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
//