NPAT_XENLA
ID NPAT_XENLA Reviewed; 1356 AA.
AC A2RRX6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Protein NPAT;
GN Name=npat;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for progression through the G1 and S phases of the
CC cell cycle and for S phase entry. Activates transcription of the
CC histone H2A, histone H2B, histone H3 and histone H4 genes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The LisH domain is required for the activation of histone gene
CC transcription. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NPAT family. {ECO:0000305}.
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DR EMBL; BC131895; AAI31896.1; -; mRNA.
DR RefSeq; NP_001091302.1; NM_001097833.1.
DR AlphaFoldDB; A2RRX6; -.
DR SMR; A2RRX6; -.
DR MaxQB; A2RRX6; -.
DR PRIDE; A2RRX6; -.
DR GeneID; 100037125; -.
DR KEGG; xla:100037125; -.
DR CTD; 100037125; -.
DR Xenbase; XB-GENE-6255262; npat.S.
DR OrthoDB; 80675at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 100037125; Expressed in testis and 19 other tissues.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR031442; NPAT_C.
DR Pfam; PF15712; NPAT_C; 1.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Activator; Cell cycle; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1356
FT /note="Protein NPAT"
FT /id="PRO_0000318165"
FT DOMAIN 3..35
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 180..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 145668 MW; 4E79116D97E1EFA6 CRC64;
MLLPSDVARL VLGYLQQEKL SSTCRSFILE SPNLREYAEH YTDEGSIPGC VLSLFGKNLT
TILNEYIAMK AKENKEEIPV MVSALWKKLD HTLSQIRSMQ NCLVLPTSQK VRTRYGIQDL
RHQRMLTSHA ASTGSAVALQ QTSTPIAAKQ VMLRSFTSQS ASQTIVSPLC SGQSTIQCTN
SPATESKGET LQNSALSDAE KKQTSSPMRR KTDCQRRRRA APLNSSSATH EGETEGNVDS
LQDLIDGNFP QLVIENAREK ILSNKSLQEK LAENINKFLG SDTATQASKL SEGGALEQYT
SIDEILGLQG GEMHMSEEAI HDILEQTELD PDFQELYDLF ACSSTKPTKL ASRDPSLQTE
GVATTSIHVA NDNLEPMESS FDASVDTSHS SNHSEVGAAQ KKDGRSQLVV PSPTPKVTES
TGMPSKVQEM PISASERQSM SDRSVESKKS IDSVIILDNT GSDTVIESNE EVQVTSMEVG
ISQSQDVDMN VLHTEVIGAD CQLAVEQGSL NMLTVDLTVP NLKEETPKMQ TYEKASEAKK
SSPLKDEVQA LGSRRLERNK SEGAEGPCTT ESQNIVVLVS IGSTVTESNL LNQRGDLPAT
PRKTDTSTET TVSEQMQAES SITSKELKVL QKQASKTPPH PMVPPISPSI KGSSSDSDGS
SLPLEVSSSV GVSTPVNTSN VEQNCSDVSS VDPSQIITLS FITEDIAEDA ELTKAVKSIS
ERSNSALLLS PFHKPQESSS IVSIPGPTSE TLTLLADPRE VVNVSGDVAT GVKPAEDCTI
ISLPGASNLS TDGGIIQLMP ATSSSFAPSG SFFISTCNTG GAQQSNIMVV PSNCAPASTQ
KQPCHFQTPP RPHSVYTVGQ AISPKLSQGS TFILASAVQP VLPGVMGMFP VSVVGQSSNT
FTTPSHQVLH VPVSQGVPKL SLPPKSQKPV PPRTLASAAE KQGTAATTDS GNRKSSSRMQ
RSENVDKNLA AMSQNKPEER QTSTTNPSTK GTENHKRVLC FENTAANRGT PNTKSLCNSA
APQNKDKVET MNTSSSSLPA KQNNKDSGKA DKTAPSTEAN SKCESVPSKQ PVVPATKDLS
GDKKPVAVAS SPDVLGGVMA NKENMLQKEN KKQELPEVSK KSSTADGAAG NLERTVQAVH
ETGRKHATLP SILRRTKLST ERMCPPSPLT KQASDLLQSM QFNSPNAKHF SGGDLPIPRT
PGSGIDDRLV DSHQDHMKTP KSKRYPEDGG TPKPMLPPAT PELPACSPAS ETGSENSVNM
AAHTLMILSR ATLAKTDGSS PLKDNTQQIK LSKNSSKKRK LDEPDEYGRR PHKKELMSPS
AILKRKKMKK HRKKSTDDFP AGMDVDKFLM SLHYDE