ZO1_CANLF
ID ZO1_CANLF Reviewed; 1769 AA.
AC O97758;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tight junction protein ZO-1 {ECO:0000250|UniProtKB:Q07157};
DE AltName: Full=Tight junction protein 1 {ECO:0000250|UniProtKB:Q07157};
DE AltName: Full=Zona occludens protein 1 {ECO:0000303|PubMed:10094817};
DE AltName: Full=Zonula occludens protein 1 {ECO:0000250|UniProtKB:Q07157};
GN Name=TJP1; Synonyms=ZO1 {ECO:0000303|PubMed:10094817};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=10094817; DOI=10.1006/excr.1999.4392;
RA Gonzalez-Mariscal L., Islas S., Contreras R.G., Garcia-Villegas M.R.,
RA Betanzos A., Vega J., Diaz-Quinonez A., Martin-Orozco N.,
RA Ortiz-Navarrete V., Cereijido M., Valdes J.;
RT "Molecular characterization of the tight junction protein ZO-1 in MDCK
RT cells.";
RL Exp. Cell Res. 248:97-109(1999).
RN [2]
RP INTERACTION WITH TJP2; OCLN AND F-ACTIN, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9792688; DOI=10.1074/jbc.273.45.29745;
RA Fanning A.S., Jameson B.J., Jesaitis L.A., Anderson J.M.;
RT "The tight junction protein ZO-1 establishes a link between the
RT transmembrane protein occludin and the actin cytoskeleton.";
RL J. Biol. Chem. 273:29745-29753(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH TJP2 AND TJP3.
RX PubMed=10575001; DOI=10.1074/jbc.274.49.35179;
RA Wittchen E.S., Haskins J., Stevenson B.R.;
RT "Protein interactions at the tight junction. Actin has multiple binding
RT partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3.";
RL J. Biol. Chem. 274:35179-35185(1999).
RN [4]
RP INTERACTION WITH HSPA4.
RX PubMed=16407410; DOI=10.1091/mbc.e05-06-0507;
RA Tsapara A., Matter K., Balda M.S.;
RT "The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and
RT regulates transcriptional activity of ZONAB.";
RL Mol. Biol. Cell 17:1322-1330(2006).
RN [5]
RP FUNCTION.
RX PubMed=24986862; DOI=10.1074/jbc.m114.556449;
RA Spadaro D., Tapia R., Jond L., Sudol M., Fanning A.S., Citi S.;
RT "ZO proteins redundantly regulate the transcription factor DbpA/ZONAB.";
RL J. Biol. Chem. 289:22500-22511(2014).
RN [6]
RP FUNCTION, DOMAIN, AND INTERACTION WITH OCLN AND F-ACTIN.
RX PubMed=27802160; DOI=10.1242/jcs.188185;
RA Odenwald M.A., Choi W., Buckley A., Shashikanth N., Joseph N.E., Wang Y.,
RA Warren M.H., Buschmann M.M., Pavlyuk R., Hildebrand J., Margolis B.,
RA Fanning A.S., Turner J.R.;
RT "ZO-1 interactions with F-actin and occludin direct epithelial polarization
RT and single lumen specification in 3D culture.";
RL J. Cell Sci. 130:243-259(2017).
CC -!- FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins
CC that link tight junction (TJ) transmembrane proteins such as claudins,
CC junctional adhesion molecules, and occludin to the actin cytoskeleton
CC (PubMed:9792688, PubMed:10575001, PubMed:27802160). The tight junction
CC acts to limit movement of substances through the paracellular space and
CC as a boundary between the compositionally distinct apical and
CC basolateral plasma membrane domains of epithelial and endothelial
CC cells. Necessary for lumenogenesis, and particularly efficient
CC epithelial polarization and barrier formation (PubMed:27802160). Plays
CC a role in the regulation of cell migration by targeting CDC42BPBb to
CC the leading edge of migrating cells (By similarity). With TJP2 and
CC TJP3, participates in the junctional retention and stability of the
CC transcription factor DBPA, but is not involved in its shuttling to the
CC nucleus (PubMed:24986862). {ECO:0000250|UniProtKB:Q07157,
CC ECO:0000269|PubMed:24986862, ECO:0000269|PubMed:27802160,
CC ECO:0000269|PubMed:9792688}.
CC -!- SUBUNIT: Homodimer, and heterodimer with TJP2 and TJP3 (PubMed:9792688,
CC PubMed:10575001). Interacts with OCLN (PubMed:9792688,
CC PubMed:27802160). Interacts with CALM, claudins, CGN/cingulin, CXADR,
CC GJA12, GJD3 and UBN1 (By similarity). Interacts (via ZU5 domain) with
CC CDC42BPB and MYZAP (By similarity). Interacts (via PDZ domain) with
CC GJA1 (By similarity). Interacts (via PDZ domains) with ANKRD2 (By
CC similarity). Interacts with BVES (via the C-terminus cytoplasmic tail)
CC (By similarity). Interacts with HSPA4 (PubMed:16407410). Interacts with
CC KIRREL1 (By similarity) (PubMed:16407410). Interacts with DLL1 (By
CC similarity). Interacts with USP53 (via the C-terminal region) (By
CC similarity). Interacts with DNMBP (via C-terminal domain); required for
CC the apical cell-cell junction localization of DNMBP (By similarity).
CC Interacts with SPEF1 (By similarity). {ECO:0000250|UniProtKB:P39447,
CC ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:10575001,
CC ECO:0000269|PubMed:16407410, ECO:0000269|PubMed:9792688}.
CC -!- INTERACTION:
CC O97758; Q2TFN9: HSPA4; NbExp=3; IntAct=EBI-6988333, EBI-8002398;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9792688};
CC Peripheral membrane protein {ECO:0000269|PubMed:9792688}; Cytoplasmic
CC side {ECO:0000269|PubMed:9792688}. Cell junction, tight junction
CC {ECO:0000269|PubMed:9792688}. Cell junction
CC {ECO:0000250|UniProtKB:P12830}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:Q07157}. Note=Moves from the cytoplasm to the
CC cell membrane concurrently with cell-cell contact (PubMed:9792688).
CC Distributed over the entire lateral surface of the plasma membrane and
CC other actin-rich structures (PubMed:9792688). Detected at the leading
CC edge of migrating and wounded cells (By similarity). Colocalizes with
CC SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By
CC similarity). {ECO:0000250|UniProtKB:Q07157,
CC ECO:0000269|PubMed:9792688}.
CC -!- DOMAIN: The 244-aa domain between residues 633 and 876 is the primary
CC occludin (OCLN)-binding site and is required for stable association
CC with the tight junction (By similarity).
CC {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The C-terminal region (residues 1151-1372) is an actin-binding
CC region (ABR) that interacts directly with F-actin and plays an
CC important role in the localization of Tjp1 at junctions
CC (PubMed:27802160). The ABR is also required for the localization to
CC puncta at the free edge of cells before initiation of cell-cell contact
CC (By similarity). The ABR is also necessary for Tjp1 recruitment to
CC podosomes (By similarity). {ECO:0000250|UniProtKB:Q07157,
CC ECO:0000269|PubMed:27802160}.
CC -!- DOMAIN: The second PDZ domain (PDZ2) mediates homodimerization and
CC heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also
CC mediates interaction with Gja12 (By similarity).
CC {ECO:0000250|UniProtKB:Q07157}.
CC -!- PTM: Phosphorylated at tyrosine redidues in response to epidermal
CC growth factor (EGF) (By similarity). This response is dependent on an
CC intact actin microfilament system (By similarity). Dephosphorylated by
CC PTPRJ (By similarity). {ECO:0000250|UniProtKB:Q07157}.
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; U55935; AAD11529.1; -; mRNA.
DR RefSeq; NP_001003140.1; NM_001003140.1.
DR AlphaFoldDB; O97758; -.
DR BMRB; O97758; -.
DR SMR; O97758; -.
DR BioGRID; 139675; 3.
DR CORUM; O97758; -.
DR IntAct; O97758; 8.
DR MINT; O97758; -.
DR STRING; 9612.ENSCAFP00000015301; -.
DR PaxDb; O97758; -.
DR PRIDE; O97758; -.
DR GeneID; 403752; -.
DR KEGG; cfa:403752; -.
DR CTD; 7082; -.
DR eggNOG; KOG3580; Eukaryota.
DR InParanoid; O97758; -.
DR OrthoDB; 1175136at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0070830; P:bicellular tight junction assembly; IDA:UniProtKB.
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:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IBA:GO_Central.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IBA:GO_Central.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IBA:GO_Central.
DR CDD; cd12026; SH3_ZO-1; 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; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865:SF25; PTHR13865:SF25; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01598; ZONOCCLUDNS1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00218; ZU5; 1.
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.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell junction; Cell membrane; Gap junction; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..1769
FT /note="Tight junction protein ZO-1"
FT /id="PRO_0000094539"
FT DOMAIN 23..110
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 185..263
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 420..501
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 515..583
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 609..790
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 1635..1769
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT REGION 102..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..875
FT /note="Occludin (OCLN)-binding region"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT REGION 824..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1370
FT /note="Actin-binding region (ABR)"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT REGION 1224..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..863
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 821
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 845
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 847
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 853
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1164
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39447"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
SQ SEQUENCE 1769 AA; 197607 MW; 181E9F36CEBC96EF CRC64;
MSARAAAAKN TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD
PEPVSENEDS YDEEVHDPRS SRGGLVSRRS EKSWARDRSA SRERSLSPRS DRRSVASSQP
PKPTKVTLVK SRKNEEYGLR LASHIFVKEI SQDSLAARDG NIQEGDVVLK INGTVTENMS
LTDAKTLIER SKGKLKMVVQ RDERATLLNV PDLSDSIHSA NASERDDISE IQSLASDHSG
RSHDRPPRHS RSRSPDQRSE PSDHSRHSPQ QPSSGSLRSR EEERISKPGA VSTPVKHADD
HTHKTVEEVV VERNEKQAPS LPEPKPVYAQ VGQPDVDLPV SPSDGVLPNS THEDGILRPS
MKLVKFRKGD SVGLRLAGGN DVGIFVAGVL EDSPAAKEGL EEGDQILRVN NVDFTNIIRE
EAVLFLLDLP KGEEVTILAQ KKKDVYRRIV ESDVGDSFYI RTHFEYEKES PYGLSFNKGE
VFRVVDTLYN GKLGSWLAIR IGKNHKEVER GIIPNKNRAE QLASVQYTLP KTAGGDRADF
WRFRGLRSSK RNLRKSREDL SAQPVQTKFP AYERVVLREA GFLRPVTIFG PIADVAREKL
AREEPDIYQI AKSEPRDAGT DQRSSGIIRL HTIKQIIDQD KHALLDVTPN AVDRLNYAQW
YPIVVFLNPD SKQGVKTMRM RLCPESRKSA RKLYERSHKL RKNNHHLFTT TINLNSMNDG
WYGALKEAIQ QQQNQLVWVS EGKADGATSD DLDLHDDRLS YLSAPGSEYS MYSTDSRHTS
DYEDTDTEGG AYTDQELDET LNDEVGTPPE SAITRSSEPV REDSSGMHHE NQTYPPYSPQ
AQPQPIHRID SPGFKTASQQ KAEASSPVPY LSPETNPASS TSAVNHNVTL TNVRLEGPTP
APSTSYSPQA DSLRTPSTEA AHIMLRDQEP SLPSHVEPAK VYRKDPYPEE MMRQNHVLKQ
PAVGHPGQRP DKEPNLSYES QPPYVEKQAN RDLEQPTYRY DSSSYTDQFS RNYDHRLRYE
ERIPTYEEQW SYYDDKQPYQ PRPSLDNQHP RDLDSRQHPE ESSERGSYPR FEEPAPLSYD
SRPRYDQPPR TSTLRHEEQP TPGYDMHNRY RPEAQSYSSA GPKASEPKQY FDQYPRSYEQ
VPSQGFSSKA GHYEPLHGAA VVPPLIPASQ HKPEVLPSNT KPLPPPPTLT EEEEDPAMKP
QSVLTRVKMF ENKRSASLEN KKDENHTAGF KPPEVASKPP GAPIIGPKPT PQNQFSEHDK
TLYRIPEPQK PQMKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFENKP STHIPAGHLS
EPAKPVHSQN QTNFSSYSSK GKSPEADAPD RSFGEKRYEP VQATPPPPPL PSQYAQPSQP
GTSSSLALHT HAKGAHGEGN SISLDFQNSL VSKPDPPPSQ NKPATFRPPN REDTVQSTFY
PQKSFPDKAP VNGAEQTQKT VTPAYNRFTP KPYTSSARPF ERKFESPKFN HNLLPSETAH
KPDLSSKAPA SPKTLAKAHS RAQPPEFDSG VETFSIHADK PKYQMNNLST VPKAIPVSPS
AVEEDEDEDG HTVVATARGV FNNNGGVLSS IETGVSIIIP QGAIPEGVEQ EIYFKVCRDN
SILPPLDKEK GETLLSPLVM CGPHGLKFLK PVELRLPHCA SMTPDGWSFA LKSSDSSSGD
PKTWQNKCLP GDPNYLVGAN CVSVLIDHF
