ID   PRT1_ESOLU              Reviewed;          32 AA.
AC   P02325;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Protamine-1;
DE   AltName: Full=Protamine-I;
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6628381; DOI=10.1111/j.1432-1033.1983.tb07739.x;
RA   Speckert W., Kennedy B., Daisley S.L., Davies P.;
RT   "Primary structure of protamine from the Northern pike Esox lucius.";
RL   Eur. J. Biochem. 136:283-289(1983).
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   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- MISCELLANEOUS: The heterogeneity indicates the existence of other
CC       protamines.
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   PIR; A02667; YZPK1.
DR   AlphaFoldDB; P02325; -.
DR   Proteomes; UP000265140; LG25.
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; Reference proteome; Spermatogenesis.
FT   PEPTIDE         1..32
FT                   /note="Protamine-1"
FT                   /id="PRO_0000044832"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         9
FT                   /note="G -> S"
FT   VARIANT         28
FT                   /note="G -> S (in 50% of the molecules)"
SQ   SEQUENCE   32 AA;  4139 MW;  F9AF8FBDF922A5EF CRC64;
     PRRRRASSGR PVRRRRRPKM SRRRRRGGRR RR