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CHR4_ARATH
ID   CHR4_ARATH              Reviewed;        2223 AA.
AC   F4KBP5; O48579; Q8GX65;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein CHROMATIN REMODELING 4 {ECO:0000303|PubMed:16547115};
DE            Short=AtCHR4;
DE            EC=3.6.4.-;
DE   AltName: Full=Protein PICKLE RELATED 1 {ECO:0000303|PubMed:10570159};
GN   Name=CHR4 {ECO:0000303|PubMed:16547115};
GN   Synonyms=PKR1 {ECO:0000303|PubMed:10570159};
GN   OrderedLocusNames=At5g44800 {ECO:0000312|Araport:AT5G44800};
GN   ORFNames=K23L20_15 {ECO:0000312|EMBL:BAB08833.1},
GN   T19K24.8 {ECO:0000312|EMBL:AAC79140.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1686-2223.
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=10570159; DOI=10.1073/pnas.96.24.13839;
RA   Ogas J., Kaufmann S., Henderson J., Somerville C.;
RT   "PICKLE is a CHD3 chromatin-remodeling factor that regulates the transition
RT   from embryonic to vegetative development in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13839-13844(1999).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA   Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT   "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene family
RT   in DNA damage response and recombination.";
RL   Genetics 173:985-994(2006).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: Chromatin-remodeling protein that binds DNA through histones
CC       and regulates gene transcription. May specifically recognize and bind
CC       trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone
CC       H3 (By similarity). Probable chromatin remodeling factor.
CC       {ECO:0000250|UniProtKB:Q8TDI0, ECO:0000303|PubMed:16547115}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC79140.1; Type=Erroneous gene model prediction;
CC       Sequence=BAB08833.1; Type=Erroneous gene model prediction;
CC       Sequence=BAC43019.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
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DR   EMBL; AB016874; BAB08833.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC002342; AAC79140.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95164.1; -; Genomic_DNA.
DR   EMBL; AK118410; BAC43019.1; ALT_INIT; mRNA.
DR   RefSeq; NP_199293.3; NM_123848.4.
DR   AlphaFoldDB; F4KBP5; -.
DR   SMR; F4KBP5; -.
DR   BioGRID; 19760; 8.
DR   STRING; 3702.AT5G44800.1; -.
DR   iPTMnet; F4KBP5; -.
DR   PaxDb; F4KBP5; -.
DR   PRIDE; F4KBP5; -.
DR   ProteomicsDB; 247003; -.
DR   EnsemblPlants; AT5G44800.1; AT5G44800.1; AT5G44800.
DR   GeneID; 834510; -.
DR   Gramene; AT5G44800.1; AT5G44800.1; AT5G44800.
DR   KEGG; ath:AT5G44800; -.
DR   Araport; AT5G44800; -.
DR   TAIR; locus:2156364; AT5G44800.
DR   eggNOG; KOG0383; Eukaryota.
DR   HOGENOM; CLU_000994_1_1_1; -.
DR   InParanoid; F4KBP5; -.
DR   OMA; INICEDK; -.
DR   OrthoDB; 54215at2759; -.
DR   PRO; PR:F4KBP5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KBP5; baseline and differential.
DR   Genevisible; F4KBP5; AT.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0042735; C:protein body; IPI:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01147; DUF1087; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromatin regulator; Coiled coil; DNA-binding; Helicase;
KW   Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..2223
FT                   /note="Protein CHROMATIN REMODELING 4"
FT                   /id="PRO_0000430852"
FT   DOMAIN          531..587
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          601..663
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          701..878
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1008..1167
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         75..122
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          39..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1268..1300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1394..1463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1483..1511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1760..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2006..2223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1375..1402
FT                   /evidence="ECO:0000255"
FT   COILED          2189..2215
FT                   /evidence="ECO:0000255"
FT   MOTIF           829..832
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           902..909
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        39..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1353..1380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1441..1455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2039..2062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2074..2098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2124..2147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2157..2181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2194..2208
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         714..721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   2223 AA;  247919 MW;  050D0E390B672B70 CRC64;
     MKDSGSEMIK RDWVMKQKRR KLPSILDILD QKVDSSMAFD SPEYTSSSKP SKQRLKTDST
     PERNSSKRKG NDGNYFECVI CDLGGDLLCC DSCPRTYHTA CLNPPLKRIP NGKWICPKCS
     PNSEALKPVN RLDAIAKRAR TKTKKRNSKA GPKCERASQI YCSSIISGEQ SSEKGKSISA
     EESKSTGKEV YSSPMDGCST AELGHASADD RPDSSSHGED DLGKPVIPTA DLPSDAGLTL
     LSCEDLSESK LSDTEKTHEA PVEKLEHASS EIVENKTVAE METGKGKRKK RKRELNDGES
     LERCKTDKKR AKKSLSKVGS SSQTTKSPES SKKKKKKNRV TLKSLSKPQS KTETPEKVKK
     LPKEERRAVR ATNKSSSCLE DTNSLPVGNL QVHRVLGCRI QGLTKTSLCS ALSDDLCSDN
     LQATDQRDSL VQDTNAELVV AEDRIDSSSE TGKSSRDSRL RDKDMDDSAL GTEGMVEVKE
     EMLSEDISNA TLSRHVDDED MKVSETHVSV ERELLEEAHQ ETGEKSTVAD EEIEEPVAAK
     TSDLIGETVS YEFLVKWVDK SNIHNTWISE AELKGLAKRK LENYKAKYGT AVINICEDKW
     KQPQRIVALR VSKEGNQEAY VKWTGLAYDE CTWESLEEPI LKHSSHLIDL FHQYEQKTLE
     RNSKGNPTRE RGEVVTLTEQ PQELRGGALF AHQLEALNWL RRCWHKSKNV ILADEMGLGK
     TVSASAFLSS LYFEFGVARP CLVLVPLSTM PNWLSEFSLW APLLNVVEYH GSAKGRAIIR
     DYEWHAKNST GTTKKPTSYK FNVLLTTYEM VLADSSHLRG VPWEVLVVDE GHRLKNSESK
     LFSLLNTFSF QHRVLLTGTP LQNNIGEMYN LLNFLQPSSF PSLSSFEERF HDLTSAEKVE
     ELKKLVAPHM LRRLKKDAMQ NIPPKTERMV PVELTSIQAE YYRAMLTKNY QILRNIGKGV
     AQQSMLNIVM QLRKVCNHPY LIPGTEPESG SLEFLHDMRI KASAKLTLLH SMLKVLHKEG
     HRVLIFSQMT KLLDILEDYL NIEFGPKTFE RVDGSVAVAD RQAAIARFNQ DKNRFVFLLS
     TRACGLGINL ATADTVIIYD SDFNPHADIQ AMNRAHRIGQ SKRLLVYRLV VRASVEERIL
     QLAKKKLMLD QLFVNKSGSQ KEFEDILRWG TEELFNDSAG ENKKDTAESN GNLDVIMDLE
     SKSRKKGGGL GDVYQDKCTE GNGKIVWDDI AIMKLLDRSN LQSASTDAAD TELDNDMLGS
     VKPVEWNEET AEEQVGAESP ALVTDDTGEP SSERKDDDVV NFTEENEWDR LLRMRWEKYQ
     SEEEAALGRG KRLRKAVSYR EAYAPHTSGP VNESGGEDEK EPEPELKKEY TPAGRALKEK
     FTKLRERQKN LIARRNSVEE SLPSGNVDQV TEVANQDEES PTSMDLDDSK ASQQCDAQKR
     KASSSDPKPD LLSQHHHGAE CLPSLPPNNL PVLGLCAPNF TQSESSRRNY SRPGSRQNRP
     ITGPHFPFNL PQTSNLVERE ANDQEPPMGK LKPQNIKEEP FQQPLSNMDG WLPHRQFPPS
     GDFERPRSSG AAFADFQEKF PLLNLPFDDK LLPRFPFQPR TMGTSHQDIM ANLSMRKRFE
     GTGHSMQDLF GGTPMPFLPN MKIPPMDPPV FNQQEKDLPP LGLDQFPSAL SSIPENHRKV
     LENIMLRTGS GIGHVQKKKT RVDAWSEDEL DSLWIGIRRH GYGNWETILR DPRLKFSKFK
     TPEYLAARWE EEQRKFLDSL SSLPSKSSRT DKSTKSSLFP GLPQGIMNRA LHGKYATPPR
     FQSHLTDIKL GFGDLASPLP LFEPSDHLGF RSEHFPPMAN LCTDNLPGEP SAGPSERAGT
     STNIPNEKPF PLNSLGMGNL GSLGLDSLSS LNTLRAEEKR DAIKRGKLPL FLDMPLPQML
     DSSNNVFLGR SANPSFLHPN RGLNPSNPMG RDIMGISSSE NKLPHWLRNV VTVPTVKSPE
     PPTLPPTVSA IAQSVRVLYG EDSTTIPPFV IPEPPPPAPR DPRHSLRKKR KRKLHSSSQK
     TTDIGSSSHN AVESSSQGNP QTSATPPLPP PSLAGETSGS SQPKLPPHNL NSTEPLSSEA
     IIIPPPEEDS VIAAAPSEAP GPSLEGITGT TKSISLESQS SEPETINQDG DLDPETDEKV
     ESERTPLHSD EKQEEQESEN ALNKQCEPIE AESQNTNAEE EAEAQEEDEE SMKMVTGNSL
     SDD
 
 
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