ID   HSP1_BOLBR              Reviewed;         107 AA.
AC   P83211;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Sperm protamine P1;
DE   Flags: Precursor;
OS   Bolinus brandaris (Purple dye murex) (Murex brandaris).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Muricoidea; Muricidae; Bolinus.
OX   NCBI_TaxID=179646 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP   SER-42, AND MASS SPECTROMETRY.
RC   TISSUE=Gonad, and Sperm;
RX   PubMed=9872998; DOI=10.1074/jbc.274.2.649;
RA   Caceres C., Gimenez-Bonafe P., Ribes E., Wouters-Tyrou D., Martinage A.,
RA   Kouach M., Sautiere P., Muller S., Palau J., Subirana J.A., Cornudella L.,
RA   Chiva M.;
RT   "DNA-interacting proteins in the spermiogenesis of the mollusc Murex
RT   brandaris.";
RL   J. Biol. Chem. 274:649-656(1999).
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:9872998}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9872998}. Chromosome
CC       {ECO:0000269|PubMed:9872998}.
CC   -!- TISSUE SPECIFICITY: Gonads. {ECO:0000269|PubMed:9872998}.
CC   -!- PTM: A series of N-terminal cleavages yield the mature protein.
CC       {ECO:0000269|PubMed:9872998}.
CC   -!- PTM: Only the mature protein is phosphorylated.
CC       {ECO:0000269|PubMed:9872998}.
CC   -!- MASS SPECTROMETRY: Mass=8416; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9872998};
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DR   AlphaFoldDB; P83211; -.
DR   iPTMnet; P83211; -.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chromosome; Developmental protein; Differentiation;
KW   Direct protein sequencing; DNA condensation; DNA-binding; Nucleosome core;
KW   Nucleus; Phosphoprotein; Spermatogenesis.
FT   PROPEP          1..35
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000025827"
FT   CHAIN           36..107
FT                   /note="Sperm protamine P1"
FT                   /id="PRO_0000025828"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..107
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9872998"
SQ   SEQUENCE   107 AA;  12584 MW;  3B1BCE4240A93F2D CRC64;
     ALRKVDRNRF VLDNVTPQPR EAKRYKEEEE FPGHGRRRRR RSKGKGKAKG KGKGKGKRRR
     RRKGKGKGKG KKKGKGRRRR CRRGRGCKKR KGKKGKGRRR RRGKKGK