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H110_CHICK
ID   H110_CHICK              Reviewed;         220 AA.
AC   P08286;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Histone H1.10;
DE   AltName: Full=Methylated DNA-binding protein 2-H1;
DE            Short=MDBP-2-H1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3597432; DOI=10.1016/s0021-9258(18)47984-7;
RA   Coles L.S., Robins A.J., Madley L.K., Wells J.R.E.;
RT   "Characterization of the chicken histone H1 gene complement. Generation of
RT   a complete set of vertebrate H1 protein sequences.";
RL   J. Biol. Chem. 262:9656-9663(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-18; 35-47 AND 66-76, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Black E.J., Gillespie D.A.;
RL   Submitted (JAN-2007) to UniProtKB.
RN   [3]
RP   IDENTIFICATION OF ALA-14.
RX   PubMed=9396815; DOI=10.1093/nar/25.24.5052;
RA   Schwarz S., Hess D., Jost J.-P.;
RT   "The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1
RT   subtypes which are truncated at the C-terminus.";
RL   Nucleic Acids Res. 25:5052-5056(1997).
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; M17018; AAA48788.1; -; Genomic_DNA.
DR   PIR; A28456; A28456.
DR   RefSeq; NP_001264297.1; NM_001277368.1.
DR   AlphaFoldDB; P08286; -.
DR   SMR; P08286; -.
DR   PaxDb; P08286; -.
DR   Ensembl; ENSGALT00000080917; ENSGALP00000055707; ENSGALG00000031159.
DR   GeneID; 417948; -.
DR   KEGG; gga:417948; -.
DR   CTD; 417948; -.
DR   VEuPathDB; HostDB:geneid_417948; -.
DR   GeneTree; ENSGT00950000183089; -.
DR   InParanoid; P08286; -.
DR   OMA; PTWIEMI; -.
DR   OrthoDB; 1565299at2759; -.
DR   TreeFam; TF313664; -.
DR   PRO; PR:P08286; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000031159; Expressed in granulocyte and 8 other tissues.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
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   Acetylation; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..220
FT                   /note="Histone H1.10"
FT                   /id="PRO_0000195930"
FT   DOMAIN          37..110
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..163
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..220
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   220 AA;  22003 MW;  3A41EF2C00A9088A CRC64;
     MSETAPAAAP AVAAPAAKAA AKKPKKAAGG AKARKPAGPS VTELITKAVS ASKERKGLSL
     AALKKALAAG GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFRLSK KPGEVKEKAP
     RKRTPAAKPK KPAAKKPASA AKKPKKAAAA KKSPKKAKKP AAAATKKAAK SPKKATKAAK
     PKKAATAKSP AKAKAVKPKA AKPKAAKPKA AKAKKAAAKK
 
 
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