ID   H1FNT_RAT               Reviewed;         418 AA.
AC   Q5RKG3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Testis-specific H1 histone;
DE   AltName: Full=Haploid germ cell-specific nuclear protein 1;
DE   AltName: Full=Histone H1.7 {ECO:0000250|UniProtKB:Q75WM6};
DE   AltName: Full=Histone H1t2;
GN   Name=H1-7 {ECO:0000250|UniProtKB:Q75WM6};
GN   Synonyms=H1f7 {ECO:0000312|RGD:1560024}, H1fnt {ECO:0000312|RGD:1560024},
GN   Hanp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Essential for normal spermatogenesis and male fertility.
CC       Required for proper cell restructuring and DNA condensation during the
CC       elongation phase of spermiogenesis. Involved in the histone-protamine
CC       transition of sperm chromatin and the subsequent production of
CC       functional sperm. Binds both double-stranded and single-stranded DNA,
CC       ATP and protamine-1. {ECO:0000250|UniProtKB:Q8CJI4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8CJI4}.
CC       Chromosome {ECO:0000250|UniProtKB:Q8CJI4}. Note=In round and elongating
CC       spermatids, specifically localizes to a chromatin domain at the apical
CC       pole. {ECO:0000250|UniProtKB:Q8CJI4}.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000305}.
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DR   EMBL; BC085950; AAH85950.1; -; mRNA.
DR   RefSeq; NP_001019527.1; NM_001024356.1.
DR   AlphaFoldDB; Q5RKG3; -.
DR   SMR; Q5RKG3; -.
DR   STRING; 10116.ENSRNOP00000046187; -.
DR   iPTMnet; Q5RKG3; -.
DR   PhosphoSitePlus; Q5RKG3; -.
DR   PaxDb; Q5RKG3; -.
DR   PRIDE; Q5RKG3; -.
DR   Ensembl; ENSRNOT00000046402; ENSRNOP00000046187; ENSRNOG00000029545.
DR   GeneID; 500928; -.
DR   KEGG; rno:500928; -.
DR   UCSC; RGD:1560024; rat.
DR   CTD; 70069; -.
DR   RGD; 1560024; H1f7.
DR   eggNOG; ENOG502S7R2; Eukaryota.
DR   GeneTree; ENSGT00730000111596; -.
DR   HOGENOM; CLU_657149_0_0_1; -.
DR   InParanoid; Q5RKG3; -.
DR   OMA; FRVWKIS; -.
DR   OrthoDB; 1487385at2759; -.
DR   TreeFam; TF338403; -.
DR   PRO; PR:Q5RKG3; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000029545; Expressed in testis and 2 other tissues.
DR   GO; GO:0000785; C:chromatin; ISS:HGNC.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   GO; GO:0035092; P:sperm DNA condensation; ISS:HGNC.
DR   GO; GO:0007290; P:spermatid nucleus elongation; ISS:HGNC.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromosome; Coiled coil; Developmental protein;
KW   Differentiation; DNA condensation; DNA-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis.
FT   CHAIN           1..418
FT                   /note="Testis-specific H1 histone"
FT                   /id="PRO_0000343416"
FT   REGION          114..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          292..330
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        133..174
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..211
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   418 AA;  47073 MW;  9E66642D9B838588 CRC64;
     MAEAAQPTGE SQGAELTIQI QQPVERALRT PVRRGAQSVL RVSQLLLRAI AGHQRLTLAA
     LKKELGNAGY EVRRKISSHQ AGDSTRSEKY TLLRVSGSDA AGYFRVWKIS KPRRKAPRSR
     LTLGSHSHGK TVLKSPRPLR PRSRRKAAKK AREVWRRKAR ALKARSRRAR SLARSMVRSR
     ASSRASSRAR SRARSRARSR ARSRARSRAS SRARSSARSS ARSSARSSVR SSVRSSARSS
     ARSSIRSRAR SRARTRARSR AKDLVRSKAR EQARTRAREQ AHARARTHDC VRAKAQEYVR
     AKEQQYVSAK EQEYVRTKEQ ECAKAREQMR IGAMEEARIK AIDNRVQTTM EDTSPWSTDE
     MRSRTKPREE KRQEPERPVK QTNQKPAVVK VDNAPSRQGK TCTKSSTKSG HPGCSGTS