NASP_RABIT
ID NASP_RABIT Reviewed; 693 AA.
AC P27123;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
DE Flags: Fragment;
GN Name=NASP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Testis;
RX PubMed=2289010; DOI=10.1095/biolreprod43.4.559;
RA Welch J.E., Zimmerman L.J., Joseph D.R., O'Rand M.G.;
RT "Characterization of a sperm-specific nuclear autoantigenic protein. I.
RT Complete sequence and homology with the Xenopus protein, N1/N2.";
RL Biol. Reprod. 43:559-568(1990).
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 -!- TISSUE SPECIFICITY: Testis- and sperm-specific.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA31423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M37893; AAA31423.1; ALT_INIT; mRNA.
DR PIR; A43800; A43800.
DR RefSeq; NP_001076258.1; NM_001082789.1.
DR AlphaFoldDB; P27123; -.
DR SMR; P27123; -.
DR STRING; 9986.ENSOCUP00000025752; -.
DR PRIDE; P27123; -.
DR GeneID; 100009592; -.
DR KEGG; ocu:100009592; -.
DR CTD; 4678; -.
DR eggNOG; KOG4563; Eukaryota.
DR InParanoid; P27123; -.
DR OrthoDB; 1176629at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; ISS:UniProtKB.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; ISS:UniProtKB.
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; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Ubl conjugation.
FT CHAIN <1..693
FT /note="Nuclear autoantigenic sperm protein"
FT /id="PRO_0000106300"
FT REPEAT 448..481
FT /note="TPR 1"
FT REPEAT 490..523
FT /note="TPR 2"
FT REGION 25..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..40
FT /note="Histone-binding"
FT /evidence="ECO:0000250"
FT REGION 124..157
FT /note="Histone-binding"
FT /evidence="ECO:0000250"
FT REGION 374..418
FT /note="Histone-binding"
FT /evidence="ECO:0000250"
FT REGION 583..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..70
FT /evidence="ECO:0000255"
FT COILED 364..399
FT /evidence="ECO:0000255"
FT COILED 503..571
FT /evidence="ECO:0000255"
FT COILED 658..674
FT /evidence="ECO:0000255"
FT MOTIF 622..628
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 40..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MD9"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CROSSLNK 642
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT NON_TER 1
SQ SEQUENCE 693 AA; 75152 MW; 438E755378E08738 CRC64;
IYYTFDSFFC SPRMENGVLG NALEGVHVEE EEGEKTEEES LVENNDNVDE EAREELREQV
YDAMGEKEES KKTEGMSLSK PETAKEQESE MEKGGREDMD ISEPTEELPE KVALTPDQLT
ETSEEAEGAA APEGLNEAEV TSGKSEQEAA DAEKGKSVSG TDVQEEHKEQ VEEKQGEVIV
RIEKPTEASE EQPGTTLGKD NTAVEVEAEP VDATAKPVDV GGHEPKEQMA TSGNEPGKAV
LNQQLVGQDV PPVEESPMVT TEAAEVGSEV SEKSEQEATV VSNDGAVNGL SAAGDQASVD
PQPSAERVTE TKGGSELEEV RAELAPSQEA KLPIEESEGA GDGVETKVAQ GVTEKSPEDK
VKIAANEETQ EREEQMKEGE ETEGSEEEDK ENDKAEEETP NDSVLENKSL PENEEEEIGN
LELAWDMLDL AKIIFKRQET KEAQLYAAQA HLKLGEVSVE SQNYIQAVEE FQACLSLQEQ
YLEAHDRLLA ETHYQLGLAY GYNSQYDEAV AQFSKSIEVI EKRMAVLNEQ MKEAEGSSTE
YEKEIEELKE LLPEIREKIE DAKESQRSGN VAELALKATL VGSSTSGFTP SGGGSSVSTI
ASRKPADGAS SSNCVTDISH LVRKKRKPEE ESPRKDDAKK AKQEPEVNGG SGDAVPSGNE
VSENMEEAEN QTESRAAMEG TVEAGATVES TAC
