ID   PRM2_RAT                Reviewed;         104 AA.
AC   P11248;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protamine-2;
DE   AltName: Full=Sperm histone P2;
DE   AltName: Full=Sperm protamine P2;
GN   Name=Prm2;
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 [GENOMIC DNA].
RC   STRAIN=Fischer;
RX   PubMed=2740236; DOI=10.1093/nar/17.11.4395;
RA   Tanhauser S.M., Hecht N.B.;
RT   "Nucleotide sequence of the rat protamine 2 gene.";
RL   Nucleic Acids Res. 17:4395-4395(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wistar; TISSUE=Spleen;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10 AND SER-33, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; X14674; CAA32804.1; -; Genomic_DNA.
DR   EMBL; Z46939; CAA87062.1; -; Genomic_DNA.
DR   PIR; S57666; S57666.
DR   RefSeq; NP_037005.1; NM_012873.1.
DR   AlphaFoldDB; P11248; -.
DR   STRING; 10116.ENSRNOP00000003450; -.
DR   iPTMnet; P11248; -.
DR   PhosphoSitePlus; P11248; -.
DR   PaxDb; P11248; -.
DR   PRIDE; P11248; -.
DR   Ensembl; ENSRNOT00000003450; ENSRNOP00000003450; ENSRNOG00000002539.
DR   GeneID; 25345; -.
DR   KEGG; rno:25345; -.
DR   UCSC; RGD:3409; rat.
DR   CTD; 5620; -.
DR   RGD; 3409; Prm2.
DR   eggNOG; ENOG502TD5P; Eukaryota.
DR   GeneTree; ENSGT00940000163619; -.
DR   HOGENOM; CLU_175685_0_0_1; -.
DR   InParanoid; P11248; -.
DR   OMA; PCAPIPG; -.
DR   OrthoDB; 1635710at2759; -.
DR   TreeFam; TF338206; -.
DR   PRO; PR:P11248; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002539; Expressed in testis and 7 other tissues.
DR   Genevisible; P11248; RN.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0046870; F:cadmium ion binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR   GO; GO:0007286; P:spermatid development; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR000492; PRM2.
DR   PANTHER; PTHR21341; PTHR21341; 1.
DR   Pfam; PF00841; Protamine_P2; 1.
PE   1: Evidence at protein 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_0000191608"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..91
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        83
FT                   /note="R -> RVSTQ (in Ref. 2; CAA87062)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   104 AA;  13366 MW;  72F0D5B4C3956BB1 CRC64;
     MVRYRMRSPS EGQHQGPGQD HEREEQGQGQ ELSPERVEDY GRTERGHHHR HRRCKRLHRI
     HKRRRSCRRR RRHSCRHRRR HRRGCRRSRR RRSCRCRKCR WHYY