ZO2_CANLF
ID ZO2_CANLF Reviewed; 1174 AA.
AC Q95168;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 151.
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 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=8824195; DOI=10.1074/jbc.271.42.25723;
RA Beatch M., Jesaitis L.A., Gallin W., Goodenough D.A., Stevenson B.R.;
RT "The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-Large/ZO-
RT 1) domains and an alternatively spliced region.";
RL J. Biol. Chem. 271:25723-25726(1996).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8132716; DOI=10.1083/jcb.124.6.949;
RA Jesaitis L.A., Goodenough D.A.;
RT "Molecular characterization and tissue distribution of ZO-2, a tight
RT junction protein homologous to ZO-1 and the Drosophila discs-large tumor
RT suppressor protein.";
RL J. Cell Biol. 124:949-961(1994).
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).
CC -!- FUNCTION: Plays a role in tight junctions and adherens junctions.
CC -!- SUBUNIT: Homodimer, and heterodimer with TJP1/ZO1 and UBN1. Interacts
CC 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) (By similarity). {ECO:0000250|UniProtKB:Q9UDY2,
CC ECO:0000250|UniProtKB:Q9Z0U1, ECO:0000269|PubMed:12403786}.
CC -!- INTERACTION:
CC Q95168; Q9EPK5: Wwtr1; Xeno; NbExp=4; IntAct=EBI-8304003, EBI-1211920;
CC Q95168; E3Q1N2: ZASP; Xeno; NbExp=5; IntAct=EBI-8304003, EBI-8310421;
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:0000250|UniProtKB:Q9Z0U1}. Note=Also nuclear under environmental
CC stress conditions and in migratory endothelial cells and subconfluent
CC epithelial cell cultures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95168-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95168-2; Sequence=Not described;
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; L27152; AAC37332.1; -; mRNA.
DR RefSeq; NP_001003204.1; NM_001003204.1. [Q95168-1]
DR AlphaFoldDB; Q95168; -.
DR SMR; Q95168; -.
DR BioGRID; 139773; 1.
DR IntAct; Q95168; 2.
DR MINT; Q95168; -.
DR STRING; 9615.ENSCAFP00000041484; -.
DR iPTMnet; Q95168; -.
DR PaxDb; Q95168; -.
DR PRIDE; Q95168; -.
DR GeneID; 403854; -.
DR KEGG; cfa:403854; -.
DR CTD; 9414; -.
DR eggNOG; KOG3580; Eukaryota.
DR InParanoid; Q95168; -.
DR OrthoDB; 1175136at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
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; 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; 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 Alternative splicing; Cell junction; Cell membrane; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..1174
FT /note="Tight junction protein ZO-2"
FT /id="PRO_0000094542"
FT DOMAIN 10..97
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 291..369
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 493..574
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 588..653
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 679..860
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 125..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1174
FT /note="Interaction with SCRIB"
FT /evidence="ECO:0000250"
FT COMPBIAS 125..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
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:0000250|UniProtKB:Q9Z0U1"
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 151
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 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 558
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1"
FT MOD_RES 889
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 909
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 917
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0U1"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 1102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDY2"
SQ SEQUENCE 1174 AA; 132086 MW; 45AB836BBDDB1226 CRC64;
MEELIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND
RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ LAPPQGSLPV DEDDRAFEVM
DEFDGRSARS GYSERSRRSS HGGRSRSWED SPERGRPHER AWSQERERSR GRSLERGLDH
DDDYRRPRER SRGRSLERGL DHDDDYGRPG ERSHGMSTDR GYDRGYDRGY DRGYDRTYSP
EAEYGRRTQP DARHAGSRSR SREHLRSRSP SPELRGRPDH AGQPDSDRPI GVLLMKSKAN
EEYGLRLGSQ IFIKQMTRTA LATKDGNLHE GDIILKINGT VTENMSLTDA RKLIEKSRGK
LQLVVLRDSK QTLINIPSLN DSDSEIEDIS EIESNRSFSP EERRQQYSDY DYHSSNEKLK
ERPNSREDMQ NRWSRMGATP TPFKSMGDIA SVVGTENSKE PRYQEEPPAP QPKAAPRTFL
RPSPEDEAIY GPNTKMVRFK KGDSVGLRLA GGNDVGIFVA GIQEGTSAEQ EGLQEGDQIL
KVNTQDFRGL VREDAVLYLL EIPKGEMVTI LAQSRADVYR DILACGRGDS FFIRSHFECE
KETPQSLAFS RGEVFRVVDT LYDGKLGHWL AVRIGNELEK GLIPNKSRAE QMASVQNAQR
DNAGDRADFW RMRGQRSGMK KNLRKSREDL TAAVSVSTKF PAYERVLLRE AGFKRPVVLF
GPIADIALEK LANELPDLFQ TAKTEPKDAG SEKSSGVVRL NTVRQIIEQD KHALLDVTPK
AVDLLNYTQW FPIVIFFNPD SRQGVKTMRQ RLNPTSNKSS RKLYDQANKL KKTCAHLFTA
TINLNSANDS WFGSLKDTIQ HQQGEAVWVS EGKMEGMDDD PEDRMSYLTA MGADYLSCDS
RLISDFEDTD GEGGAYTDNE LDEPAEEPLV SSITRSSEPV QHEESIRKPS PEPRAQMRRA
ASRDQLRDSS PPPAFKPEPP KAKTQNREES FDISRSHDYK SNPSAVAGNE VSGASTRSCP
PPIAAKPSFG RSILKPSTPV PSPESEEVGE GSEEQEGAPK SVLGKVKIFE KMDHKARLQR
MQELQEAQNA RIEIAQKHPD IYAVPIKTHK PDPGLSQHTS SRPPEPQKGP SRLYQDPRGS
YGSDAEEEEY RQQLSEHSKR GYYSQPSRYR DTEL
