PRM2_MACNE
ID PRM2_MACNE Reviewed; 103 AA.
AC P35298;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protamine-2;
DE AltName: Full=Sperm histone P2;
DE AltName: Full=Sperm protamine P2;
GN Name=PRM2;
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545;
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; X71340; CAA50480.1; -; Genomic_DNA.
DR PIR; S33337; S33337.
DR RefSeq; XP_011715771.1; XM_011717469.1.
DR AlphaFoldDB; P35298; -.
DR STRING; 9545.ENSMNEP00000009009; -.
DR Ensembl; ENSMNET00000033177; ENSMNEP00000009007; ENSMNEG00000028974.
DR GeneTree; ENSGT00940000163619; -.
DR OMA; PCAPIPG; -.
DR OrthoDB; 1595135at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000028974; Expressed in multicellular organism.
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; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..103
FT /note="Protamine-2"
FT /id="PRO_0000191603"
FT REGION 1..103
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 49..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"
SQ SEQUENCE 103 AA; 13241 MW; C5F8C29963F3B0B8 CRC64;
MVRYRMRSLS ERPHEVHGQQ VHGQDQGHNG QEEQGLNPEH VEVYERTHRG HSHHRRRRCS
RRRLHRIHRR RHRSCRRRRR RSCRHRRRHR RGCRTRRRRC RRH
