ID A0A2K5KZ03_CERAT Unreviewed; 194 AA.
AC A0A2K5KZ03;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histone H1.0 {ECO:0000256|ARBA:ARBA00040426};
DE AltName: Full=Histone H1(0) {ECO:0000256|ARBA:ARBA00043204};
GN Name=H1-0 {ECO:0000313|Ensembl:ENSCATP00000005932.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000005932.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000005932.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037763}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU003894}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC {ECO:0000256|RuleBase:RU003894}.
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DR RefSeq; XP_011893581.1; XM_012038191.1.
DR AlphaFoldDB; A0A2K5KZ03; -.
DR SMR; A0A2K5KZ03; -.
DR STRING; 9531.ENSCATP00000005932; -.
DR Ensembl; ENSCATT00000021674.1; ENSCATP00000005932.1; ENSCATG00000018822.1.
DR GeneID; 105575840; -.
DR KEGG; caty:105575840; -.
DR GeneTree; ENSGT00810000125570; -.
DR OMA; KSTHASY; -.
DR OrthoDB; 5363206at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000018822; Expressed in colon and 12 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:Ensembl.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR11467; HISTONE H1; 1.
DR PANTHER; PTHR11467:SF154; HISTONE H1.0; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|RuleBase:RU003894};
KW Citrullination {ECO:0000256|ARBA:ARBA00022934};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003894};
KW Nucleus {ECO:0000256|RuleBase:RU003894};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 24..97
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 194 AA; 20863 MW; 03ED6F01919F8BE1 CRC64;
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKKSVAFKKT KKEIKKVATP
KKASKPKKAA SKAPTKKPKA TPVKKAKKKL AATPKKAKKP KTVKAKPVKA SKPKKAKPVK
PKAKSSAKRA GKKK
//