ZO2_MOUSE
ID ZO2_MOUSE Reviewed; 1167 AA.
AC Q9Z0U1; Q8K210;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Tight junction protein ZO-2;
DE AltName: Full=Tight junction protein 2;
DE AltName: Full=Zona occludens protein 2;
DE AltName: Full=Zonula occludens protein 2;
GN Name=Tjp2; Synonyms=Zo2;
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=C57BL/6 X CBA;
RX PubMed=10026224; DOI=10.1074/jbc.274.9.5981;
RA Itoh M., Morita K., Tsukita S.;
RT "Characterization of ZO-2 as a MAGUK family member associated with tight as
RT well as adherens junctions with a binding affinity to occludin and alpha
RT catenin.";
RL J. Biol. Chem. 274:5981-5986(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SAFB.
RX PubMed=12403786; DOI=10.1074/jbc.m206821200;
RA Traweger A., Fuchs R., Krizbai I.A., Weiger T.M., Bauer H.-C., Bauer H.;
RT "The tight junction protein ZO-2 localizes to the nucleus and interacts
RT with the heterogeneous nuclear ribonucleoprotein scaffold attachment
RT factor-B.";
RL J. Biol. Chem. 278:2692-2700(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1136, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP 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-968 AND TYR-1095, AND
RP 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-107; SER-140; SER-239;
RP SER-378; SER-380; SER-479; SER-684; SER-884; THR-887; SER-895; SER-988 AND
RP SER-1136, AND IDENTIFICATION BY 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 INTERACTION WITH USP53, AND SUBCELLULAR LOCATION.
RX PubMed=26609154; DOI=10.1523/jneurosci.1965-15.2015;
RA Kazmierczak M., Harris S.L., Kazmierczak P., Shah P., Starovoytov V.,
RA Ohlemiller K.K., Schwander M.;
RT "Progressive hearing loss in mice carrying a mutation in usp53.";
RL J. Neurosci. 35:15582-15598(2015).
RN [12]
RP STRUCTURE BY NMR OF 1-106.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of N-terminal PDZ domain from mouse TJP2.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in tight junctions and adherens junctions.
CC -!- SUBUNIT: Homodimer, and heterodimer with TJP1/ZO1. Interacts with UBN1.
CC Interacts with SCRIB (By similarity). Interacts with occludin and SAFB.
CC Interaction with SAFB occurs in the nucleus. Interacts with USP53 (via
CC the C-terminal region) (PubMed:26609154).
CC {ECO:0000250|UniProtKB:Q9UDY2, ECO:0000269|PubMed:12403786,
CC ECO:0000269|PubMed:26609154}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cell junction, tight junction
CC {ECO:0000269|PubMed:26609154}. Note=Also nuclear under environmental
CC stress conditions and in migratory endothelial cells and subconfluent
CC epithelial cell cultures. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AF113005; AAD19964.1; -; mRNA.
DR EMBL; BC034677; AAH34677.1; -; mRNA.
DR EMBL; BC039924; AAH39924.1; -; mRNA.
DR CCDS; CCDS89365.1; -.
DR RefSeq; NP_035727.2; NM_011597.4.
DR RefSeq; XP_006526971.1; XM_006526908.3.
DR RefSeq; XP_011245521.1; XM_011247219.2.
DR PDB; 2CSJ; NMR; -; A=1-104.
DR PDBsum; 2CSJ; -.
DR AlphaFoldDB; Q9Z0U1; -.
DR SMR; Q9Z0U1; -.
DR BioGRID; 204210; 7.
DR IntAct; Q9Z0U1; 3.
DR MINT; Q9Z0U1; -.
DR STRING; 10090.ENSMUSP00000097154; -.
DR iPTMnet; Q9Z0U1; -.
DR PhosphoSitePlus; Q9Z0U1; -.
DR SwissPalm; Q9Z0U1; -.
DR EPD; Q9Z0U1; -.
DR jPOST; Q9Z0U1; -.
DR MaxQB; Q9Z0U1; -.
DR PaxDb; Q9Z0U1; -.
DR PeptideAtlas; Q9Z0U1; -.
DR PRIDE; Q9Z0U1; -.
DR ProteomicsDB; 275312; -.
DR DNASU; 21873; -.
DR Ensembl; ENSMUST00000099558; ENSMUSP00000097154; ENSMUSG00000024812.
DR Ensembl; ENSMUST00000233658; ENSMUSP00000156728; ENSMUSG00000024812.
DR GeneID; 21873; -.
DR KEGG; mmu:21873; -.
DR UCSC; uc008ham.2; mouse.
DR CTD; 9414; -.
DR MGI; MGI:1341872; Tjp2.
DR VEuPathDB; HostDB:ENSMUSG00000024812; -.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000158634; -.
DR HOGENOM; CLU_006234_1_0_1; -.
DR InParanoid; Q9Z0U1; -.
DR OMA; GDQILKX; -.
DR OrthoDB; 1175136at2759; -.
DR PhylomeDB; Q9Z0U1; -.
DR TreeFam; TF315957; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 21873; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tjp2; mouse.
DR EvolutionaryTrace; Q9Z0U1; -.
DR PRO; PR:Q9Z0U1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z0U1; protein.
DR Bgee; ENSMUSG00000024812; Expressed in ear vesicle and 254 other tissues.
DR ExpressionAtlas; Q9Z0U1; baseline and differential.
DR Genevisible; Q9Z0U1; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005921; C:gap junction; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0070160; C:tight junction; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0050892; P:intestinal absorption; ISO:MGI.
DR GO; GO:2001205; P:negative regulation of osteoclast development; IMP:MGI.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:MGI.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IBA:GO_Central.
DR GO; GO:0090559; P:regulation of membrane permeability; ISO:MGI.
DR GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IMP:MGI.
DR CDD; cd12027; SH3_ZO-2; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005417; ZO.
DR InterPro; IPR005419; ZO-2.
DR InterPro; IPR035598; ZO-2_SH3.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01599; ZONOCCLUDNS2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..1167
FT /note="Tight junction protein ZO-2"
FT /id="PRO_0000094544"
FT DOMAIN 10..97
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 287..365
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 489..570
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 584..649
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 660..858
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 129..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1167
FT /note="Interaction with SCRIB"
FT /evidence="ECO:0000250"
FT COMPBIAS 244..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 907
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 1095
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 100
FT /note="Q -> L (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..107
FT /note="QGS -> LGC (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="SH -> CL (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="R -> G (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="K -> Q (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="S -> R (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="A -> P (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> T (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="T -> A (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="A -> P (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="E -> D (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="A -> D (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="D -> V (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="R -> W (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="G -> R (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="S -> R (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="V -> D (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="N -> T (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 690..691
FT /note="AA -> RS (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="T -> N (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="M -> I (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="S -> T (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT CONFLICT 1069
FT /note="A -> P (in Ref. 1; AAD19964)"
FT /evidence="ECO:0000305"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:2CSJ"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2CSJ"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2CSJ"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2CSJ"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:2CSJ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2CSJ"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:2CSJ"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:2CSJ"
SQ SEQUENCE 1167 AA; 131280 MW; C29AF94F423A3A70 CRC64;
MEEVIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND
RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ VAPLQGSPPL SHDDRGFEVI
EEFDGRSFRS GYSERSRHSS HDMLSHSWEG NRERGRPHQR TQSRERERSR GRSLERGLDQ
EDYGRSRERS RGRSLERGLD RDFVSRDHSR GRSIDRDYDR DYERSYHEAY EPDYGGGYSP
SYDRRAHPET RYERSRSREH LRSRSPSPES RSRHEHKGQH DPDRPIGVLL TKSKANEEYG
LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI EKSRGKLQLV
VLRDSKQTLI NIPALNDSDS EVEDISEIES NRSFSPEERR QQYSDQDYHS STEKLKERPS
SREETSGRLS RMGATPTPFK STGDITAAGV TEASREPRYQ EEGPVPQPRT APRVFLRPSP
EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT
QDFRGLVRED AVLYLLEIPK GETVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP
QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS VQNAQRENAG
DRADFWRMRG QRSSGGVKKN LRKSREDLAA AVSVSTKFPA YEKVLLREAG FKRPVVLFGP
IADIAMERLA TELPDLFQTA KTEPKDAGSE KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV
DLLNYTQWFP IVIFFNPDSR QGVKTIRQRL SPTSNKSSRK LFDQANKLKK TCSHLFTATI
NVNSANDGWF GSLKDSIQQQ QNEAVWVSEG KMEGMDDDAE DRMSYLTAMG ADYLSCDSRL
ISDFEDTDGE GGAYTDNELE EPAEEPLVSS ITRSSEPVQH EENIRKSSPE PRAQMRRAAS
RDQLRDASPP PAFKPEPPKA RSQNREDSFD YSKSNLPATA GSEIPGGSTK GYPPPIAAKP
AFGRPILKPS TPVPMPESEE VGESTEEQED APRSVLGRVK IFEKMDHKAK LQRMQELQEA
QNARIEIAQK HPDIYAVPIK APKPDAGLPP HMSSRPPEPQ KAPSRLYQDT RGSYGSDPEE
EEYRQQLAAH SKRGYYSQPS RYRDTEL
