ID A0A093EQ13_9AVES Unreviewed; 1770 AA.
AC A0A093EQ13;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Tight junction protein ZO-1 {ECO:0000313|EMBL:KFV16601.1};
DE Flags: Fragment;
GN ORFNames=N339_04781 {ECO:0000313|EMBL:KFV16601.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV16601.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV16601.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV16601.1};
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; KL248798; KFV16601.1; -; Genomic_DNA.
DR Proteomes; UP000053149; 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; cd12026; SH3_ZO-1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.60.220.30; -; 1.
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; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR PANTHER; PTHR13865:SF25; TIGHT JUNCTION PROTEIN ZO-1; 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; 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.
DR PROSITE; PS51145; ZU5; 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:UP000053149};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 14..101
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 178..256
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 411..492
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 506..574
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 680..781
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1636..1770
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 105..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV16601.1"
FT NON_TER 1770
FT /evidence="ECO:0000313|EMBL:KFV16601.1"
SQ SEQUENCE 1770 AA; 198287 MW; 739FAB9EF0662477 CRC64;
STTMEETAIW EQHTVTLHRA PGFGFGIAIS GGRDNPHFQS GETSIVISDV LKGGPAEGLL
QENDRVAMVN GVSMDNVEHA FAVQQLRKSG KNAKITIRRM KKIQIPVARP EPEPVSENED
DSYDEEIRDP RSSRGGPSAN RRHEKSWVRD RSASRERSLS PRSDRRSVTS SQPAKPTKVT
LVKSRKNEEY GLRLASHIFV KEISQDSLAA RDGNIQEGDV VLKINGTVTE NMSLADAKTL
IERSKGKLKM VVQRDERATL LNVPDLSDSI HSANASERDD ISEIQSLASD HSNRSHDRPR
RSRSRSPDQR SEPSDHSRHS PQQPSNGSLR SREDERITKP GAVSTPVKNA DDISKTMEEV
SVERTEKQTP PIPEPKPVYA QGGQPDVDLP VSPSDGPLPN STHEDGMLRP SMKLVKFRKG
DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL
PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD FWRFRGLRSS
KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK LAREEPDIFQ
IAKSEPRDAG TDQRSSGIIR LHTIKQIIDR DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP
DSKQGVKTMR MRLCPESRKS ARKLYERAHK LRKNNHHLFT TTINLNSMNE GWYGALKEAI
QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGIHH ETQTYPTYAS QAQPQPNLRI
DSSGFKTTTT QPKAEASSAV PYLSPSPESN PATSSTSAVN ANVNLTNVRL EEPTTAPFNS
YQPQAGPLRT SSAEGAHIVL RDQEPSSLSP HIDPAKIHRK DPYINEEVSR QSYVLKQPAV
NHPVQRQERD PNLIYESQAQ YAEKQPSRDY EQSTYRYDST NYVDQFSRGY DPRLHYDDRV
PPYEEHWAYY DEKQPYNQAR TVYENQPPRD LDSRQKLEES TERSYYPAQP RFEEPPPMSY
DGRPRYEHAP KNFSLPQVRY EDQHTVGYDT HGRYKQEAQP YQSAISRSPE PKQYFDPHIR
GYEQGPPQAY NAKAGQYEPS HSTSGVSLPP PPSSQTKPEV LPSNSKPLPT PPSLAEEEED
PAMKPQSVRS RVKIFERRRS PSLEKMKDPT DTSAVKPPEL APKPALTTVS GPKPTSQSQY
DHDKTTYRAP EPQRPQVKPP EDIVRSNHYD PEEDEEYYRK QLSYFDRRSF ENKPSAQVPA
SHHSEPTKPI HSQNQLNFTN YSKGKPTDTE SMDRPVGEKR YEPVPQVTTP PPPSVQYTQP
QSINSPVLSL PAHHKPALSE VTSSGIFICI AVNSVSDPPP PQNKPAIFRS SREDTVQSTF
YPQKSFPDKG PVNGTEQLQK TVTPSYNRFT TKPYTSAARP FERKFESPKF NHNLLPNEAQ
HKPELPSKSL NSPQPVLKAH SSSQPPEFDS GMDTFAVQVD KPKYQPNNVN AVPKAIPVSP
SALEDEEEED GHTVVATARG VFNSNGGVLS SIETGVSIII PQGAIPEGIE QEIYFKVCRD
NSILPPLDKE KGETLLSPLV MCGPHGLKFL KPVELRLPHC ASMTPDGWSF ALKSSDSSSG
DPKTWQNKSL PGDPNYLVGA NCVSVLIDHF
//