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PRM2_BOVIN
ID   PRM2_BOVIN              Reviewed;         115 AA.
AC   P19782; Q02097; Q28171; Q32L38;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Protamine-2;
DE   AltName: Full=Sperm histone P2;
DE   AltName: Full=Sperm protamine P2;
GN   Name=PRM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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], AND ALTERNATIVE SPLICING.
RX   PubMed=1390885; DOI=10.1016/0167-4781(92)90003-i;
RA   Kremling H., Reinhart N., Schlosser M., Engel W.;
RT   "The bovine protamine 2 gene: evidence for alternative splicing.";
RL   Biochim. Biophys. Acta 1132:133-139(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P19782-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P19782-2; Sequence=VSP_021840;
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA42912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X16559; CAA34558.1; -; mRNA.
DR   EMBL; X60353; CAA42913.1; -; Genomic_DNA.
DR   EMBL; X60353; CAA42912.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC109783; AAI09784.1; -; mRNA.
DR   PIR; S28937; S28937.
DR   RefSeq; NP_776582.2; NM_174157.4. [P19782-2]
DR   AlphaFoldDB; P19782; -.
DR   STRING; 9913.ENSBTAP00000037295; -.
DR   PaxDb; P19782; -.
DR   GeneID; 281424; -.
DR   KEGG; bta:281424; -.
DR   CTD; 5620; -.
DR   InParanoid; P19782; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   Alternative splicing; Chromosome; Developmental protein; Differentiation;
KW   DNA condensation; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Spermatogenesis.
FT   CHAIN           1..115
FT                   /note="Protamine-2"
FT                   /id="PRO_0000191594"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..80
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..115
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   VAR_SEQ         79..99
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_021840"
FT   CONFLICT        60..62
FT                   /note="RRP -> A (in Ref. 1; CAA34558)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="R -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="G -> R (in Ref. 2; CAA42913/CAA42912)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   115 AA;  13646 MW;  4749080EF087308C CRC64;
     MVRCHVKSPT ESPPGQQGSG QQGETEHPDQ ARELRPEDIP VYGRTHRGRY HYRHRSHTRR
     RPYRRRRRRA CRHRRRRRGA AGPPCAPIPG TPQASRQGSG CRRMRRRRRR CGRQL
 
 
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