PRM2_PIG
ID PRM2_PIG Reviewed; 92 AA.
AC P19757;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protamine-2;
DE AltName: Full=Sperm histone P2;
DE AltName: Full=Sperm protamine P2;
GN Name=PRM2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=2320417; DOI=10.1093/nar/18.5.1249;
RA Maier W.-M., Nussbaum G., Domenjoud L., Klemm U., Engel W.;
RT "The lack of protamine 2 (P2) in boar and bull spermatozoa is due to
RT mutations within the P2 gene.";
RL Nucleic Acids Res. 18:1249-1254(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1627265; DOI=10.1515/bchm3.1992.373.1.261;
RA Keime S., Heitland K., Kumm S., Schloesser M., Hroch N., Holtz W.,
RA Engel W.;
RT "Characterization of four genes encoding basic proteins of the porcine
RT spermatid nucleus and close linkage of three of them.";
RL Biol. Chem. Hoppe-Seyler 373:261-270(1992).
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; X16558; CAA34557.1; -; mRNA.
DR EMBL; M80676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S13132; S13132.
DR RefSeq; NP_999417.1; NM_214252.1.
DR AlphaFoldDB; P19757; -.
DR STRING; 9823.ENSSSCP00000024012; -.
DR PaxDb; P19757; -.
DR PeptideAtlas; P19757; -.
DR Ensembl; ENSSSCT00015071908; ENSSSCP00015028844; ENSSSCG00015053982.
DR GeneID; 397486; -.
DR KEGG; ssc:397486; -.
DR CTD; 5620; -.
DR eggNOG; ENOG502TD5P; Eukaryota.
DR HOGENOM; CLU_175685_0_0_1; -.
DR InParanoid; P19757; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P19757; SS.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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..92
FT /note="Protamine-2"
FT /id="PRO_0000191610"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
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 CONFLICT 64
FT /note="R -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="R -> W (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 92 AA; 11807 MW; FD30DCC160136A9F CRC64;
MVRCRVRSPS ESPQQGSGQQ RENERQDQDQ ELRPEDVPVY GRTHRGRYHY RHRSHTRRRR
SCRRRRRRAC RHRRHRRGCR RIRRRRRCRR RL