ID   PRT2_SCOSC              Reviewed;          35 AA.
AC   P83265;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Sperm protamine alpha isoform 2;
DE   AltName: Full=Scombrine alpha-2;
OS   Scomber scombrus (Atlantic mackerel) (Scomber vernalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Scomber.
OX   NCBI_TaxID=13677 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-35, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND PHOSPHORYLATION AT SER-9 AND SER-21.
RC   TISSUE=Sperm;
RX   PubMed=9530815; DOI=10.1016/s0305-0491(97)00297-6;
RA   Buesa C., del Valle L., Saperas N., Goethals M., Lloris D., Chiva M.;
RT   "Primary structure of scombrine alpha: two different species with an
RT   identical protamine.";
RL   Comp. Biochem. Physiol. 119B:145-149(1998).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY OF UNPHOSPHORYLATED FORM.
RA   Buesa C., del Valle L., Saperas N., Goethals M., Lloris D., Chiva M.;
RL   Unpublished observations (JAN-2002).
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:9530815}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9530815}. Chromosome
CC       {ECO:0000269|PubMed:9530815}.
CC   -!- TISSUE SPECIFICITY: Gonads. {ECO:0000269|PubMed:9530815}.
CC   -!- PTM: Phosphorylated in immature sperm. Dephosphorylated in mature sperm
CC       allowing a stronger interaction with DNA. {ECO:0000269|PubMed:9530815}.
CC   -!- MASS SPECTROMETRY: Mass=4551.3; Method=Electrospray;
CC       Note=Unphosphorylated.; Evidence={ECO:0000269|Ref.2};
CC   -!- MISCELLANEOUS: Two isoforms exist, a major form and a minor form. This
CC       is the minor form. {ECO:0000269|PubMed:9530815}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P83265; -.
DR   iPTMnet; P83265; -.
DR   GO; GO:0000786; C:nucleosome; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; TAS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; TAS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9530815"
FT   PEPTIDE         2..35
FT                   /note="Sperm protamine alpha isoform 2"
FT                   /id="PRO_0000044849"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9530815"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9530815"
SQ   SEQUENCE   35 AA;  4679 MW;  BF0B20F5B011C3C8 CRC64;
     MPRRRRRASR PIRRRRRARR STAVRRRRRV VRRRR