ID   H1_PARAN                Reviewed;         248 AA.
AC   P02256;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Histone H1, gonadal;
OS   Parechinus angulosus (Angulate sea urchin) (Cidaris angulosus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Parechinus.
OX   NCBI_TaxID=7658;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-84.
RX   PubMed=6767609; DOI=10.1111/j.1432-1033.1980.tb04459.x;
RA   Strickland W.N., Strickland M., de Groot P.C., von Holt C.,
RA   Wittmann-Liebold B.;
RT   "The primary structure of histone H1 from sperm of the sea urchin
RT   Parechinus angulosus. 1. Chemical and enzymatic fragmentation of the
RT   protein and the sequence of amino acids in the four N-terminal cyanogen
RT   bromide peptides.";
RL   Eur. J. Biochem. 104:559-566(1980).
RN   [2]
RP   PROTEIN SEQUENCE OF 80-248.
RX   PubMed=7363905; DOI=10.1111/j.1432-1033.1980.tb04460.x;
RA   Strickland W.N., Strickland M., Brandt W.F., von Holt C., Lehmann A.,
RA   Wittmann-Liebold B.;
RT   "The primary structure of histone H1 from sperm of the sea urchin
RT   Parechinus angulosus. 2. Sequence of the C-terminal CNBr peptide and the
RT   entire primary structure.";
RL   Eur. J. Biochem. 104:567-578(1980).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC       chains into higher-order structures.
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; A91090; HSUR1P.
DR   AlphaFoldDB; P02256; -.
DR   SMR; P02256; -.
DR   iPTMnet; P02256; -.
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   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Nucleus.
FT   CHAIN           1..248
FT                   /note="Histone H1, gonadal"
FT                   /id="PRO_0000195942"
FT   DOMAIN          41..115
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..39
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..248
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         144
FT                   /note="K -> R"
SQ   SEQUENCE   248 AA;  26387 MW;  1B25B3F136541947 CRC64;
     PGSPQKRAAS PRKSPRKSPK KSPRKASASP RRKAKRARAS THPPVLEMVQ AAITAMKERK
     GSSAAKIKSY MAANYRVDMN VLAPHVRRAL RNGVASGALK QVTGTGASGR FRVGAVAKPK
     KAKKTSAAAK AKKAKAAAAK KARKAKAAAK RKAALAKKKA AAAKRKAAAK AKKAKKPKKK
     AAKKAKKPAK KSPKKAKKPA KKSPKKKKAK RSPKKAKKAA GKRKPAAKKA RRSPRKAGKR
     RSPKKARK