NU153_DROME
ID NU153_DROME Reviewed; 1883 AA.
AC Q9VXE6; Q1LZ48;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nuclear pore complex protein Nup153;
DE AltName: Full=153 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup153;
GN Name=Nup153; ORFNames=CG4453;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7641726;
RA Berrios M., Meller V.H., McConnell M., Fisher P.A.;
RT "Drosophila gp210, an invertebrate nuclear pore complex glycoprotein.";
RL Eur. J. Cell Biol. 67:1-7(1995).
RN [5]
RP FUNCTION, ASSOCIATION WITH THE MSL COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [6]
RP FUNCTION IN PROTEIN IMPORT, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17682050; DOI=10.1083/jcb.200612135;
RA Sabri N., Roth P., Xylourgidis N., Sadeghifar F., Adler J., Samakovlis C.;
RT "Distinct functions of the Drosophila Nup153 and Nup214 FG domains in
RT nuclear protein transport.";
RL J. Cell Biol. 178:557-565(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18562695; DOI=10.1091/mbc.e07-11-1162;
RA Katsani K.R., Karess R.E., Dostatni N., Doye V.;
RT "In vivo dynamics of Drosophila nuclear envelope components.";
RL Mol. Biol. Cell 19:3652-3666(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20174442; DOI=10.1371/journal.pgen.1000846;
RA Vaquerizas J.M., Suyama R., Kind J., Miura K., Luscombe N.M., Akhtar A.;
RT "Nuclear pore proteins nup153 and megator define transcriptionally active
RT regions in the Drosophila genome.";
RL PLoS Genet. 6:E1000846-E1000846(2010).
RN [9]
RP FUNCTION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [10]
RP FUNCTION.
RX PubMed=26502056; DOI=10.1038/ncb3258;
RA Ryu T., Spatola B., Delabaere L., Bowlin K., Hopp H., Kunitake R.,
RA Karpen G.H., Chiolo I.;
RT "Heterochromatic breaks move to the nuclear periphery to continue
RT recombinational repair.";
RL Nat. Cell Biol. 17:1401-1411(2015).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope
CC (PubMed:17682050). Functions as a scaffolding element in the nuclear
CC phase of the NPC (PubMed:17682050). Essential for the nuclear import of
CC nuclear localization signal (NLS)-containing proteins in a Importin
CC alpha/Importin beta receptor-dependent manner (PubMed:17682050).
CC Required for nuclear import of Mad (PubMed:20547758). Plays a role in
CC chromosomal organization and gene expression regulation; stimulates
CC transcription by promoting the formation of an open chromatin
CC environment (PubMed:20174442). Binds chromatin to nucleoporin-
CC associated regions (NARs) that define transcriptionally active regions
CC of the genome (PubMed:20174442). Associates with extended chromosomal
CC regions that alternate between domains of high density binding with
CC those of low occupancy (PubMed:20174442). Preferentially binds to NARs
CC of the male X chromosome (PubMed:20174442). In males, together with
CC Mtor, required for the localization of the male-specific lethal (MSL)
CC histone acetyltransferase complex to the X chromosome and therefore for
CC the transcription of dosage compensation genes (PubMed:16543150). May
CC play a role in double strand break DNA repair (PubMed:26502056).
CC {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050,
CC ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:20547758,
CC ECO:0000269|PubMed:26502056}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds at least 4 zinc ions per subunit.;
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:17682050).
CC Associates with male-specific lethal (MSL) histone acetyltransferase
CC complex (PubMed:16543150). {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:17682050}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17682050}. Nucleus
CC membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17682050,
CC ECO:0000269|PubMed:18562695}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:7641726}. Chromosome
CC {ECO:0000269|PubMed:20174442}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:18562695}. Note=Localized to the nucleoplasmic side
CC of the nuclear pore complex (NPC) core structure, forming a fibrous
CC structure called the nuclear basket (PubMed:17682050). Localized at the
CC spindle in mitotic syncytial embryos (PubMed:18562695). Associates with
CC chromatin (PubMed:20174442). {ECO:0000269|PubMed:18562695,
CC ECO:0000269|PubMed:20174442, ECO:0000303|PubMed:17682050}.
CC -!- TISSUE SPECIFICITY: Expressed in adult male accessory glands (at
CC protein level). {ECO:0000269|PubMed:7641726}.
CC -!- DEVELOPMENTAL STAGE: Expressed in syncytial embryos.
CC {ECO:0000269|PubMed:18562695}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NUP153 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48628.4; -; Genomic_DNA.
DR EMBL; AE014298; ACL82938.1; -; Genomic_DNA.
DR EMBL; BT025178; ABE98144.1; -; mRNA.
DR RefSeq; NP_001138206.1; NM_001144734.2.
DR RefSeq; NP_573136.3; NM_132908.5.
DR AlphaFoldDB; Q9VXE6; -.
DR SMR; Q9VXE6; -.
DR BioGRID; 58967; 19.
DR IntAct; Q9VXE6; 11.
DR MINT; Q9VXE6; -.
DR STRING; 7227.FBpp0112385; -.
DR PaxDb; Q9VXE6; -.
DR PRIDE; Q9VXE6; -.
DR DNASU; 32630; -.
DR EnsemblMetazoa; FBtr0074284; FBpp0074059; FBgn0061200.
DR EnsemblMetazoa; FBtr0299587; FBpp0288862; FBgn0061200.
DR GeneID; 32630; -.
DR KEGG; dme:Dmel_CG4453; -.
DR UCSC; CG4453-RA; d. melanogaster.
DR CTD; 9972; -.
DR FlyBase; FBgn0061200; Nup153.
DR VEuPathDB; VectorBase:FBgn0061200; -.
DR eggNOG; KOG4719; Eukaryota.
DR GeneTree; ENSGT00940000153253; -.
DR HOGENOM; CLU_002102_0_0_1; -.
DR InParanoid; Q9VXE6; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; Q9VXE6; -.
DR BioGRID-ORCS; 32630; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32630; -.
DR PRO; PR:Q9VXE6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0061200; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; Q9VXE6; baseline and differential.
DR Genevisible; Q9VXE6; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0044613; C:nuclear pore central transport channel; IMP:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:FlyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0007549; P:dosage compensation; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:FlyBase.
DR GO; GO:0006999; P:nuclear pore organization; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23193; PTHR23193; 3.
DR Pfam; PF00641; zf-RanBP; 5.
DR SMART; SM00547; ZnF_RBZ; 6.
DR SUPFAM; SSF90209; SSF90209; 6.
DR PROSITE; PS01358; ZF_RANBP2_1; 6.
DR PROSITE; PS50199; ZF_RANBP2_2; 6.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA-binding; Membrane; Metal-binding; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Translocation; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1883
FT /note="Nuclear pore complex protein Nup153"
FT /id="PRO_0000422142"
FT REPEAT 1287..1288
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 1315..1316
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 1317..1318
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 1340..1341
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 1353..1354
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 1415..1416
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 1469..1470
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 1511..1512
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1528..1529
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1548..1549
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1586..1587
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1599..1600
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1613..1614
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1647..1648
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1653..1654
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1672..1673
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1694..1695
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 1724..1725
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 1737..1738
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 1748..1749
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 1768..1769
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 1785..1786
FT /note="22"
FT /evidence="ECO:0000305"
FT ZN_FING 903..932
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 962..993
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1009..1038
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1067..1097
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1126..1155
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1237..1266
FT /note="RanBP2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1786
FT /note="22 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1301..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 926
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 970
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 984
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 987
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1015
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1018
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1074
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1077
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1088
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 1091
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P49791"
SQ SEQUENCE 1883 AA; 196585 MW; 46CC3237B37E2454 CRC64;
MEDAQEQRES SQAELAKKHP LTPLKELPEE SEEEEEEEDE SSAGALRESD SNNSIMGKMK
MRVSSILPAS LSGWFSPSSK DGNDALSSPA NLRQSQPRQS NGRLTTKRKR GRRRIMLAEV
DADAADDLDD GSDAKGLNYE EVALADNIAE HDLAAEDEQT RRSEYNVFLL RKRAGAVAAA
GGDEDEAEED ELEEDDEDGD EEDDDEEQEN LQQSAAVQTK RRRLELETPV NLPNMRRLPL
LSSTPAAPLA AATSSSSSQM YKGVSHIAPH RRNHLNLYGS QRQREPAYNF FTGNEAAEGS
TGDLPHSIRR SLNIPFGGSS TATSYNNSLS SLPNHKRPSL IGKQTHRRDL TMDETGTGPA
MSSEEHLNHL LRISRTNNNT SNNNNNNNNN NNVIETKTRR SELSAAAGGC GDSQSESDMN
EYHDNGEGHD GLRPSHYNSN SNLEFYGNLQ SSKSIFNRSN TAAQQSHRNS TWSLNSLTQR
RRFNASIYGS TSALSDSRLL SGSASNSGSA SASSSPFYQG RTTFGGNSGN NRLFSRSNLS
SSAASSMLGL NSAGSSPAHQ LHASMTGGIG YGMKAVDMRP SDSGSLAETS VGQGGSKKPG
TGLSNTTMRI LNLLESYSTP LIDAKRMGSS IKEHQSSRQQ RQGTPATPYL RSTSASRNVS
VPNHINELAE LRSNKLLVPT MQQLLERRRL HRVTQNSRDV VHSQNVRAGG ENNQEKPKPT
APYVAPIDQS ANHTQHTNKM RSRLSHQTRN KETRTAEEEA PPPLDLPQIS FPDMASAPKF
DLIIKPTVPV VSKPSTTDPI QSSKSSNTNL STTNSKQMPN FLANPQPAAP IVNFAANGNV
SAISKPSKRT FTFSEPTPLS NFQENCIPKP KINRKYTFSA PAPLDDLRIT NKQSQPTING
TPSSKEWECD TCMVRNKPEI NKCVACETAK PVASAAPVQA PLPPSTAAID TQSFVGFGDR
FKKSTTAWEC DACMLSNKAE ASKCIACETP RKTVAPKVNN FSPLITNAKS NEWECSVCLV
RNKVEVSKCV ACESAKPGAT MALPATSNIA VATPSIITDG FGDRFKKSAT AWECDACMLS
NKAEASKCIA CETPRKSSTP IANSSYPSIN NNLPAGSGFD ISFTRKANMW ECQTCLVMNK
SSDEECIACQ TPNSQARNSN SESALISSIS SSSASFSGSL SRPSSRSSSG STSTCGSVCS
GSIVSISSTT ESAKALSAKK VPPKPDAGFQ QLVAAQKTST WECEACLAKN DMSRKTCICC
EQMMPEAFNP AATTANSAAS SVPKFRFGFS HVKEVVKPSV ETTTTPAPTS AQFSFGFGQS
NQGKDVADSK KTEAPKTFMF GVSKVEEPKT VSFGTGIKET TATSSTEATA PTPAAAAPAP
VQFVFKAPTT ATTASSLTTT ISTTSNAPAL GGFSFGAPSS SSTVSSSTTS TSANPAAVKP
MFSWSGAGSA VSSTSSSQQP VAKAPTLGFG VSSSTVTTTT TSTKVFAFTP ASGLDPAAAT
SAPAAGAGFS FGSQSKPATT QNTGTFFFGQ PTAVAPATPT NPSVSSIFGA PATSTTASTS
VSATTSTSTA NAIASSFAPT STPQLFGNWG EKKTDLTTFG ASSGSGTTTT PSFGWSSNGD
AAKSNSAAVG SAAVPSSSAS TMATPIFGSS SMFGPSSSSN NTTSTSTTSL PFGSAATTAA
TTPAGGNAAL TGLFGNVGNS LAGVGAPVAT TPAATAAAPL TNIFGNPTPV AAAAPVFGSG
STIPSAGFGA PAAAAPLAAP ALPGAFNFGG ATAATPAASS APFVFGSSTN EPLAKPSFNF
TGSAASSTAP APAFNFTANT AATNNPSGGD STPNANALFQ FSATSTAPAN IFAFNPPAAG
NSAQSSQTAR RKIRAPVRRL PPR
