STP1_SHEEP
ID STP1_SHEEP Reviewed; 55 AA.
AC P22613; W5QDS0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Spermatid nuclear transition protein 1;
DE Short=Protein T;
DE Short=STP-1;
DE Short=TP-1;
GN Name=TNP1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2]
RP PROTEIN SEQUENCE OF 2-55, VARIANT GLY-28, PHOSPHORYLATION AT SER-9; SER-36;
RP SER-37 AND SER-40, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=2040274; DOI=10.1111/j.1432-1033.1991.tb15980.x;
RA Chirat F., Martinage A., Briand G., Kouach M., van Dorsselaer A., Loir M.;
RT "Nuclear transition protein 1 from ram elongating spermatids. Mass
RT spectrometric characterization, primary structure and phosphorylation sites
RT of two variants.";
RL Eur. J. Biochem. 198:13-20(1991).
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; AMGL01055949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S16075; BGSH.
DR RefSeq; XP_004004966.1; XM_004004917.3.
DR AlphaFoldDB; P22613; -.
DR STRING; 9940.ENSOARP00000020868; -.
DR iPTMnet; P22613; -.
DR Ensembl; ENSOART00000021156; ENSOARP00000020868; ENSOARG00000019426.
DR Ensembl; ENSOART00020039914; ENSOARP00020033079; ENSOARG00020025444.
DR GeneID; 101108026; -.
DR KEGG; oas:101108026; -.
DR CTD; 7141; -.
DR eggNOG; ENOG502TKT1; Eukaryota.
DR OMA; FKSHGMR; -.
DR OrthoDB; 1751529at2759; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000019426; Expressed in testis and 24 other tissues.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:2040274"
FT CHAIN 2..55
FT /note="Spermatid nuclear transition protein 1"
FT /evidence="ECO:0000269|PubMed:2040274"
FT /id="PRO_0000191421"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..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:0000269|PubMed:2040274"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2040274"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2040274"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2040274"
FT VARIANT 28
FT /note="C -> G"
FT /evidence="ECO:0000269|PubMed:2040274"
SQ SEQUENCE 55 AA; 6475 MW; 728408304DCA8479 CRC64;
MSTSRKLKSQ GTRRGKNRTP HKGVKRGCSK RKYRKSSLKS RKRCDDANRN FRSHL
