H1_ANAPL
ID H1_ANAPL Reviewed; 218 AA.
AC P09426;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Histone H1;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2822942; DOI=10.1007/bf02603121;
RA Toenjes R., Doenecke D.;
RT "A highly conserved sequence in H1 histone genes as an oligonucleotide
RT hybridization probe: isolation and sequence of a duck H1 gene.";
RL J. Mol. Evol. 25:361-370(1987).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X06128; CAA29495.1; -; Genomic_DNA.
DR AlphaFoldDB; P09426; -.
DR SMR; P09426; -.
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: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 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Nucleus.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..218
FT /note="Histone H1"
FT /id="PRO_0000195926"
FT DOMAIN 37..110
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..162
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P09987"
SQ SEQUENCE 218 AA; 21831 MW; C874C7ED8A0CB4E1 CRC64;
MSETAPVAAP AVSAPGAKAA GKKPKKAAGG SKARKPAGPS VTELITKAVA ASKERKGLSL
AALKKALAAG GYDVEKNNSR IKLGLKSLVG KGTLVQTKGT GASGSFKLNK KPGETKEKAT
KKKPAAKPKK PAAKKPASAA KKPKKAAAVK KSPKKAKKPA AAATKKAAKS PKKAAKAGRP
KKAAKSPAKA KAVKPKAAKP KAAKPKAAKA KKAAPKKK