STP1_PIG
ID STP1_PIG Reviewed; 55 AA.
AC P17306;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Spermatid nuclear transition protein 1;
DE Short=STP-1;
DE Short=TP-1;
GN Name=TNP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=2777004; DOI=10.1111/j.1432-0436.1989.tb00597.x;
RA Kremling H., Luerssen H., Abham I.M., Klemm U., Tsaousidou S., Engel W.;
RT "Nucleotide sequences and expression of cDNA clones for boar and bull
RT transition protein 1 and its evolutionary conservation in mammals.";
RL Differentiation 40:184-190(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1627265; DOI=10.1515/bchm3.1992.373.1.261;
RA Keime S., Heitland K., Kumm S., Schloesser M., Hroch N., Holtz W.,
RA Engel W.;
RT "Characterization of four genes encoding basic proteins of the porcine
RT spermatid nucleus and close linkage of three of them.";
RL Biol. Chem. Hoppe-Seyler 373:261-270(1992).
RN [3]
RP PROTEIN SEQUENCE OF 2-55.
RX PubMed=8019440;
RA Akama K., Kojima S., Nakano M., Tobita T., Hayashi H.;
RT "The amino acid sequence and phosphorylation sites of a boar transition
RT protein 1.";
RL Biochem. Mol. Biol. Int. 32:349-357(1994).
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; X16170; CAA34292.1; -; mRNA.
DR EMBL; M80679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S21670; BGPG.
DR RefSeq; XP_003133695.1; XM_003133647.3.
DR AlphaFoldDB; P17306; -.
DR STRING; 9823.ENSSSCP00000017139; -.
DR iPTMnet; P17306; -.
DR PaxDb; P17306; -.
DR PRIDE; P17306; -.
DR Ensembl; ENSSSCT00000017617; ENSSSCP00000017139; ENSSSCG00000016179.
DR Ensembl; ENSSSCT00005018131; ENSSSCP00005010843; ENSSSCG00005011734.
DR Ensembl; ENSSSCT00015106602; ENSSSCP00015044886; ENSSSCG00015078707.
DR Ensembl; ENSSSCT00025065680; ENSSSCP00025028013; ENSSSCG00025048283.
DR Ensembl; ENSSSCT00030032302; ENSSSCP00030014549; ENSSSCG00030023253.
DR Ensembl; ENSSSCT00035033007; ENSSSCP00035013017; ENSSSCG00035025089.
DR Ensembl; ENSSSCT00040047914; ENSSSCP00040020027; ENSSSCG00040035687.
DR Ensembl; ENSSSCT00045011999; ENSSSCP00045008164; ENSSSCG00045007240.
DR Ensembl; ENSSSCT00050098796; ENSSSCP00050042700; ENSSSCG00050072369.
DR Ensembl; ENSSSCT00055035451; ENSSSCP00055028160; ENSSSCG00055018109.
DR Ensembl; ENSSSCT00060102199; ENSSSCP00060044479; ENSSSCG00060074696.
DR Ensembl; ENSSSCT00065084472; ENSSSCP00065036844; ENSSSCG00065061637.
DR Ensembl; ENSSSCT00070035722; ENSSSCP00070029847; ENSSSCG00070018112.
DR GeneID; 100513764; -.
DR KEGG; ssc:100513764; -.
DR CTD; 7141; -.
DR VGNC; VGNC:95550; TNP1.
DR eggNOG; ENOG502TKT1; Eukaryota.
DR GeneTree; ENSGT00390000000539; -.
DR HOGENOM; CLU_3019482_0_0_1; -.
DR InParanoid; P17306; -.
DR OMA; FKSHGMR; -.
DR TreeFam; TF338391; -.
DR Proteomes; UP000008227; Chromosome 15.
DR Proteomes; UP000314985; Chromosome 15.
DR Bgee; ENSSSCG00000016179; Expressed in testis and 7 other tissues.
DR GO; GO:0001673; C:male germ cell nucleus; IBA:GO_Central.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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: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:8019440"
FT CHAIN 2..55
FT /note="Spermatid nuclear transition protein 1"
FT /id="PRO_0000191419"
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 9
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"
SQ SEQUENCE 55 AA; 6424 MW; FA740830174A7D35 CRC64;
MSTSRKLKSH GMRRGKNRAP HKGVKRGGSK RKYRKGSLKS RKRCDDANRN YRSHL
