HSP1_MOUSE
ID HSP1_MOUSE Reviewed; 51 AA.
AC P02319;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Sperm protamine P1;
DE AltName: Full=Cysteine-rich protamine;
GN Name=Prm1; Synonyms=Prm-1;
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].
RX PubMed=2986684; DOI=10.1021/bi00324a027;
RA Kleene K.C., Distel R.J., Hecht N.B.;
RT "Nucleotide sequence of a cDNA clone encoding mouse protamine 1.";
RL Biochemistry 24:719-722(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=3358932; DOI=10.1016/0167-4781(88)90071-1;
RA Johnson P.A., Pschon J.J., Yelick P.C., Palmiter R.D., Hecht N.B.;
RT "Sequence homologies in the mouse protamine 1 and 2 genes.";
RL Biochim. Biophys. Acta 950:45-53(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3037541; DOI=10.1073/pnas.84.15.5316;
RA Peschon J.J., Behringer R.R., Brinster R.L., Palmiter R.D.;
RT "Spermatid-specific expression of protamine 1 in transgenic mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5316-5319(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3445973; DOI=10.1111/j.1749-6632.1987.tb25000.x;
RA Hecht N.B.;
RT "Gene expression during spermatogenesis.";
RL Ann. N. Y. Acad. Sci. 513:90-101(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C129;
RA Schlueter G., Engel W.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [7]
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 [8]
RP PHOSPHORYLATION BY SRPK1.
RX PubMed=10390541; DOI=10.1093/nar/27.14.2972;
RA Papoutsopoulou S., Nikolakaki E., Chalepakis G., Kruft V., Chevaillier P.,
RA Giannakouros T.;
RT "SR protein-specific kinase 1 is highly expressed in testis and
RT phosphorylates protamine 1.";
RL Nucleic Acids Res. 27:2972-2980(1999).
CC -!- FUNCTION: Protamines substitute for histones in the chromatin of sperm
CC during the haploid phase of spermatogenesis. They compact sperm DNA
CC into a highly condensed, stable and inactive complex.
CC -!- SUBUNIT: Cross-linked by interchain disulfide bonds around the DNA-
CC helix. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- PTM: Phosphorylated by SRPK1. {ECO:0000269|PubMed:10390541}.
CC -!- SIMILARITY: Belongs to the protamine P1 family. {ECO:0000305}.
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DR EMBL; K02926; AAA39980.1; -; mRNA.
DR EMBL; X07625; CAA30472.1; -; Genomic_DNA.
DR EMBL; X14003; CAA32169.1; -; mRNA.
DR EMBL; M27500; AAA39985.1; -; mRNA.
DR EMBL; Z47352; CAA87410.1; -; Genomic_DNA.
DR EMBL; AK007068; BAC25162.1; -; mRNA.
DR EMBL; BC059733; AAH59733.1; -; mRNA.
DR CCDS; CCDS27956.1; -.
DR PIR; I51954; HSMSS1.
DR RefSeq; NP_038665.1; NM_013637.4.
DR AlphaFoldDB; P02319; -.
DR STRING; 10090.ENSMUSP00000023144; -.
DR PhosphoSitePlus; P02319; -.
DR PaxDb; P02319; -.
DR PRIDE; P02319; -.
DR DNASU; 19118; -.
DR Ensembl; ENSMUST00000023144; ENSMUSP00000023144; ENSMUSG00000022501.
DR Ensembl; ENSMUST00000230568; ENSMUSP00000155855; ENSMUSG00000022501.
DR GeneID; 19118; -.
DR KEGG; mmu:19118; -.
DR UCSC; uc007yej.1; mouse.
DR CTD; 5619; -.
DR MGI; MGI:97765; Prm1.
DR VEuPathDB; HostDB:ENSMUSG00000022501; -.
DR GeneTree; ENSGT00900000142796; -.
DR HOGENOM; CLU_214580_2_0_1; -.
DR OMA; MARYICC; -.
DR BioGRID-ORCS; 19118; 2 hits in 55 CRISPR screens.
DR ChiTaRS; Prm1; mouse.
DR PRO; PR:P02319; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P02319; protein.
DR Bgee; ENSMUSG00000022501; Expressed in seminiferous tubule of testis and 46 other tissues.
DR ExpressionAtlas; P02319; baseline and differential.
DR Genevisible; P02319; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; TAS:MGI.
DR GO; GO:0030261; P:chromosome condensation; TAS:MGI.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0035092; P:sperm DNA condensation; IEA:InterPro.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR000221; Protamine_P1.
DR Pfam; PF00260; Protamine_P1; 1.
DR PROSITE; PS00048; PROTAMINE_P1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation; Disulfide bond;
KW DNA condensation; DNA-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..51
FT /note="Sperm protamine P1"
FT /id="PRO_0000191498"
FT DISULFID 6
FT /note="Interchain (with C-22)"
FT /evidence="ECO:0000250|UniProtKB:P02318"
FT DISULFID 7..15
FT /evidence="ECO:0000250|UniProtKB:P02318"
FT DISULFID 22
FT /note="Interchain (with C-6)"
FT /evidence="ECO:0000250|UniProtKB:P02318"
FT DISULFID 37
FT /note="Interchain (with C-37)"
FT /evidence="ECO:0000250|UniProtKB:P02318"
FT DISULFID 38..48
FT /evidence="ECO:0000250|UniProtKB:P02318"
SQ SEQUENCE 51 AA; 6958 MW; B61CD660AD1D7978 CRC64;
MARYRCCRSK SRSRCRRRRR RCRRRRRRCC RRRRRRCCRR RRSYTIRCKK Y
