STP2_MOUSE
ID STP2_MOUSE Reviewed; 117 AA.
AC P11378; Q91XK4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nuclear transition protein 2;
DE Short=TP-2;
DE Short=TP2;
GN Name=Tnp2 {ECO:0000312|MGI:MGI:98785};
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 [GENOMIC DNA].
RX PubMed=2249785; DOI=10.1016/0378-1119(90)90376-3;
RA Kleene K.C., Gerstel J., Shih D.;
RT "Nucleotide sequence of the gene encoding mouse transition protein 2.";
RL Gene 95:301-302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3693351; DOI=10.1016/s0021-9258(18)45373-2;
RA Kleene K.C., Flynn J.F.;
RT "Characterization of a cDNA clone encoding a basic protein, TP2, involved
RT in chromatin condensation during spermiogenesis in the mouse.";
RL J. Biol. Chem. 262:17272-17277(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C129;
RX PubMed=8720108;
RX DOI=10.1002/(sici)1098-2795(199601)43:1<1::aid-mrd1>3.0.co;2-w;
RA Schlueter G., Celik A.B., Obata R., Schlicker M., Hofferbert S.,
RA Schlung A., Adham I.M., Engel W.;
RT "Sequence analysis of the conserved protamine gene cluster shows that it
RT contains a fourth expressed gene.";
RL Mol. Reprod. Dev. 43:1-6(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15163613; DOI=10.1095/biolreprod.104.028191;
RA Zhao M., Shirley C.R., Mounsey S., Meistrich M.L.;
RT "Nucleoprotein transitions during spermiogenesis in mice with transition
RT nuclear protein Tnp1 and Tnp2 mutations.";
RL Biol. Reprod. 71:1016-1025(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15189834; DOI=10.1095/biolreprod.104.029363;
RA Shirley C.R., Hayashi S., Mounsey S., Yanagimachi R., Meistrich M.L.;
RT "Abnormalities and reduced reproductive potential of sperm from Tnp1- and
RT Tnp2-null double mutant mice.";
RL Biol. Reprod. 71:1220-1229(2004).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15083521; DOI=10.1002/gene.20019;
RA Zhao M., Shirley C.R., Hayashi S., Marcon L., Mohapatra B., Suganuma R.,
RA Behringer R.R., Boissonneault G., Yanagimachi R., Meistrich M.L.;
RT "Transition nuclear proteins are required for normal chromatin condensation
RT and functional sperm development.";
RL Genesis 38:200-213(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
CC -!- FUNCTION: Plays a key role in the replacement of histones to protamine
CC in the elongating spermatids of mammals (PubMed:15163613,
CC PubMed:15189834, PubMed:15083521, PubMed:28366643). In condensing
CC spermatids, loaded onto the nucleosomes, where it promotes the
CC recruitment and processing of protamines, which are responsible for
CC histone eviction (PubMed:28366643). The histone H2AB1-H2BC1/TH2B dimer
CC is required for loading of TNP2 onto chromatin (PubMed:28366643).
CC {ECO:0000269|PubMed:15083521, ECO:0000269|PubMed:15163613,
CC ECO:0000269|PubMed:15189834, ECO:0000269|PubMed:28366643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15163613}. Chromosome
CC {ECO:0000269|PubMed:28366643}. Note=Loaded onto the nucleosomes of
CC condensing spermatids (PubMed:28366643). Inclusion of the H2AB1-
CC H2BC1/TH2B dimer into chromatin opens the nucleosomes, releasing the
CC nucleosomal DNA ends and allowing the invasion of nucleosomes by
CC transition protein TNP2 (PubMed:28366643). Nuclear import is mediated
CC by IPO4. Nucleolar localization requires the protein to be
CC phosphorylated (By similarity). {ECO:0000250|UniProtKB:P11101,
CC ECO:0000269|PubMed:28366643}.
CC -!- DEVELOPMENTAL STAGE: Appears in elongating/condensing spermatids when
CC histones are still detectable (PubMed:15163613). Coexpressed with H2ab1
CC during late spermiogenesis (PubMed:28366643).
CC {ECO:0000269|PubMed:15163613, ECO:0000269|PubMed:28366643}.
CC -!- DISRUPTION PHENOTYPE: Male mice lacking both Tnp1 and Tnp2 are
CC completely infertile, but protamine alone are capable of histone
CC eviction (PubMed:15163613, PubMed:15189834, PubMed:15083521). A
CC significant proportion of Prm2 remains unprocessed (PubMed:15163613,
CC PubMed:15189834, PubMed:15083521). Chromatin in mature spermatozoa
CC shows defects in density (PubMed:15189834, PubMed:15083521).
CC {ECO:0000269|PubMed:15083521, ECO:0000269|PubMed:15163613,
CC ECO:0000269|PubMed:15189834}.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40468.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60254; AAA40469.1; -; Genomic_DNA.
DR EMBL; J03494; AAA40467.1; -; mRNA.
DR EMBL; J03494; AAA40468.1; ALT_INIT; mRNA.
DR EMBL; Z47352; CAA87413.1; -; Genomic_DNA.
DR EMBL; AK005689; BAB24187.1; -; mRNA.
DR EMBL; CT010583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97324.1; -; Genomic_DNA.
DR EMBL; BC092529; AAH92529.1; -; mRNA.
DR CCDS; CCDS27953.1; -.
DR PIR; S14529; S14529.
DR RefSeq; NP_038722.3; NM_013694.4.
DR AlphaFoldDB; P11378; -.
DR STRING; 10090.ENSMUSP00000053078; -.
DR iPTMnet; P11378; -.
DR PhosphoSitePlus; P11378; -.
DR PaxDb; P11378; -.
DR PRIDE; P11378; -.
DR ProteomicsDB; 254593; -.
DR Antibodypedia; 65957; 130 antibodies from 20 providers.
DR DNASU; 21959; -.
DR Ensembl; ENSMUST00000051297; ENSMUSP00000053078; ENSMUSG00000043050.
DR GeneID; 21959; -.
DR KEGG; mmu:21959; -.
DR UCSC; uc007yee.1; mouse.
DR CTD; 7142; -.
DR MGI; MGI:98785; Tnp2.
DR VEuPathDB; HostDB:ENSMUSG00000043050; -.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00390000008176; -.
DR InParanoid; P11378; -.
DR OMA; RPQSHTC; -.
DR BioGRID-ORCS; 21959; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tnp2; mouse.
DR PRO; PR:P11378; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P11378; protein.
DR Bgee; ENSMUSG00000043050; Expressed in seminiferous tubule of testis and 38 other tissues.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IGI:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IGI:MGI.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR GO; GO:0010954; P:positive regulation of protein processing; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
DR InterPro; IPR000678; TP2.
DR PANTHER; PTHR17488; PTHR17488; 1.
DR Pfam; PF01254; TP2; 2.
DR PROSITE; PS00970; TP2_1; 1.
DR PROSITE; PS00971; TP2_2; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Zinc.
FT CHAIN 1..117
FT /note="Nuclear transition protein 2"
FT /id="PRO_0000191428"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 90..98
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11101"
FT CONFLICT 111
FT /note="S -> T (in Ref. 1; AAA40469, 2; AAA40467/AAA40468
FT and 3; CAA87413)"
SQ SEQUENCE 117 AA; 13117 MW; F5692E66E5F3F2CA CRC64;
MDTKMQSLPT THPHPHSSSR PQSHTSNQCN QCTCSHHCRS CSQAGHAGSS SSPSPGPPMK
HPKPSVHSRH SPARPSHRGS CPKNRKTFEG KVSKRKAVRR RKRTHRAKRR SSGRRYK
