H10B_XENLA
ID H10B_XENLA Reviewed; 196 AA.
AC P22844; Q5D034;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Histone H1.0-B;
DE AltName: Full=H1-SA;
DE AltName: Full=H1D;
DE AltName: Full=Histone H1(0)-2;
DE AltName: Full=Histone H5A;
DE AltName: Full=XlH5A;
GN Name=h1-0-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroid cell;
RX PubMed=2907322; DOI=10.1016/0378-1119(88)90110-2;
RA Rutledge R.G., Neelin J.M., Seligy V.L.;
RT "Isolation and expression of cDNA clones coding for two sequence variants
RT of Xenopus laevis histone H5.";
RL Gene 70:117-126(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9161423; DOI=10.1016/s0378-1119(96)00845-1;
RA Brocard M., Triebe S., Peretti M., Doenecke D., Khochbin S.;
RT "Characterization of the two H1(0)-encoding genes from Xenopus laevis.";
RL Gene 189:127-134(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 31-38.
RA Brown G.L.;
RL Thesis (1982), Carleton University / Ottawa, Canada.
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures. The histones H1.0 are found in
CC cells that are in terminal stages of differentiation or that have low
CC rates of cell division (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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 EMBL; M22834; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC068618; AAH68618.1; -; mRNA.
DR EMBL; Z71503; CAA96130.1; -; Genomic_DNA.
DR PIR; JT0403; HSXL5A.
DR PDB; 5NL0; X-ray; 5.40 A; Z=1-196.
DR PDBsum; 5NL0; -.
DR AlphaFoldDB; P22844; -.
DR SMR; P22844; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
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 3D-structure; Chromosome; Direct protein sequencing; DNA condensation;
KW DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..196
FT /note="Histone H1.0-B"
FT /id="PRO_0000196008"
FT DOMAIN 24..97
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..196
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 21062 MW; A0BAE0C3FEAD6B87 CRC64;
MAENSAATPA AKPKRSKALK KSTDHPKYSD MILAAVQAEK SRSGSSRQSI QKYIKNHYKV
GENADSQIKL SIKRLVTSGA LKQTKGVGAS GSFRLAKADE GKKPAKKPKK EIKKAVSPKK
VAKPKKAAKS PAKAKKPKVA EKKVKKVAKK KPAPSPKKAK KTKTVKAKPV RASKVKKAKP
SKPKAKASPK KSGRKK