ID H2RAW2_PANTR Unreviewed; 2454 AA.
AC H2RAW2; A0A2J8KK38; K7C2V6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Transcriptional regulator ATRX {ECO:0000256|ARBA:ARBA00016932};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
DE AltName: Full=X-linked nuclear protein {ECO:0000256|ARBA:ARBA00043074};
GN Name=ATRX {ECO:0000313|EMBL:JAA18585.1,
GN ECO:0000313|Ensembl:ENSPTRP00000054614.3,
GN ECO:0000313|VGNC:VGNC:53808};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000054614.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000054614.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA18585.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Smooth vascular {ECO:0000313|EMBL:JAA18585.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000054614.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; AACZ04026359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04026365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABF01003560; JAA18585.1; -; mRNA.
DR Ensembl; ENSPTRT00000062063.3; ENSPTRP00000054614.3; ENSPTRG00000022047.7.
DR VGNC; VGNC:53808; ATRX.
DR GeneTree; ENSGT00940000155902; -.
DR HOGENOM; CLU_000863_0_0_1; -.
DR TreeFam; TF313172; -.
DR Proteomes; UP000002277; Chromosome X.
DR Bgee; ENSPTRG00000022047; Expressed in thymus and 21 other cell types or tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd11726; ADDz_ATRX; 1.
DR CDD; cd18068; DEXHc_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 121..258
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1543..1730
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1987..2167
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1875..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2424..2454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1153
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2431..2445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2454 AA; 278213 MW; D87A9E7EFBDF3730 CRC64;
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS
LPKEDGLHGI VSCTACGQQV NHFQKDSIYR HPSLQVLICK NCFKYYMSDD ISRDSDGMDE
QCRWCAEGGN LICCDFCHNA FCKKCILRNL GRKELSTIMD ENNQWYCYIC HPEPLLDLVT
ACNSVFENLE QLLQQNKKKI KVDSEKSNKV YEHTSRFSPK KTSSNCNGEE KKLDDSCSGS
VTYSYSALIV PKEMIKKAKK LIETTANMNS SYVKFLKQAT DNSEISSATK LRQLKAFKSV
LADIKKAHLA LEEDLNSEFR AMDAVNKEKN TKEHKVIDAK FETKARKGEK PCALEKKDIS
KSEAKLSRKQ VDSEHMDQNV PTEEQRANKS TGGEHKKSDR KEEPQYEPAN TSEDLDMDIV
SVPSSVPEDI FENLETAMEV QSSVDHQGDG SSGTEQEVES SSVKLNISSK DNRGGIKSKT
TAKVTKELYV KLTPVSLSNS PIKGADCQEV PQDKDGYKSC GLNPKLEKCG LGQENSDNEH
LVENEVSLLL EESDLRRSPR VKTTPLRRPT ETNPVTSNSD EECNETVKEK QKLSVPVRKK
DKRNSSDSAI DNPKPNKLPK SKQSETVDQN SDSDEMLAIL KEVSRMSHSS SSDTDINEIH
TNHKTLYDLK TQAGKDDKGK RKRKSSTSGS DFDTKKGKSA KSSIISKKKR QTQSESSNYD
SELEKEIKSM SKIGAARTTK KRIPNTKDFD SSEDEKHSKK GMDNQGHKNL KTSQEGSSDD
AERKQERENF SSAEGTVDKD TTIMELRDRL PKKQQASAST DGVDKFSGKE ESFTSLEVRK
VAETKEKSKH LKTKTCKKVQ DGLSDTAEKF LKKDQSDETS EDDKKQSKKG TEEKKKPSDF
KKKVIKMEQQ YESSSDGTEK LPEREEICHF PKGIKQIKNG TTDGEKKSKK IRDKTSKKKD
ELSDYAEKST GKGDSCDSSE DKKSKNGAYG REKKRCKLLG KSSRKRQDCS SSDTEKYSMK
EDGCNSSDKR LKRIELRERR NLSSKRNTKE IQSGSSSSDA EESSEDNKKK QQRTSSKKKA
VIVKEKKRNS LRTSTKRKQA DITSSSSSDI EDDDQNSIGE GSSDEQKIKP VTENLVLSSH
TGFCQSSGDE ALSKSVPVTV DDDDDDNDPE NRIAKKMLLE EIKANLSSDE DGSSDDEPEE
GKKRTGKQNE ENPGDEEAKN QVNSESDSDS EESKKPRYRH RLLRHKLTVS DGESGEEKKT
KPKEHKEVKG RNRRKVSSED SEDSDFQESG VSEEVSESED EQRPRTRSAK KAELEENQRS
YKQKKKRRRI KVQEDSSSEN KSNSEEEEEE KEEEEEEEEE EEEEEEDEND DSKSPGKGRK
KIRKILKDDK LRTETQNALK EEEERRKRIA EREREREKLR EVIEIEDASP TKCPITTKLV
LDEDEETKEP LVQVHRNMVI KLKPHQVDGV QFMWDCCCES VKKTKKSPGS GCILAHCMGL
GKTLQVVSFL HTVLLCDKLD FSTALVVCPL NTALNWMNEF EKWQEGLKDD EKLEVSELAT
VKRPQERSYM LQRWQEDGGV MIIGYEMYRN LAQGRNVKSR KLKEIFNKAL VDPGPDFVVC
DEGHILKNEA SAVSKAMNSI RSRRRIILTG TPLQNNLIEY HCMVNFIKEN LLGSIKEFRN
RFINPIQNGQ CADSTMVDVR VMKKRAHILY EMLAGCVQRK DYTALTKFLP PKHEYVLAVR
MTSIQCKLYQ YYLDHLTGVG NNSEGGRGKA GAKLFQDFQM LSRIWTHPWC LQLDYISKEN
KGYFDEDSMD EFIASDSDET SMSLSSDDYT KKKKKGKKGK KDSSSSGSGS DNDVEVIKVW
NSRSRGGGEG NVDETGNNPS VSLKLEESKA TSSSNPSSPA PDWYKDFVTD ADAEVLEHSG
KMVLLFEILR MAEEIGDKVL VFSQSLISLD LIEDFLELAS REKTEDKDKP LIYKGEGKWL
RNIDYYRLDG STTAQSRKKW AEEFNDETNV RGRLFIISTK AGSLGINLVA ANRVIIFDAS
WNPSYDIQSI FRVYRFGQTK PVYVYRFLAQ GTMEDKIYDR QVTKQSLSFR VVDQQQVERH
FTMNELTELY TFEPDLLDDP NSEKKKKRDT PMLPKDTILA ELLQIHKEHI VGYHEHDSLL
DHKEEEELTE EERKAAWAEY EAEKKGLTMR FNIPTGTNLP PVSFNSQTPY IPFNLGALSA
MSNQQLEDLI NQGREKVVEA TNSVTAVRIQ PLEDIISAVW KENMNLSEAQ VQALALSRQA
SQELDVKRRE AIYNDVLTKQ QMLISCVQRI LMNRRLQQQY NQQQQQQMTY QQATLGHLMM
PKPPNLIMNP SNYQQIDMRG MYQPVAGGMQ PPPLQRAPPP MRSKNPGPSQ GKSM
//
