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 24-JAN-2024, entry version 203. 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], FUNCTION, AND INTERACTION WITH TJP1; OCLN AND RP CTNNA1. 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, RC Pancreas, 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 FUNCTION, INTERACTION WITH CLDN18, AND SUBCELLULAR LOCATION. RX PubMed=22437732; DOI=10.1002/jbmr.1600; RA Linares G.R., Brommage R., Powell D.R., Xing W., Chen S.T., Alshbool F.Z., RA Lau K.H., Wergedal J.E., Mohan S.; RT "Claudin 18 is a novel negative regulator of bone resorption and osteoclast RT differentiation."; RL J. Bone Miner. Res. 27:1553-1565(2012). RN [12] 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 [13] 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 (PubMed:10026224). Acts as a positive regulator of RANKL-induced CC osteoclast differentiation, potentially via mediating downstream CC transcriptional activity (PubMed:22437732). CC {ECO:0000269|PubMed:10026224, ECO:0000269|PubMed:22437732}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via PDZ2 domain) with CC TJP1/ZO1 (via PDZ2 domain) (PubMed:10026224). Interacts with UBN1 (By CC similarity). Interacts with SCRIB (By similarity). Interacts with OCLN CC (PubMed:10026224). Interacts with SAFB in the nucleus CC (PubMed:12403786). Interacts with USP53 (via the C-terminal region) CC (PubMed:26609154). Interacts with claudins, including CLDN1, CLDN2, CC CLDN3, CLDN5 and CLDN7 (By similarity). Interacts with CLDN18 CC (PubMed:22437732). Interacts (via N-terminus) with CTNNA1 CC (PubMed:10026224). {ECO:0000250|UniProtKB:Q9UDY2, CC ECO:0000269|PubMed:10026224, ECO:0000269|PubMed:12403786, CC ECO:0000269|PubMed:22437732, ECO:0000269|PubMed:26609154}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus CC {ECO:0000269|PubMed:22437732}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9. DR IntAct; Q9Z0U1; 3. DR MINT; Q9Z0U1; -. DR STRING; 10090.ENSMUSP00000156728; -. DR ChEMBL; CHEMBL4879525; -. DR GlyGen; Q9Z0U1; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9Z0U1; -. DR PhosphoSitePlus; Q9Z0U1; -. DR SwissPalm; Q9Z0U1; -. DR EPD; Q9Z0U1; -. DR jPOST; Q9Z0U1; -. DR MaxQB; Q9Z0U1; -. DR PaxDb; 10090-ENSMUSP00000097154; -. DR PeptideAtlas; Q9Z0U1; -. DR ProteomicsDB; 275312; -. DR Pumba; Q9Z0U1; -. DR DNASU; 21873; -. DR Ensembl; ENSMUST00000099558.5; ENSMUSP00000097154.5; ENSMUSG00000024812.12. DR Ensembl; ENSMUST00000233658.3; ENSMUSP00000156728.3; ENSMUSG00000024812.12. DR GeneID; 21873; -. DR KEGG; mmu:21873; -. DR UCSC; uc008ham.2; mouse. DR AGR; MGI:1341872; -. 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; RQRHSKI; -. DR OrthoDB; 2904077at2759; -. 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 77 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 257 other cell types or tissues. DR ExpressionAtlas; Q9Z0U1; baseline and differential. 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: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:0044325; F:transmembrane transporter binding; 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; cd00992; PDZ_signaling; 3. DR CDD; cd12027; SH3_ZO-2; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1. DR PANTHER; PTHR13865:SF26; TIGHT JUNCTION PROTEIN ZO-2; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 3. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9Z0U1; MM. 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 //