSCJAT00000063031; ENSCJAP00000051954; ENSCJAG00000016052.
DR   GeneID; 100401666; -.
DR   KEGG; cjc:100401666; -.
DR   CTD; 5620; -.
DR   eggNOG; ENOG502TD5P; Eukaryota.
DR   GeneTree; ENSGT00940000163619; -.
DR   InParanoid; Q28337; -.
DR   Proteomes; UP000008225; Chromosome 12.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0046870; F:cadmium ion binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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..104
FT                   /note="Protamine-2"
FT                   /id="PRO_0000191595"
FT   REGION          23..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..104
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"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11248"
SQ   SEQUENCE   104 AA;  13372 MW;  B643DA337EE3D815 CRC64;
     MVRYRVRSPS ERPHEEYRQL VNWQEQGRNG QEEQGLSAEG GEVYGRTHQG YSSYRRRRCS
     RRRRYRIHRR RSRSCRRRRR RSCRYRRRPR RGCRSRRRRR CRRY