ID   HSP1_OCTVU              Reviewed;          56 AA.
AC   P83214;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Sperm protamine P1;
DE            Short=Po1;
DE   Contains:
DE     RecName: Full=Sperm protamine P2;
DE              Short=Po2;
DE     AltName: Full=Main protamine;
OS   Octopus vulgaris (Common octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=6645 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, PHOSPHORYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Sperm;
RX   PubMed=15095345; DOI=10.1002/mrd.20068;
RA   Gimenez-Bonafe P., Soler F.M., Buesa C., Sautiere P.-E., Ausio J.,
RA   Kouach M., Kasinsky H.E., Chiva M.;
RT   "Chromatin organization during spermiogenesis in Octopus vulgaris. II: DNA-
RT   interacting proteins.";
RL   Mol. Reprod. Dev. 68:232-239(2004).
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:15095345, ECO:0000305}.
CC   -!- FUNCTION: Octopus spermiogenesis is characterized by a double nuclear
CC       protein transition: Histones are first replaced by P1, which allows the
CC       chromatin to adopt a shape that is not as relaxed as with histones. The
CC       majority of P1 is later replaced by P2, forming a compact chromatin. P2
CC       is the main protamine of sperm. {ECO:0000269|PubMed:15095345,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- TISSUE SPECIFICITY: Testis. {ECO:0000305}.
CC   -!- PTM: P2 is phosphorylated in immature sperm. It is dephosphorylated in
CC       mature sperm allowing a stronger interaction with DNA.
CC       {ECO:0000269|PubMed:15095345}.
CC   -!- MASS SPECTROMETRY: [Sperm protamine P1]: Mass=7428;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:15095345,
CC       ECO:0000305};
CC   -!- MASS SPECTROMETRY: [Sperm protamine P2]: Mass=6028;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:15095345,
CC       ECO:0000305};
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DR   AlphaFoldDB; P83214; -.
DR   Proteomes; UP000515154; Genome assembly.
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; Reference proteome; Spermatogenesis.
FT   CHAIN           1..56
FT                   /note="Sperm protamine P1"
FT                   /id="PRO_0000025829"
FT   CHAIN           15..56
FT                   /note="Sperm protamine P2"
FT                   /id="PRO_0000025831"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   56 AA;  7430 MW;  41EFEA8E024A93D6 CRC64;
     RLSRRRVYSI GGRRRRRRRR SRGRRGRRRG RRRGRRRGRR RGRRRRRRRG GRRRRR