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Database: UniProt
Entry: A0A091PC01_LEPDC
LinkDB: A0A091PC01_LEPDC
Original site: A0A091PC01_LEPDC 
ID   A0A091PC01_LEPDC        Unreviewed;      1107 AA.
AC   A0A091PC01;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Tight junction protein ZO-2 {ECO:0000313|EMBL:KFQ05110.1};
DE   Flags: Fragment;
GN   ORFNames=N330_04223 {ECO:0000313|EMBL:KFQ05110.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ05110.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ05110.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ05110.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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DR   EMBL; KK671159; KFQ05110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PC01; -.
DR   PhylomeDB; A0A091PC01; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   SMART; SM00326; SH3; 1.
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.
PE   4: Predicted;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          10..97
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          274..352
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          478..559
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          573..638
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          659..845
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          127..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1107
FT                   /evidence="ECO:0000313|EMBL:KFQ05110.1"
SQ   SEQUENCE   1107 AA;  123972 MW;  0A2B65AAA5E03370 CRC64;
     MEELIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND
     RVVIVNGTPM ENVPHSFAVQ QLRKSGKVAT IVVKRPRKVQ AAAFKRSPSL DYEDRALDVM
     DDHAEFDGKS ARSGYSDRSW HSGAGGRSQS WGNSLDQSYR DEQDRGRNRS RDHDRERGYS
     RDRSRGRSVD RSLDRDYRRD RSRGRSIDRD GGYERDYKGD YSPPSYSHGS QPDARYGREV
     RSRSRDRLRS RSPSPEIHHQ HEYLGLQDQN GPISVLLTKG RHNEEYGLRL GSQIFIKEMT
     GTGLATKDGN LHEGDIILKI NGTVTENMSL ADARKLIEKS RGKLQLVVLR DRKQTLLNIP
     SLNDSDSEMD DISEIESNRS LSPQDDRLHH SDLDSHSSNE KLKEKPNAKG DPSSKMSRMG
     AMPTPFTSTG DIATPAVTVT DTNKELKYQD EPAVSQPKAA TRTILKPSPE DEAIYGPNTK
     MVRFKKGDSV GLRLAGGNDV GIFIAGIQEG TSADQEGLQE GDQILKVNTQ DFRGIVREDA
     VLYLLEIPKG ETVTILAQSK YEVYRDIMAC GRGDSFFIRS HFECEKESPQ SLAFTRGEIF
     RVVDTLYDGK LGNWLAVRIG NELEKGLIPN KSRAEQMASV QNAPKDGSSD RADFWRTRGQ
     RSGAKKNLRK SREDLTAIVS VSTKFPAYER VQLREAGFKR PVVIFGPIAD VAMEKLSNDL
     PHLYQTAKTE PRDAGSEKST GVVRLNTVRQ IIEQDKHALL DVTPKAVDLL NYTQWFPIVV
     FFNPDSKQGV KTMRQRLCST SNKSSRKLYE QANKLKKTCS HLFTATINLN SANDSWYGSL
     KDTIQQQQGE AVWVSEGKMD GMEDDADDRM SYLTAMGADY LSCDSRLISD LEDTDGEGGA
     YTDNELDEPL DEPRISSVGR SSEPVHHEES LKKFSPEPRA QLRKAGSREI LREPSPPPAF
     KPEPPKGKLQ NKEDLYDFPK NYDSKSSNIA VSSETSTASA KAAPPPVSVK PAFGRPILRN
     SQPAVPPAEE EEEAKLEEEG SEQENTPKSV LRKVKIFEEM DHKARMQRMQ ELQEAQNARL
     EIAQKHPDIY AVPVKTQKSE QNWPQPM
//
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