PRM2_MOUSE
ID PRM2_MOUSE Reviewed; 107 AA.
AC P07978;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protamine-2;
DE AltName: Full=Sperm histone P2;
DE AltName: Full=Sperm protamine P2;
DE Contains:
DE RecName: Full=PP2-A;
DE Contains:
DE RecName: Full=PP2-C;
DE Contains:
DE RecName: Full=PP2-D;
DE Contains:
DE RecName: Full=PP2-B;
DE AltName: Full=Protamine mP2 {ECO:0000303|PubMed:3600661};
GN Name=Prm2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-64.
RX PubMed=3600661; DOI=10.1128/mcb.7.6.2173-2179.1987;
RA Yelick P.C., Balhorn R., Johnson P.A., Corzett M., Mazrimas J.A.,
RA Kleene K.C., Hecht N.B.;
RT "Mouse protamine 2 is synthesized as a precursor whereas mouse protamine 1
RT is not.";
RL Mol. Cell. Biol. 7:2173-2179(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=3358932; DOI=10.1016/0167-4781(88)90071-1;
RA Johnson P.A., Pschon J.J., Yelick P.C., Palmiter R.D., Hecht N.B.;
RT "Sequence homologies in the mouse protamine 1 and 2 genes.";
RL Biochim. Biophys. Acta 950:45-53(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3445973; DOI=10.1111/j.1749-6632.1987.tb25000.x;
RA Hecht N.B.;
RT "Gene expression during spermatogenesis.";
RL Ann. N. Y. Acad. Sci. 513:90-101(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C129;
RA Schlueter G., Engel W.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 45-107.
RX PubMed=3401454; DOI=10.1021/bi00408a034;
RA Bellve A.R., McKay D.J., Renaux B.S., Dixon G.H.;
RT "Purification and characterization of mouse protamines P1 and P2. Amino
RT acid sequence of P2.";
RL Biochemistry 27:2890-2897(1988).
RN [7]
RP PROTEOLYTIC PROCESSING.
RX PubMed=2001695; DOI=10.1111/j.1432-1033.1991.tb15800.x;
RA Elsevier S.M., Noiran J., Carre-Eusebe D.;
RT "Processing of the precursor of protamine P2 in mouse. Identification of
RT intermediates by their insolubility in the presence of sodium dodecyl
RT sulfate.";
RL Eur. J. Biochem. 196:167-175(1991).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1854346; DOI=10.1042/bj2770039;
RA Carre-Eusebe D., Lederer F., Le K.H.D., Elsevier S.M.;
RT "Processing of the precursor of protamine P2 in mouse. Peptide mapping and
RT N-terminal sequence analysis of intermediates.";
RL Biochem. J. 277:39-45(1991).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12620939; DOI=10.1095/biolreprod.102.015115;
RA Cho C., Jung-Ha H., Willis W.D., Goulding E.H., Stein P., Xu Z.,
RA Schultz R.M., Hecht N.B., Eddy E.M.;
RT "Protamine 2 deficiency leads to sperm DNA damage and embryo death in
RT mice.";
RL Biol. Reprod. 69:211-217(2003).
RN [10]
RP INTERACTION WITH TDRP.
RX PubMed=27069551;
RA Mao S., Wu F., Cao X., He M., Liu N., Wu H., Yang Z., Ding Q., Wang X.;
RT "TDRP deficiency contributes to low sperm motility and is a potential risk
RT factor for male infertility.";
RL Am. J. Transl. Res. 8:177-187(2016).
RN [11]
RP FUNCTION, PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
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:0000269|PubMed:12620939, ECO:0000269|PubMed:28366643}.
CC -!- SUBUNIT: Interacts with TDRP. {ECO:0000269|PubMed:27069551}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome
CC {ECO:0000269|PubMed:28366643}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- PTM: Proteolytic processing into mature chains is required for histone
CC eviction during spermatogenesis (PubMed:28366643). Transition proteins
CC (TNP1 and TNP2) are required for processing (PubMed:28366643).
CC {ECO:0000269|PubMed:28366643}.
CC -!- DISRUPTION PHENOTYPE: Male mice are sterile due to reduced compaction
CC of chromatin in sperm. {ECO:0000269|PubMed:12620939}.
CC -!- SIMILARITY: Belongs to the protamine P2 family. {ECO:0000305}.
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DR EMBL; M16456; AAA39981.1; -; mRNA.
DR EMBL; X07626; CAA30473.1; -; Genomic_DNA.
DR EMBL; X14004; CAA32170.1; -; mRNA.
DR EMBL; M27501; AAA39986.1; -; mRNA.
DR EMBL; Z47352; CAA87411.1; -; Genomic_DNA.
DR EMBL; BC049612; AAH49612.1; -; mRNA.
DR CCDS; CCDS27955.1; -.
DR PIR; A27809; A29995.
DR RefSeq; NP_032959.1; NM_008933.2.
DR AlphaFoldDB; P07978; -.
DR STRING; 10090.ENSMUSP00000047925; -.
DR iPTMnet; P07978; -.
DR PhosphoSitePlus; P07978; -.
DR PaxDb; P07978; -.
DR PRIDE; P07978; -.
DR ProteomicsDB; 291660; -.
DR Antibodypedia; 58005; 56 antibodies from 15 providers.
DR DNASU; 19119; -.
DR Ensembl; ENSMUST00000037996; ENSMUSP00000047925; ENSMUSG00000038015.
DR Ensembl; ENSMUST00000189593; ENSMUSP00000139898; ENSMUSG00000038015.
DR GeneID; 19119; -.
DR KEGG; mmu:19119; -.
DR UCSC; uc007yeh.1; mouse.
DR CTD; 5620; -.
DR MGI; MGI:97766; Prm2.
DR VEuPathDB; HostDB:ENSMUSG00000038015; -.
DR eggNOG; ENOG502TD5P; Eukaryota.
DR GeneTree; ENSGT00940000163619; -.
DR HOGENOM; CLU_175685_0_0_1; -.
DR InParanoid; P07978; -.
DR OMA; PCAPIPG; -.
DR OrthoDB; 1635710at2759; -.
DR TreeFam; TF338206; -.
DR BioGRID-ORCS; 19119; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Prm2; mouse.
DR PRO; PR:P07978; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P07978; protein.
DR Bgee; ENSMUSG00000038015; Expressed in seminiferous tubule of testis and 26 other tissues.
DR ExpressionAtlas; P07978; baseline and differential.
DR Genevisible; P07978; MM.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0046870; F:cadmium ion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; TAS:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0030261; P:chromosome condensation; TAS:MGI.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP: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;
KW Direct protein sequencing; DNA condensation; DNA-binding; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..107
FT /note="PP2-A"
FT /evidence="ECO:0000305|PubMed:1854346"
FT /id="PRO_0000025790"
FT CHAIN 12..107
FT /note="PP2-C"
FT /evidence="ECO:0000305|PubMed:1854346"
FT /id="PRO_0000025791"
FT CHAIN 21..107
FT /note="PP2-D"
FT /evidence="ECO:0000305|PubMed:1854346"
FT /id="PRO_0000025792"
FT CHAIN 45..107
FT /note="PP2-B"
FT /evidence="ECO:0000269|PubMed:3401454,
FT ECO:0000305|PubMed:1854346, ECO:0000305|PubMed:3600661"
FT /id="PRO_0000025793"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..94
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 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11248"
SQ SEQUENCE 107 AA; 13638 MW; 66F6C3776D2DC09E CRC64;
MVRYRMRSPS EGPHQGPGQD HEREEQGQGQ GLSPERVEDY GRTHRGHHHH RHRRCSRKRL
HRIHKRRRSC RRRRRHSCRH RRRHRRGCRR SRRRRRCRCR KCRRHHH
