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H1L2_OSTED
ID   H1L2_OSTED              Reviewed;         126 AA.
AC   Q86QI0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Sperm-specific H1/protamine-like protein type 2;
DE   Contains:
DE     RecName: Full=Sperm-specific protein OE2;
DE     AltName: Full=Sperm-specific linker histone H1-like protein OE2;
DE   Contains:
DE     RecName: Full=Sperm-specific protein OE3;
DE     AltName: Full=Protamine-like OS3;
DE   Flags: Precursor; Fragment;
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:AAO16248.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-70, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Sperm {ECO:0000312|EMBL:AAO16248.1};
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: OE2 and OE3 are produced by post-translational cleavage of a
CC       common precursor. {ECO:0000269|PubMed:14732486}.
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DR   EMBL; AY182774; AAO16248.1; -; mRNA.
DR   AlphaFoldDB; Q86QI0; -.
DR   SMR; Q86QI0; -.
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:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; 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..112
FT                   /note="Sperm-specific protein OE2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000013162"
FT   CHAIN           113..>126
FT                   /note="Sperm-specific protein OE3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000013163"
FT   DOMAIN          5..84
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          74..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..116
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        53
FT                   /note="L -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="V -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="L -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="T -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAO16248.1"
FT   NON_TER         126
FT                   /evidence="ECO:0000312|EMBL:AAO16248.1"
SQ   SEQUENCE   126 AA;  13007 MW;  134F7D27790C222A CRC64;
     AGGVKKPTTL SMIVAAITAM KNRKGSSVQA IRKYILANNK GINTSHLGSA MKLAFAKGLK
     SGVLVRLKTS AGASGATGSF RVGKAPASPK KAKKAKSPKK KSSKKSKNKS NNAKAKKSPK
     KKADSN
 
 
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