H1FNT_MOUSE
ID H1FNT_MOUSE Reviewed; 398 AA.
AC Q8CJI4; Q5GKZ6; Q5RKV2; Q9CVV3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
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|MGI:MGI:1917319},
GN H1fnt {ECO:0000312|MGI:MGI:1917319}, Hanp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16055721; DOI=10.1128/mcb.25.16.7107-7119.2005;
RA Tanaka H., Iguchi N., Isotani A., Kitamura K., Toyama Y., Matsuoka Y.,
RA Onishi M., Masai K., Maekawa M., Toshimori K., Okabe M., Nishimune Y.;
RT "HANP1/H1T2, a novel histone H1-like protein involved in nuclear formation
RT and sperm fertility.";
RL Mol. Cell. Biol. 25:7107-7119(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=15710904; DOI=10.1073/pnas.0406060102;
RA Martianov I., Brancorsini S., Catena R., Gansmuller A., Kotaja N.,
RA Parvinen M., Sassone-Corsi P., Davidson I.;
RT "Polar nuclear localization of H1T2, a histone H1 variant, required for
RT spermatid elongation and DNA condensation during spermiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2808-2813(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-398.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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:0000269|PubMed:15710904,
CC ECO:0000269|PubMed:16055721}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15710904,
CC ECO:0000269|PubMed:16055721}. Chromosome {ECO:0000269|PubMed:15710904,
CC ECO:0000269|PubMed:16055721}. Note=In round and elongating spermatids,
CC specifically localizes to a chromatin domain at the apical pole.
CC {ECO:0000269|PubMed:15710904}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Specifically expressed in haploid
CC germ cells. {ECO:0000269|PubMed:15710904, ECO:0000269|PubMed:16055721}.
CC -!- DEVELOPMENTAL STAGE: First detected in round spermatids at stage 4 and
CC expression strongly increases through stages 5-8. Localization in the
CC nucleus is highly polar and it is concentrated in a cap-like structure
CC at the inner periphery of the nuclear membrane. Polarized expression
CC persists in steps 9-14 elongating spermatids before rapidly
CC disappearing by stage 15. {ECO:0000269|PubMed:15710904}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24570.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB016273; BAC20949.1; -; mRNA.
DR EMBL; AY496853; AAS49491.1; -; mRNA.
DR EMBL; BC052363; AAH52363.1; -; mRNA.
DR EMBL; AK006402; BAB24570.1; ALT_FRAME; mRNA.
DR CCDS; CCDS49721.1; -.
DR RefSeq; NP_081580.2; NM_027304.2.
DR AlphaFoldDB; Q8CJI4; -.
DR SMR; Q8CJI4; -.
DR BioGRID; 213847; 1.
DR IntAct; Q8CJI4; 1.
DR MINT; Q8CJI4; -.
DR STRING; 10090.ENSMUSP00000127616; -.
DR iPTMnet; Q8CJI4; -.
DR PhosphoSitePlus; Q8CJI4; -.
DR PaxDb; Q8CJI4; -.
DR PRIDE; Q8CJI4; -.
DR ProteomicsDB; 269706; -.
DR Antibodypedia; 55622; 31 antibodies from 13 providers.
DR DNASU; 70069; -.
DR Ensembl; ENSMUST00000060855; ENSMUSP00000127616; ENSMUSG00000048077.
DR GeneID; 70069; -.
DR KEGG; mmu:70069; -.
DR UCSC; uc007xmd.2; mouse.
DR CTD; 70069; -.
DR MGI; MGI:1917319; H1f7.
DR VEuPathDB; HostDB:ENSMUSG00000048077; -.
DR eggNOG; ENOG502S7R2; Eukaryota.
DR GeneTree; ENSGT00730000111596; -.
DR HOGENOM; CLU_657149_0_0_1; -.
DR InParanoid; Q8CJI4; -.
DR OMA; FRVWKIS; -.
DR OrthoDB; 1487385at2759; -.
DR TreeFam; TF338403; -.
DR BioGRID-ORCS; 70069; 2 hits in 71 CRISPR screens.
DR ChiTaRS; H1fnt; mouse.
DR PRO; PR:Q8CJI4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CJI4; protein.
DR Bgee; ENSMUSG00000048077; Expressed in seminiferous tubule of testis and 14 other tissues.
DR Genevisible; Q8CJI4; MM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; TAS:MGI.
DR GO; GO:0006997; P:nucleus organization; TAS:MGI.
DR GO; GO:0035092; P:sperm DNA condensation; IMP:UniProtKB.
DR GO; GO:0007290; P:spermatid nucleus elongation; IMP:UniProtKB.
PE 2: Evidence at transcript 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..398
FT /note="Testis-specific H1 histone"
FT /id="PRO_0000343415"
FT REGION 115..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..312
FT /evidence="ECO:0000255"
FT COMPBIAS 137..177
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKG3"
FT CONFLICT 16
FT /note="L -> R (in Ref. 2; AAS49491)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="R -> H (in Ref. 1; BAC20949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44400 MW; 162206F0E2DCFC57 CRC64;
MAEAVQPSGE SQGAELTIQI QQPAERALRT PAKRGTQSVL RVSQLLLRAI AGHQHLTLDA
LKKELGNAGY EVRREISSHH EGKSTRLEKG TLLRVSGSDA AGYFRVWKIS KPREKAGQSR
LTLGSHSSGK TVLKSPRPLR PRSRRKAAKK AREVWRRKAR ALKARSRRVR TRSTSGARSR
TRSRASSRAT SRATSRARSR ARSRAQSSAR SSARSSAKSS AKSSTRSSAK SWARSKARSR
ARSRAKDLVR SKAREQAQAR EQARARAREQ AHARARTQDW VRAKAQEFVS AKEQQYVRAK
EQERAKAREQ VRIGARDEAR IKAKDYNRVR PTKEDTSPRP AEEKSSNSKL REEKGQEPER
PVKQTIQKPA LDNAPSIQGK ACTKSFTKSG QPGDTESP
