ID A0A099YX96_TINGU Unreviewed; 1083 AA.
AC A0A099YX96;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Tight junction protein ZO-2 {ECO:0000313|EMBL:KGL73548.1};
DE Flags: Fragment;
GN ORFNames=N309_05310 {ECO:0000313|EMBL:KGL73548.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73548.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL73548.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73548.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL886158; KGL73548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YX96; -.
DR STRING; 94827.A0A099YX96; -.
DR Proteomes; UP000053641; 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:UP000053641};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 1..82
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 234..312
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 438..519
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 537..602
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 707..809
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 113..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL73548.1"
FT NON_TER 1083
FT /evidence="ECO:0000313|EMBL:KGL73548.1"
SQ SEQUENCE 1083 AA; 120880 MW; 4BA555B5C32D60F4 CRC64;
DSKRGFGIAV SGGRDNPHFE NGETSIVISD VLPGGPADGL LQENDRVVIV NGTPMENVQH
SFAVQQLRKS GKVATIVVKR PRKVQAAVLR RSPSLDYEDR ALDVMDDHAE FDGRSGYSDR
SWHSGNGGRS QSWGNNLDQS YRADEERGRN RSRERSYSRD GSRGRSIDRD GGYERGYRGD
YSPPRYGHGS HADARYRREA RSRSRDRLYS RSPSPETRHQ HEYLGAQDQE GPVSVLLTKG
KHSEEYGLRL GSQIFIKEMT NTGLATKDGN LHEGDIILKI NGTVTENMSL ADARKLIEKS
RGKLQLVVLR DRKQTLLNIP SLNDSDSEMD DISEIESNRS FSPQDDRLHH SDLDSHSSNE
KLKEKPSAKD DPSSRMSRMG AMPTPFKSTS DITTNTATVA DISKEPKYQD DAPVSQPKPA
ARTILKPSPE DEAIYGPNTK MVKFKKGDSV GLRLAGGNDV GIFIAGIQEG TSADEEGLQE
GDQILKVNTQ DFRGIVREDA VLYLLEIPKG ETVTILAQSK YEVLLLVYRD IMACGRGDSF
FIRSHFECEK ESPQSLAFTR GEIFRVVDTL YDGKLGNWLA VRIGNELEKG LIPNKSRAEQ
MASVQNAQKD GSSDRADFWR TRGQRSGVKK NLRKSREDLT AIASVSTKFP AYERVQLREA
GFKRPVVIFG PIADVAMEKL SNDLPHLYQT AKTEPRDAGS EKSTGVVRLN TVRQIIEQDK
HALLDVTPKA VDLLNYTQWF PIVVFFNPDS KQGVKTMRQR LCSTSNKSSR KLYEQANKLK
KTCSHLFTAT INLNSANDSW YGSLKDTIQQ QQGETVWVSE GKMDGMEDDA DDRMSYLTAM
GADYLSCDSR LISDLEDTDG EGGAYTDNEL DEPLDEPRIS SVSRSSEPVH HEESLKKSSP
EPRAQMRKAG SREILRDPSP PPAFKPEPPK GKLQSKEDLY DFPKSYDSKP SSMAVSSEAP
AVATKPVPPP VSTKPVFGRP VMRNSQPAAP ASEEEEEKLE EEGSEQENTP KSVLRKVKIF
EEMDHKARIQ RMQELQEAQN ARLEIAQKHP DIYAVPVKTQ KSDQNWPQPV SSRAPEPQKP
PGR
//
