RBP2_MOUSE
ID RBP2_MOUSE Reviewed; 3053 AA.
AC Q9ERU9; E9QM01; Q61992; Q8C9K9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=E3 SUMO-protein ligase RanBP2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P49792};
DE AltName: Full=Ran-binding protein 2;
DE Short=RanBP2;
GN Name=Ranbp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola;
RX PubMed=11353387; DOI=10.1007/s003350010291;
RA Fauser S., Aslanukov A., Roepman R., Ferreira P.A.;
RT "Genomic organization, expression, and localization of murine Ran-binding
RT protein 2 (RanBP2) gene.";
RL Mamm. Genome 12:406-415(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-222.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 985-2249.
RX PubMed=8603673;
RA Wilken N., Senecal J.L., Scheer U., Dabauvalle M.C.;
RT "Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side
RT of the nuclear pore complex.";
RL Eur. J. Cell Biol. 68:211-219(1995).
RN [5]
RP INTERACTION WITH PRKN.
RX PubMed=16332688; DOI=10.1074/jbc.m504994200;
RA Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.;
RT "Parkin ubiquitinates and promotes the degradation of RanBP2.";
RL J. Biol. Chem. 281:3595-3603(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-954; SER-2083;
RP THR-2130; SER-2134; SER-2348; SER-2505; SER-2576; THR-2578 AND SER-2729,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954; SER-1154 AND SER-2729,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-788 AND SER-2505,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-781; SER-788;
RP SER-954; SER-1101; SER-1154; THR-1842; SER-1845; THR-1990; SER-2083;
RP SER-2088; SER-2107; SER-2117; SER-2127; THR-2130; SER-2134; SER-2299;
RP SER-2330; SER-2505; SER-2576; THR-2578 AND SER-2729, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP DISULFIDE BOND.
RX PubMed=23641069; DOI=10.1242/jcs.124172;
RA Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.;
RT "Intermolecular disulfide bonds between nucleoporins regulate karyopherin-
RT dependent nuclear transport.";
RL J. Cell Sci. 126:3141-3150(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1814, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1015, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
CC conjugation by UBE2I. Involved in transport factor (Ran-GTP,
CC karyopherin)-mediated protein import via the F-G repeat-containing
CC domain which acts as a docking site for substrates. Binds single-
CC stranded RNA (in vitro). May bind DNA. Component of the nuclear export
CC pathway. Specific docking site for the nuclear export factor exportin-1
CC (By similarity). Sumoylates PML at 'Lys-490' which is essential for the
CC proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and
CC cytoplasmic stacks of nuclear pore complex known as annulate lamellae
CC during G2 phase of cell cycle. Probable inactive PPIase with no
CC peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Part of the nuclear pore complex (By similarity). Forms a
CC complex with NXT1, NXF1 and RANGAP1 (By similarity). Forms a tight
CC complex with RANBP1 and UBE2I (By similarity). Interacts with SUMO1 but
CC not SUMO2 (By similarity). Interacts with sumoylated RANGAP1 (By
CC similarity). Interacts with CDCA8 (By similarity). Interacts with PML
CC (By similarity). Interacts with BICD2 (By similarity). Interacts with
CC PRKN (PubMed:16332688). Interacts with MCM3AP (By similarity).
CC Interacts with COX11 (By similarity). {ECO:0000250|UniProtKB:P49792,
CC ECO:0000269|PubMed:16332688}.
CC -!- INTERACTION:
CC Q9ERU9; Q9WVS6: Prkn; NbExp=2; IntAct=EBI-643756, EBI-973635;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus
CC membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P49792}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete
CC intranuclear foci. Cytoplasmic filaments.
CC {ECO:0000250|UniProtKB:P49792}.
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 -!- DOMAIN: The PPIase cyclophilin-type domain has high structural
CC similarity with PPIA, but has extremely low and barely detectable
CC proline isomerase activity (in vitro) (By similarity). Only about half
CC of the residues that surround the PPIA active site cleft are conserved.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC {ECO:0000269|PubMed:23641069}.
CC -!- SIMILARITY: Belongs to the RanBP2 E3 ligase family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a PPIase cyclophilin-type domain, it
CC has probably no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792}.
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DR EMBL; AF279458; AAG17403.1; -; Genomic_DNA.
DR EMBL; AC158593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK041932; BAC31101.1; -; mRNA.
DR EMBL; X87337; CAA60778.1; -; mRNA.
DR CCDS; CCDS23861.1; -.
DR PIR; S57968; S57968.
DR RefSeq; NP_035370.2; NM_011240.3.
DR SMR; Q9ERU9; -.
DR BioGRID; 202582; 97.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR ComplexPortal; CPX-4921; E3 ligase (RANBP2) complex.
DR IntAct; Q9ERU9; 92.
DR MINT; Q9ERU9; -.
DR STRING; 10090.ENSMUSP00000003310; -.
DR iPTMnet; Q9ERU9; -.
DR PhosphoSitePlus; Q9ERU9; -.
DR SwissPalm; Q9ERU9; -.
DR EPD; Q9ERU9; -.
DR jPOST; Q9ERU9; -.
DR MaxQB; Q9ERU9; -.
DR PaxDb; Q9ERU9; -.
DR PeptideAtlas; Q9ERU9; -.
DR PRIDE; Q9ERU9; -.
DR ProteomicsDB; 255049; -.
DR Antibodypedia; 33105; 209 antibodies from 24 providers.
DR DNASU; 19386; -.
DR Ensembl; ENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226.
DR GeneID; 19386; -.
DR KEGG; mmu:19386; -.
DR UCSC; uc007fdd.1; mouse.
DR CTD; 5903; -.
DR MGI; MGI:894323; Ranbp2.
DR VEuPathDB; HostDB:ENSMUSG00000003226; -.
DR eggNOG; KOG0864; Eukaryota.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000154389; -.
DR HOGENOM; CLU_000378_0_0_1; -.
DR InParanoid; Q9ERU9; -.
DR OMA; ACQNPNK; -.
DR OrthoDB; 201737at2759; -.
DR PhylomeDB; Q9ERU9; -.
DR TreeFam; TF314797; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 19386; 20 hits in 72 CRISPR screens.
DR ChiTaRS; Ranbp2; mouse.
DR PRO; PR:Q9ERU9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9ERU9; protein.
DR Bgee; ENSMUSG00000003226; Expressed in humerus cartilage element and 261 other tissues.
DR Genevisible; Q9ERU9; MM.
DR GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990723; C:cytoplasmic periphery of the nuclear pore complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; ISO:MGI.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0061665; F:SUMO ligase activity; ISO:MGI.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0051642; P:centrosome localization; IEA:Ensembl.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0051168; P:nuclear export; IC:ComplexPortal.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; IDA:MGI.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138; PTHR23138; 4.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 6.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 6.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF90209; SSF90209; 4.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 6.
DR PROSITE; PS50199; ZF_RANBP2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Disulfide bond; Isopeptide bond; Membrane; Metal-binding;
KW Methylation; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; RNA-binding; TPR repeat;
KW Transferase; Translocation; Transport; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..3053
FT /note="E3 SUMO-protein ligase RanBP2"
FT /id="PRO_0000204914"
FT REPEAT 26..59
FT /note="TPR 1"
FT REPEAT 60..93
FT /note="TPR 2"
FT REPEAT 94..128
FT /note="TPR 3"
FT REPEAT 165..201
FT /note="TPR 4"
FT REPEAT 288..319
FT /note="TPR 5"
FT REPEAT 583..616
FT /note="TPR 6"
FT REPEAT 648..681
FT /note="TPR 7"
FT REPEAT 1000..1001
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1099..1100
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1117..1118
FT /note="3"
FT /evidence="ECO:0000305"
FT DOMAIN 1165..1301
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 1449..1450
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1538..1539
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1696..1697
FT /note="6"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1737..1738
FT /note="7"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1775..1776
FT /note="8"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1798..1799
FT /note="9"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 1849..1985
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2097..2098
FT /note="10"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 2146..2282
FT /note="RanBD1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2354..2355
FT /note="11"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2373..2374
FT /note="12"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2383..2384
FT /note="13"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2470..2522
FT /note="1"
FT REPEAT 2546..2596
FT /note="2"
FT REPEAT 2674..2675
FT /note="14"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2676..2677
FT /note="15"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2697..2698
FT /note="16"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2714..2715
FT /note="17"
FT /evidence="ECO:0000305"
FT DOMAIN 2740..2875
FT /note="RanBD1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 2896..3052
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 2935..2936
FT /note="18"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 3018..3019
FT /note="19"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 3034..3035
FT /note="20"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT ZN_FING 1345..1375
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1410..1439
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1469..1498
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1494..1527
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1558..1587
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1617..1646
FT /note="RanBP2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 773..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..3035
FT /note="20 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1147..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1984..2124
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REGION 2030..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2316..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2394..2430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2443..2463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2468..2472
FT /note="Interaction with sumoylated RANGAP1"
FT /evidence="ECO:0000250"
FT REGION 2470..2596
FT /note="2 X 50 AA approximate repeats"
FT REGION 2470..2545
FT /note="Required for E3 SUMO-ligase activity"
FT /evidence="ECO:0000250"
FT REGION 2470..2522
FT /note="Interaction with UBE2I"
FT /evidence="ECO:0000250"
FT REGION 2523..2596
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT REGION 2598..2666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2111..2132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2598..2615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2651..2665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 944
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1015
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1015
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1096
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1814
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1842
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1990
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2088
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 2364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2503
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 2576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 3036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1859
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2627
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CONFLICT 213..222
FT /note="EYLESLQCLD -> VGETYFSTVF (in Ref. 3; BAC31101)"
FT /evidence="ECO:0000305"
FT CONFLICT 985..1001
FT /note="LVAHASRSAESKVIEFG -> IPGSRFKVSRIKGYRIWL (in Ref. 4;
FT CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1086..1089
FT /note="ISGQ -> YLA (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="L -> F (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1273
FT /note="E -> G (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="A -> S (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1280
FT /note="K -> Q (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="E -> G (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="N -> D (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861
FT /note="E -> D (in Ref. 4; CAA60778)"
FT /evidence="ECO:0000305"
FT CONFLICT 2868..2869
FT /note="EC -> DS (in Ref. 1; AAG17403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3053 AA; 341121 MW; 62FD4249DEE466AE CRC64;
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP
KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDIHVNIR LVELYRSNKR
LKDAVAHCHE ADRNTALRSS LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA
NLMLLTLSTR DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR LSQSGHMLLN
LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF LGNDDIGNLD GQVPDPDDLA
RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL PAIRKWLKQL FHHLPQETSR LETNAPESIC
ILDLEVFLLG VIYTSHLQLK EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH
RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA HITFAILDAV
NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIR
ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCWRS ADSELKHSTP
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR
WPAEPYGQDP APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT GILSPRGDDY
FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF GKSNFVQPMQ GEVIRPPLTT
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPSTAYS NSESLLGLLT SDKPLQGDGY
SGLKPISGQA SGSRNTFSFG SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA
SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW
HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNTSTAP NHTLRIVKES
ATQDNKDICK ADGGNLNFEF QIVKKEGPYW NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL
LGPPLVENGF APKTGLENAQ DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS
SFVQTSFKFG QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG FEGMFAKKEG
QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS ETSRSPKSGF EGLFPKKEGE
WECAVCSVQN ESSSLKCVAC EASKPTHKPH EAPSAFTVGS KSQSNESAGS QVGTEFKSNF
PEKNFKVGIS EQKFKFGHVD QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ
EKGNQEKKSE KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF EPVVQMPEKV
ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL KNEVNGKLRM LMRREQVLKV
CANHWITTTM NLKPLSGSDR AWMWLASDFS DGDAKLEQLA AKFKTPELAE EFKQKFEECQ
RLLLDIPLQT PHKLVDTGRA AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA
PSASDTTAKQ NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV VPLPDLVEVS
SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY DNKQVRIVMR RDQVLKLCAN
HRITPDMTLQ TMKGTERVWV WTACDFADGE RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ
EKDSLITPHV SHLSTPRESP CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE
TTPKAVVSPP KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT PEKAQEKSKP
EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR PGYVSEEEED DEDYEMAVKK
LNGKLYLDDS EKPLEENLAD NDKECVIVWE KKPTVEERAK ADTLKLPPTF FCGVCSDTDE
DNGNGEDFQS ELRKVCEAQK SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS
SPVSGTMDKP VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV EVKSGEEDEE
VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI LMRRDQVFKV CANHVITKAM
ELKPLNVSNN ALVWTASDYA DGEAKVEQLA VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH
TSLAAELSKD TNPVVFFDVC ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS
IFHRVVPDFI CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC GQL
