H1L1_OSTED
ID H1L1_OSTED Reviewed; 202 AA.
AC Q86QH9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Sperm-specific H1/protamine-like protein type 1;
DE Contains:
DE RecName: Full=Sperm-specific protein OE1;
DE AltName: Full=Sperm-specific linker histone H1-like protein OE1;
DE Contains:
DE RecName: Full=Sperm-specific protein OE3;
DE AltName: Full=Protamine-like OS3;
DE Flags: Precursor;
OS Ostrea edulis (Native oyster) (European flat oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Ostrea.
OX NCBI_TaxID=37623 {ECO:0000312|EMBL:AAO16249.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Sperm {ECO:0000312|EMBL:AAO16249.1};
RX PubMed=14732486; DOI=10.1016/j.bbaexp.2003.10.004;
RA Agelopoulou B., Cary P.D., Pataryas T., Aleporou-Marinou V.,
RA Crane-Robinson C.;
RT "The sperm-specific proteins of the edible oyster (European flat oyster
RT (Ostrea edulis)) are products of proteolytic processing.";
RL Biochim. Biophys. Acta 1676:12-22(2004).
CC -!- FUNCTION: Linker histones are implicated in chromatin remodeling and/or
CC transcriptional regulation during spermiogenesis, the process of
CC spermatid maturation into spermatozoa. Protamines substitute for
CC histones in the chromatin of sperm during the haploid phase of
CC spermatogenesis. They compact sperm DNA into a highly condensed, stable
CC and inactive complex (By similarity). {ECO:0000250|UniProtKB:P04553,
CC ECO:0000250|UniProtKB:P60008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC -!- TISSUE SPECIFICITY: Sperm. {ECO:0000269|PubMed:14732486}.
CC -!- PTM: OE1 and OE3 are produced by post-translational cleavage of a
CC common precursor. {ECO:0000269|PubMed:14732486}.
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DR EMBL; AY182775; AAO16249.1; -; Genomic_DNA.
DR AlphaFoldDB; Q86QH9; -.
DR SMR; Q86QH9; -.
DR PRIDE; Q86QH9; -.
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:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Developmental protein; Differentiation; DNA condensation;
KW DNA-binding; Nucleosome core; Nucleus; Spermatogenesis.
FT CHAIN 1..148
FT /note="Sperm-specific protein OE1"
FT /id="PRO_0000013160"
FT CHAIN 149..202
FT /note="Sperm-specific protein OE3"
FT /id="PRO_0000013161"
FT DOMAIN 41..120
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..36
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..152
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 21932 MW; FDF1928A41E7D2F2 CRC64;
MPSPSRKSRS RSRSRSKSPK RSPAKKARKT PKKPRAAGGA KKPTTLSMIV AAITAMKNRK
GSSVQAIRKY ILANNKGINT SHLGSAMKLA FAKGLKSGVL VRPKTSAGAS GATGSFRVGK
APASPKKAKK AKSPKKKSSK KSKNKSNNAK AKKSPKKKAD SNGIRYQAYR YRRPRGGARY
PFRYQAYRYR RPRGGPGTQF AL