HSPL_MULSU
ID HSPL_MULSU Reviewed; 178 AA.
AC Q08GK9; P84802;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Protamine-like protein;
DE Short=PL-I;
GN Name=pl {ECO:0000312|EMBL:CAK95907.1};
OS Mullus surmuletus (Striped red mullet).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Syngnathiaria; Syngnathiformes; Mulloidea; Mullidae; Mullus.
OX NCBI_TaxID=87757;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAK95907.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-178, PROTEIN SEQUENCE OF 1-138, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MASS
RP SPECTROMETRY.
RC TISSUE=Sperm {ECO:0000269|PubMed:16965539}, and
RC Testis {ECO:0000269|PubMed:16965539};
RX PubMed=16965539; DOI=10.1111/j.1742-4658.2006.05461.x;
RA Saperas N., Chiva M., Casas M.T., Campos J.L., Eirin-Lopez J.M.,
RA Frehlick L.J., Prieto C., Subirana J.A., Ausio J.;
RT "A unique vertebrate histone H1-related protamine-like protein results in
RT an unusual sperm chromatin organization.";
RL FEBS J. 273:4548-4561(2006).
CC -!- FUNCTION: Replaces histones in the chromatin of sperm during the
CC haploid phase of spermatogenesis. Compacts sperm DNA into a highly
CC condensed, stable and inactive complex. {ECO:0000269|PubMed:16965539}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837,
CC ECO:0000269|PubMed:16965539}. Chromosome {ECO:0000255|PROSITE-
CC ProRule:PRU00837, ECO:0000269|PubMed:16965539}.
CC -!- TISSUE SPECIFICITY: Male germ cells. {ECO:0000269|PubMed:16965539}.
CC -!- DEVELOPMENTAL STAGE: Expressed during spermiogenesis.
CC {ECO:0000269|PubMed:16965539}.
CC -!- MASS SPECTROMETRY: Mass=20354.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16965539};
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; AM284397; CAK95907.1; -; mRNA.
DR AlphaFoldDB; Q08GK9; -.
DR SMR; Q08GK9; -.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA condensation; DNA-binding; Nucleosome core;
KW Nucleus; Spermatogenesis.
FT CHAIN 1..178
FT /note="Protamine-like protein"
FT /id="PRO_0000263031"
FT DOMAIN 21..89
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..178
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 20391 MW; 9982D18269029B75 CRC64;
PSTTSSKSPK RRAKSPRRKR TGPTVSDLIL MAMSASSDRG GLSLAALKKD LKGRGYDVVR
NKGRVLMAIK RLVANKSVVK AKGFYKLNKN PPTPRRRVAK RKKPKAKRAK RGRKRKAAPK
KKSAKKKRKR RRRKSKSPKK ARKARRAKSP RRARSPRRSK SPRKAKRRTT KTRRRAKK
