NASP_RAT
ID NASP_RAT Reviewed; 776 AA.
AC Q66HD3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=Nasp {ECO:0000312|EMBL:AAH81913.1};
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] {ECO:0000312|EMBL:AAH81913.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH81913.1};
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-242; SER-306;
RP SER-321; THR-379; SER-398; THR-452; SER-468; THR-482; SER-485 AND SER-714,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for DNA replication, normal cell cycle progression
CC and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1
CC linker histones and stimulates HSP90 ATPase activity. NASP and H1
CC histone are subsequently released from the complex and translocate to
CC the nucleus where the histone is released for binding to DNA.
CC {ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones (By
CC similarity). Interacts with histones H2A, H2B, H3 and H4 (By
CC similarity). Interacts with histone H3.3 (By similarity). Also binds to
CC HSP90 in the cytoplasm. This interaction stimulates binding of NASP to
CC H1-6/H1T (By similarity). {ECO:0000250|UniProtKB:P49321,
CC ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MD9}. Nucleus
CC {ECO:0000250|UniProtKB:Q99MD9}.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; BC081913; AAH81913.1; -; mRNA.
DR RefSeq; NP_001005543.1; NM_001005543.1.
DR RefSeq; XP_006238708.1; XM_006238646.3.
DR RefSeq; XP_008762215.1; XM_008763993.2.
DR AlphaFoldDB; Q66HD3; -.
DR SMR; Q66HD3; -.
DR STRING; 10116.ENSRNOP00000022170; -.
DR iPTMnet; Q66HD3; -.
DR PhosphoSitePlus; Q66HD3; -.
DR jPOST; Q66HD3; -.
DR PaxDb; Q66HD3; -.
DR PRIDE; Q66HD3; -.
DR Ensembl; ENSRNOT00000022170; ENSRNOP00000022170; ENSRNOG00000016454.
DR GeneID; 298441; -.
DR KEGG; rno:298441; -.
DR UCSC; RGD:1359609; rat.
DR CTD; 4678; -.
DR RGD; 1359609; Nasp.
DR eggNOG; KOG4563; Eukaryota.
DR GeneTree; ENSGT00390000016650; -.
DR HOGENOM; CLU_010162_0_0_1; -.
DR InParanoid; Q66HD3; -.
DR OMA; SSAFPCE; -.
DR OrthoDB; 1176629at2759; -.
DR PhylomeDB; Q66HD3; -.
DR TreeFam; TF317297; -.
DR PRO; PR:Q66HD3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016454; Expressed in testis and 20 other tissues.
DR Genevisible; Q66HD3; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISS:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Coiled coil; Cytoplasm; DNA replication;
KW Isopeptide bond; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CHAIN 2..776
FT /note="Nuclear autoantigenic sperm protein"
FT /id="PRO_0000261598"
FT REPEAT 43..76
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 530..563
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 572..605
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 115..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..127
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 210..242
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 256..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..500
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 685..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..160
FT /evidence="ECO:0000255"
FT COILED 191..216
FT /evidence="ECO:0000255"
FT COILED 597..650
FT /evidence="ECO:0000255"
FT MOTIF 704..710
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 127..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CROSSLNK 724
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P49321"
SQ SEQUENCE 776 AA; 84200 MW; 8E36041F0B86272F CRC64;
MATESTATAA IAAELVSADK VEDAPAPSTS ADKMESLDVD SEAKKLLGLG QKHLVMGDIP
AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG
EKTEDESLVE NNDNVDEEAR EELREQVYDA MGEKEAKKAE GQSLTKPETD KEQESEVEKG
GREDMDISEP AEKLQEKVES TSKQLTESSE EAKEAAIPGL NEDEVTSGKT EQESLCTEEG
KSISGVYVQN KEFREAVPQE EGEEMISLEK KPKETSEDQT IGAPEKQDTL MKVVEIEAEI
DSEVKSVDVG GEEPKDQGAI SESELGKAVL MQLSGQDVEV SPVVAAEAGS EVSEKPGQEI
TVLPNNGPVV GQSSAGDQTP SEPQNSAERL SETKDGASVE EVKAELVPEQ EEAMPPVEES
EAAGDGVETK VAQRATEKAP EDKFKIAANE ETQERDEQMK EGEETEGSEE EDKENDKAEE
TTNESVLEKK TLQENEEEEI GNLELAWDML DLAKIIFKRQ ETKEAQLYAA QAHLKLGEVS
VESENYIQAV EEFQACLSLQ EQYLEAHDRL LAETHYQLGL AYGYNSQYDE AVAQFGKSID
VIEKRMAVLL EQMKEAEGSF TEYEKEIEEL KELLPEIREK IEDAKESQRS GNVAELALKA
TLVESSTSGF TPSGAGASVS MIASRKPTDG ASSSNCVTDI SHLVRKKRKP EEESPRKDDA
KKAKPEPEVN GGSGDAVSSG NEVSENMEAE AENQAESQTT AEGTVDSAAT VKSTAC
