STP1_RAT
ID STP1_RAT Reviewed; 55 AA.
AC P02317;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Spermatid nuclear transition protein 1;
DE Short=STP-1;
DE Short=TP-1;
DE AltName: Full=Testis-specific basic protein;
GN Name=Tnp1;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2820847; DOI=10.1016/0378-1119(87)90498-7;
RA Heidaran M.A., Kistler W.S.;
RT "Isolation of a cDNA clone for transition protein 1 (TP1), a major
RT chromosomal protein of mammalian spermatids.";
RL Gene 54:281-284(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2524424; DOI=10.1016/0378-1119(89)90381-8;
RA Heidaran M.A., Kozak C.A., Kistler W.S.;
RT "Nucleotide sequence of the Stp-1 gene coding for rat spermatid nuclear
RT transition protein 1 (TP1): homology with protamine P1 and assignment of
RT the mouse Stp-1 gene to chromosome 1.";
RL Gene 75:39-46(1989).
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 PROTEIN SEQUENCE OF 13-55.
RC TISSUE=Testis;
RX PubMed=1112834; DOI=10.1016/s0021-9258(19)41772-9;
RA Kistler W.S., Noyes C., Hsu R., Heinrikson R.L.;
RT "The amino acid sequence of a testis-specific basic protein that is
RT associated with spermatogenesis.";
RL J. Biol. Chem. 250:1847-1853(1975).
RN [5]
RP PROTEIN SEQUENCE OF 2-24.
RC TISSUE=Testis;
RX PubMed=4829397; DOI=10.1016/0006-291x(74)90935-8;
RA Kistler W.S., Noyes C., Heinrikson R.L.;
RT "Partial structural analysis of a highly basic low molecular weight protein
RT from rat testis.";
RL Biochem. Biophys. Res. Commun. 57:341-347(1974).
CC -!- FUNCTION: Plays a key role in the replacement of histones to protamine
CC in the elongating spermatids of mammals. In condensing spermatids,
CC loaded onto the nucleosomes, where it promotes the recruitment and
CC processing of protamines, which are responsible for histone eviction.
CC {ECO:0000250|UniProtKB:P10856}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10856}.
CC Chromosome {ECO:0000250|UniProtKB:P10856}. Note=Loaded onto the
CC nucleosomes of condensing spermatids. {ECO:0000250|UniProtKB:P10856}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the nuclear transition protein 1 family.
CC {ECO:0000305}.
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DR EMBL; X07284; CAA30264.1; -; Genomic_DNA.
DR EMBL; M17096; AAA42260.1; -; mRNA.
DR EMBL; BC078850; AAH78850.1; -; mRNA.
DR PIR; A29095; BGRT.
DR RefSeq; NP_058752.1; NM_017056.2.
DR AlphaFoldDB; P02317; -.
DR STRING; 10116.ENSRNOP00000023769; -.
DR iPTMnet; P02317; -.
DR PhosphoSitePlus; P02317; -.
DR PaxDb; P02317; -.
DR GeneID; 24839; -.
DR KEGG; rno:24839; -.
DR UCSC; RGD:3884; rat.
DR CTD; 7141; -.
DR RGD; 3884; Tnp1.
DR VEuPathDB; HostDB:ENSRNOG00000017611; -.
DR eggNOG; ENOG502TKT1; Eukaryota.
DR HOGENOM; CLU_3019482_0_0_1; -.
DR InParanoid; P02317; -.
DR OMA; FKSHGMR; -.
DR PhylomeDB; P02317; -.
DR TreeFam; TF338391; -.
DR PRO; PR:P02317; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000017611; Expressed in testis and 8 other tissues.
DR Genevisible; P02317; RN.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:RGD.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; ISS:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0007290; P:spermatid nucleus elongation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR InterPro; IPR001319; Nuclear_transition_prot1.
DR InterPro; IPR020062; Nuclear_transition_prot1_CS.
DR PANTHER; PTHR17486; PTHR17486; 1.
DR Pfam; PF02079; TP1; 1.
DR PROSITE; PS00541; TP1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4829397"
FT CHAIN 2..55
FT /note="Spermatid nuclear transition protein 1"
FT /id="PRO_0000191420"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22613"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22613"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22613"
FT CONFLICT 46..48
FT /note="DAS -> SAD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 55 AA; 6395 MW; C371582FD98A7B92 CRC64;
MSTSRKLKTH GMRRGKNRAP HKGVKRGGSK RKYRKSSLKS RKRGDDASRN YRSHL
