ID A0A093LNW2_FULGA Unreviewed; 1771 AA.
AC A0A093LNW2;
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:KFW10471.1};
DE Flags: Fragment;
GN ORFNames=N327_02969 {ECO:0000313|EMBL:KFW10471.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW10471.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW10471.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW10471.1};
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; KK608279; KFW10471.1; -; Genomic_DNA.
DR Proteomes; UP000053806; 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:UP000053806};
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 1637..1771
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 815..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1593
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..914
FT /note="Polar 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 1423..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW10471.1"
FT NON_TER 1771
FT /evidence="ECO:0000313|EMBL:KFW10471.1"
SQ SEQUENCE 1771 AA; 198364 MW; 227E44858EB02F3B 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 DDTSKTVEDV
AVERTEKQTP PLPEPKPVYA 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 VREDSSGMHH ETQTYPTYAS QAQPQPNLRI
DSSGFKTTTA QPKAEASPAV PYLSPSPESN PATSSTSAVN ANVNLTNVRL EEPTAAPYNS
YQPQVGPLRT SSTEGAHIVL RDQESSSLSP HIDPAKVYRK DPYINEEVSR QSYVLKQPAI
NHPVQRQERD PNLIYESQAQ YAEKQPSRDY EQSTYRYNST NYVDQFSRGY DPRLHYDDRV
PPYEEHWAYY DEKQPYNQTR TVYENQPPRD LDSRQNIEES TERSYYPAQP RFEEPPPMSY
DGRPRYEHAP KNFSLPQVRY EDQHTVGYDT HGRYKQEAQP YQSAISRSPE PKQYFDPHIR
GYEQGPPQAY NAKAGQYEPS HSTSGVSLPP PPSSQTKPEV LPSNSKPLPT PPSLAEEEED
PAMKPQSVRS RVKIFERRRS PSLEKMKDPS DTSAVKPPEL APKPTLATVS GPKPTSQSQY
EHDKTTYRAP EPQRPQVKPP EDIVRSNHYD PEEDEEYYRK QLSYFDRRSF ENKPSAQVPA
SHQSEPTKPI HSQNQLNFTN YSKGKPTDTE SMERPVGEKR YEPISQVTTS PPAPSVQYTQ
PQSINSPVLS LPAHHKPALS EGEHSAIFIC AAVNSVSDPP PPQNKPAVFR SSREDTVQST
YYPQKSFPDK GPVNGTEQIQ KTVTPSYNRF TTKPYTSAAR PFERKFESPK FNHNLLPNEA
QHKPELPSKS PNSPQPILKA HSSSQPPEFD SGMDTFAVQV DKPKYQPNNV NAVPKAIPVS
PSALEDEEEE DGHTVVATAR GVFNSNGGVL SSIETGVSII IPQGAIPEGI EQEIYFKVCR
DNSILPPLDK EKGETLLSPL VMCGPHGLKF LKPVELRLPH CASMTPDGWS FALKSSDSSS
GDPKTWQNKS LPGDPNYLVG ANCVSVLIDH F
//
