ID F6ZEY8_MACMU Unreviewed; 2459 AA.
AC F6ZEY8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 74.
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|Ensembl:ENSMMUP00000029718.4,
GN ECO:0000313|VGNC:VGNC:70195};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000029718.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000029718.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029718.4};
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 SMR; F6ZEY8; -.
DR Ensembl; ENSMMUT00000031763.4; ENSMMUP00000029718.4; ENSMMUG00000022574.4.
DR VEuPathDB; HostDB:ENSMMUG00000022574; -.
DR VGNC; VGNC:70195; ATRX.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR Proteomes; UP000006718; Chromosome X.
DR Bgee; ENSMMUG00000022574; Expressed in ileum and 22 other cell types or tissues.
DR ExpressionAtlas; F6ZEY8; baseline.
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 3: Inferred from homology;
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:UP000006718};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 157..294
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1548..1735
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1992..2172
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 23..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2429..2459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2436..2450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2459 AA; 279054 MW; 327E63E5E6A00B35 CRC64;
MWCRSSESKL NTLVQKLHDF LAHSSEESEE TSSPPRLAMN QNTDKISGSG SNSDMMENSK
EEGTSSSEKS KSSGSSRSKR KPSIVTKYVE SDDEKPLDDE TVNEDASNEN SENDITMQSL
PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKTENLKKRG DGLHGIVSCT ACGQQVNHFQ
KDSIYRHPSL QVLICKNCFK YYMSDDISRD SDGMDEQCRW CAEGGNLICC DFCHNAFCKK
CILRNLGRKE LSTIMDENNQ WYCYICHPEP LLDLVTACNS VFENLEQLLQ QNKKKIKVDS
EKSNKVYEHT SRFSPKKTSS NCNGEEKKLD DSCSGSVTYS YSALIVPKEM IKKAKKLIET
TANMNSSYVK FLKQATDNSE ISSATKLRQL KAFKSVLADI KKAHLALEED LNSEFRALDA
VNKEKNTKEH KVIDAKFETK ARKGEKPCAL ERKDISKSEA KLSRKQVDSE HMDQNVPTEE
QRANKSTGGE HKKSDRKEEP QYEPANTSED LDMDIVSVPS SVPEDIFENL ETAMEVQSSA
DHQGDGSSGT EQELESASVK LNISSKDNRG GADCQEVPQD KDGYKSCGLN PKLEKCGLGQ
ENSDNEHLVE NEVSLLLEES DLRRSPRVKT TPLRRQTETN PVTSNSDEEC NETVKEKQKL
PVPVRKKDKR NSSDSAIDNP KPNKLPKSKQ SETVDQNSDS DEMLAILKEV SRMSHSSSSD
TDVNEIHTNH KTLYDLKTQA GKDDKGKRKR KSSTSGSDFD TKKGKSAKSA IISKKKRQTQ
SESSNYDSEL EKEIKSMSKI GAARTTKKRI PNTKDFDSSE DEKHSKKGMD NQGHKGLKTS
QEGSSDDAER KQDRENFSSA EGTVDKDTTI MELRDRLPKK QQASASSDGV SKLSGKEESF
TSLDVRKVAE TKEKSKHLKT KTCKKVQDGL SDIAEKFLKK DQSDETSEDD KKQSKKGAEE
KKEISDFKKK VIKMEQQYES SSDGTEKLPE REEICHFPKG IKQNKNETTD GEKKSKKIRE
KTSKKKDELS DYAEKSTGKG DSCDSSEDKK SKNGAYGREK KRCKLLGKSS RKRQDCSSSD
TEKYSMKEDG CNSSDKRLKR IELRERRNLS SKRNTKEIQS GSSSSDAEES SEDNKKKKQR
TSSKKKAVIV KEKKRNSLRT STKRKQADIT SSSSDIEDDD QNSIGEGSSD EQKIKPVTEN
LVLSSHTGFC QSSGDEALSK SVPVTVDDDD DDNDPENRIA KKMLLEEIKA NLSSDEDGSS
DDEPEEGKKR TGKQNEENPG DEEAKNQINS ESDSDSEESK KPRYRHRLLR HKLTVSDGES
GEEKKTKPKE HKEVKGRNRR KVSSEDSEDS DFQESGVSEE VSESEDEQRP RTRSAKKAEL
EENQRSYKQK KKRRRIKVQE DSSSENKSNS EEEEEEKEEE EEEEEEEEEE EDENDDSKSP
GKGRKKIRKI LKDDKLRTET QNALKEEEER RKRIAERERE REKLREVIEI EDASPTKCPI
TTKLVLDEDE ETKEPLVQVH RNMVIKLKPH QVDGVQFMWD CCCESVKKTK KSPGSGCILA
HCMGLGKTLQ VVSFLHTVLL CDKLDFSTAL VVCPLNTALN WMNEFEKWQE GLKDDEKLEV
SELATVKRPQ ERSYMLQRWQ EDGGVMIIGY EMYRNLAQGR NVKSRKLKEI FNKALVDPGP
DFVVCDEGHI LKNEASAVSK AMNSIRSRRR IILTGTPLQN NLIEYHCMVN FIKENLLGSI
KEFRNRFINP IQNGQCADST MVDVRVMKKR AHILYEMLAG CVQRKDYTAL TKFLPPKHEY
VLAVRMTPIQ CKLYQYYLDH LTGVGNNSEG GRGKAGAKLF QDFQMLSRIW THPWCLQLDY
ISKENKGYFD EDSMDEFIAS DSDETSMSLS SDDYTKKKKK GKKGKKDSSS SGSGSDNDVE
VIKVWNSRSR GGGEGNVDET GNNPSVSLKL EESKATSSSN PSSPAPDWYK DFVTDADAEV
LEHSGKMVLL FEILRMAEEI GDKVLVFSQS LISLDLIEDF LELASREKTE DKDKPLIYKG
EGKWLRNIDY YRLDGSTTAQ SRKKWAEEFN DETNVRGRLF IISTKAGSLG INLVAANRVI
IFDASWNPSY DIQSIFRVYR FGQTKPVYVY RFLAQGTMED KIYDRQVTKQ SLSFRVVDQQ
QVERHFTMNE LTELYTFEPD LLDDPNSEKK KKRDTPMLPK DTILAELLQI HKEHIVGYHE
HDSLLDHKEE EELTEEERKA AWAEYEAEKK GLTMRFNIPT GTNLPPVSFN SQTPYIPFNL
GALSAMSNQQ LEDLINQGRE KVVEATNSVT AVRIQPLEDI ISAVWKENMN LSEAQVQALA
LSRQASQELD VKRREAIYND VLTKQQMLIS CVQRILMNRR LQQQYNQQQQ QQMTYQQATL
GHLMMPKPPN LIMNPSNYQQ IDMRGMYQPV AGGMQPPPLQ RAPPPMRSKN PGPSQGKSM
//
