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H1L_MYTCA
ID   H1L_MYTCA               Reviewed;         148 AA.
AC   P22974;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Sperm-specific protein PHI-2B;
DE   AltName: Full=PL-II*;
DE   AltName: Full=Sperm-specific linker histone H1-like protein;
OS   Mytilus californianus (California mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=6549;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Sperm;
RX   PubMed=7677995; DOI=10.1016/s0021-9258(18)54132-6;
RA   Carlos S., Jutglar L., Borrell I., Hunt D.F., Ausio J.;
RT   "Sequence and characterization of a sperm-specific histone H1-like protein
RT   of Mytilus californianus.";
RL   J. Biol. Chem. 268:185-194(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 35-118.
RC   TISSUE=Sperm;
RX   PubMed=2022636; DOI=10.1016/s0021-9258(18)92959-5;
RA   Jutglar L., Borrell J.I., Ausio J.;
RT   "Primary, secondary, and tertiary structure of the core of a histone H1-
RT   like protein from the sperm of Mytilus.";
RL   J. Biol. Chem. 266:8184-8191(1991).
CC   -!- FUNCTION: Linker histones are implicated in chromatin remodeling and/or
CC       transcriptional regulation during spermiogenesis, the process of
CC       spermatid maturation into spermatozoa. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- TISSUE SPECIFICITY: Sperm.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00837}.
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DR   PIR; A45316; A45316.
DR   AlphaFoldDB; P22974; -.
DR   SMR; P22974; -.
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..148
FT                   /note="Sperm-specific protein PHI-2B"
FT                   /id="PRO_0000196010"
FT   DOMAIN          40..119
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..142
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   148 AA;  15688 MW;  58ACFCE0B03114D3 CRC64;
     PSPSRRSRSR SRSRSKSPKR SPAKKARKTP KKRRATGGAK KPSTLSMIVA AIQAMKNRKG
     SSVQAIRKYI LANNKGINTS RLGSAMKLAF AKGLKSGVLV RPKTSAGASG ATGSFRVGKA
     PSSPKKKAKK AKSPKKKSSK KSSNKSNN
 
 
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