ID   PRM2_SEMEN              Reviewed;         103 AA.
AC   Q9GKM1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Protamine-2;
DE   AltName: Full=Sperm histone P2;
DE   AltName: Full=Sperm protamine P2;
GN   Name=PRM2;
OS   Semnopithecus entellus (Northern plains gray langur) (Presbytis entellus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Semnopithecus.
OX   NCBI_TaxID=88029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Karanth P.K., Stewart C.-B., Holt R.A., de Koning J., Messier W.;
RT   "Positive Darwinian selection on the lineage leading to humans.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF195643; AAG42202.1; -; Genomic_DNA.
DR   EMBL; AF195642; AAG42202.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q9GKM1; -.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0007286; P:spermatid development; IEA:InterPro.
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; Spermatogenesis.
FT   CHAIN           1..103
FT                   /note="Protamine-2"
FT                   /id="PRO_0000191609"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..103
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   103 AA;  13304 MW;  51637ACF92393886 CRC64;
     MVRYRMRSLS ERPHEVHGQQ VYGQEQGHNG QEEQGLSPEH VEVYERTHQG YSHHRRRRCS
     RRRLYRIHRR RHRSCRRRRR RSCRHRRRHR RGCRTRRRRC RRY