ID   HSP1_BOVIN              Reviewed;          51 AA.
AC   P02318;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Sperm protamine P1;
DE   AltName: Full=Cysteine-rich protamine;
GN   Name=PRM1; Synonyms=PRM-1;
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].
RX   PubMed=3829889; DOI=10.1089/dna.1987.6.47;
RA   Krawetz S.A., Connor W., Dixon G.H.;
RT   "Cloning of bovine P1 protamine cDNA and the evolution of vertebrate P1
RT   protamines.";
RL   DNA 6:47-57(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2436637; DOI=10.1515/bchm3.1987.368.1.131;
RA   Lee C.-H., Mansouri A., Hecht W., Hecht N.B., Engel W.;
RT   "Nucleotide sequence of a bovine protamine cDNA.";
RL   Biol. Chem. Hoppe-Seyler 368:131-135(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3335501; DOI=10.1016/s0021-9258(19)57395-1;
RA   Krawetz S.A., Connor W., Dixon G.H.;
RT   "Bovine protamine genes contain a single intron. The structures of the two
RT   alleles.";
RL   J. Biol. Chem. 263:321-326(1988).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-51.
RX   PubMed=4675900; DOI=10.1016/0005-2795(72)90174-2;
RA   Coelingh J.P., Monfoort C.H., Rozijn T.H., Gevers Leuven J.A., Schiphof R.,
RA   Steyn-Parve E.P., Braunitzer G., Schrank B., Ruhfus A.;
RT   "The complete amino acid sequence of the basic nuclear protein of bull
RT   spermatozoa.";
RL   Biochim. Biophys. Acta 285:1-14(1972).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-51.
RX   PubMed=3730390; DOI=10.1016/0167-4838(86)90141-x;
RA   Mazrimas J.A., Corzett M., Campos C., Balhorn R.;
RT   "A corrected primary sequence for bull protamine.";
RL   Biochim. Biophys. Acta 872:11-15(1986).
RN   [6]
RP   DISULFIDE BONDS.
RX   PubMed=1988019; DOI=10.1021/bi00215a026;
RA   Balhorn R., Corzett M., Mazrimas J., Watkins B.;
RT   "Identification of bull protamine disulfides.";
RL   Biochemistry 30:175-181(1991).
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   -!- SUBUNIT: Cross-linked by interchain disulfide bonds around the DNA-
CC       helix.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- PTM: Phosphorylated by SRPK1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protamine P1 family. {ECO:0000305}.
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DR   EMBL; M14559; AAA30741.1; -; mRNA.
DR   EMBL; M18625; AAA30742.1; -; mRNA.
DR   EMBL; M18396; AAA30735.1; -; Genomic_DNA.
DR   EMBL; M18395; AAA30736.1; -; Genomic_DNA.
DR   PIR; A29911; HSBOS.
DR   RefSeq; NP_776581.1; NM_174156.2.
DR   AlphaFoldDB; P02318; -.
DR   PaxDb; P02318; -.
DR   PRIDE; P02318; -.
DR   GeneID; 281423; -.
DR   KEGG; bta:281423; -.
DR   CTD; 5619; -.
DR   HOGENOM; CLU_214580_1_0_1; -.
DR   Proteomes; UP000009136; Unplaced.
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:0035092; P:sperm DNA condensation; IEA:InterPro.
DR   InterPro; IPR000221; Protamine_P1.
DR   Pfam; PF00260; Protamine_P1; 1.
DR   PROSITE; PS00048; PROTAMINE_P1; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; DNA condensation; DNA-binding;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Spermatogenesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3730390,
FT                   ECO:0000269|PubMed:4675900"
FT   CHAIN           2..51
FT                   /note="Sperm protamine P1"
FT                   /evidence="ECO:0000269|PubMed:3730390,
FT                   ECO:0000269|PubMed:4675900"
FT                   /id="PRO_0000191451"
FT   DISULFID        6
FT                   /note="Interchain (with C-23)"
FT                   /evidence="ECO:0000269|PubMed:1988019"
FT   DISULFID        7..15
FT                   /evidence="ECO:0000269|PubMed:1988019"
FT   DISULFID        23
FT                   /note="Interchain (with C-6)"
FT                   /evidence="ECO:0000269|PubMed:1988019"
FT   DISULFID        39
FT                   /note="Interchain (with C-39)"
FT                   /evidence="ECO:0000269|PubMed:1988019"
FT   DISULFID        40..48
FT                   /evidence="ECO:0000269|PubMed:1988019"
FT   CONFLICT        30
FT                   /note="F -> S (in Ref. 2; AAA30742)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40..42
FT                   /note="Missing (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   51 AA;  6758 MW;  9B2A10843B92E2C7 CRC64;
     MARYRCCLTH SGSRCRRRRR RRCRRRRRRF GRRRRRRVCC RRYTVIRCTR Q