ID   H1L_MYTTR               Reviewed;         203 AA.
AC   Q05831;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Sperm-specific protein PHI-2B/PHI-3;
DE   Contains:
DE     RecName: Full=Sperm-specific protein PHI-2B;
DE     AltName: Full=PL-II*;
DE     AltName: Full=Sperm-specific linker histone H1-like protein;
DE   Contains:
DE     RecName: Full=Sperm-specific protein PHI-3;
DE     AltName: Full=PL-IV;
DE     AltName: Full=Protamine-like protein PHI-3;
OS   Mytilus trossulus (Blue mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=6551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 146-203, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Sperm;
RX   PubMed=8416927; DOI=10.1016/s0021-9258(18)54133-8;
RA   Carlos S., Hunt D.F., Rocchini C., Arnott D.P., Ausio J.;
RT   "Post-translational cleavage of a histone H1-like protein in the sperm of
RT   Mytilus.";
RL   J. Biol. Chem. 268:195-199(1993).
CC   -!- FUNCTION: Linker histones are implicated in chromatin remodeling and/or
CC       transcriptional regulation during spermiogenesis, the process of
CC       spermatid maturation into spermatozoa. Protamines substitute for
CC       histones in the chromatin of sperm during the haploid phase of
CC       spermatogenesis. They compact sperm DNA into a highly condensed, stable
CC       and inactive complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- TISSUE SPECIFICITY: Sperm. {ECO:0000269|PubMed:8416927}.
CC   -!- PTM: PL-II* and PL-IV are produced by post-translational cleavage of a
CC       common precursor.
CC   -!- MISCELLANEOUS: The sequence of variant I is shown.
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DR   EMBL; L02875; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L02876; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A45317; A45317.
DR   PIR; B45317; B45317.
DR   AlphaFoldDB; Q05831; -.
DR   SMR; Q05831; -.
DR   PRIDE; Q05831; -.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; Developmental protein; Differentiation;
KW   Direct protein sequencing; DNA condensation; DNA-binding; Nucleosome core;
KW   Nucleus; Spermatogenesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..145
FT                   /note="Sperm-specific protein PHI-2B"
FT                   /id="PRO_0000013164"
FT   CHAIN           146..203
FT                   /note="Sperm-specific protein PHI-3"
FT                   /id="PRO_0000013165"
FT   DOMAIN          41..120
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          104..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..36
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..203
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         40
FT                   /note="V -> A (in variant 2)"
FT   VARIANT         44
FT                   /note="S -> T (in variant 2)"
FT   VARIANT         103
FT                   /note="P -> L (in variant 2)"
FT   VARIANT         140
FT                   /note="K -> KKSK (in variant 2)"
FT   VARIANT         153
FT                   /note="R -> K (in variant 2)"
SQ   SEQUENCE   203 AA;  21602 MW;  AAF0865CC6D942D5 CRC64;
     MPSPSRKSRS RSRSRSKSPK RSPAKKARKT PKKPRAAGGV KKPSTLSMIV AAITAMKNRK
     GSSVQAIRKY ILANNKGINT SHLGSAMKLA FAKGLKSGVL VRPKTSAGAS GATGSFRVGK
     APASPKKAKK AKSPKKKSSK NKSNNAKAKK SPRKKAAVKK STKSKAKKPK SPKKKAAKKT
     ARKSPKKKAR KSPKKKAAKK SKK