ID A0A3B4VG84_SERDU Unreviewed; 1651 AA.
AC A0A3B4VG84;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Tight junction protein ZO-1-like {ECO:0000313|Ensembl:ENSSDUP00000029582.1};
GN Name=TJP1 {ECO:0000313|Ensembl:ENSSDUP00000029582.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000029582.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000029582.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSSDUT00000030085.1; ENSSDUP00000029582.1; ENSSDUG00000021279.1.
DR GeneTree; ENSGT00940000155164; -.
DR Proteomes; UP000261420; Unplaced.
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; 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 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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 21..108
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 181..259
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 413..494
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 508..576
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 682..783
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1530..1651
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 113..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1651 AA; 184190 MW; 0016B2F5E2C0405C CRC64;
LSAEAALFAA MEETVIWEQH TVTLHRAPGF GFGIAISGGR DNPHFQSGET SIVISDVLKG
GPAEGLLQEN DRVVMVNAVS MDNVEHAYAV QQLRKSGKIA KITIRRKRKV HVPMGRLGER
ETMSEHDEEE DSYDEEIYET RSGGRSSGRR DRERERSGSR ERSVSPRSDR RSHNLPPRPA
KVTLVKSRKN EEYGLRLASH IFVKDISPES LAARDGNIQE GDVVLKINGT VTENLSLIDA
KKLIERSKGK LKMVVQRDER ATLLNIPDLD DSIPSANASD RDDISDIHSL ASDHSNRSHD
RHRSSRSRSP DRRSEPSDHS RHSPPQISNG SHRSRDDERL SKPASTPAKL AEEVPLPKPK
ESAIGREEKQ LPPLPEPKPV YAQPGQPDVD LPVSPSDAPV PSAAHDDSIL RPSMKLVKFK
KGESVGLRLA GGNDVGIFVA GVLEDSPAAK EGLEEGDQIL RVNNVDFANI IREEAVLFLL
DLPKGEEVTI LAQKKKDVYR RIVESDVGDS FYIRTHFEYE KESPYGLSFN KGEVFRVVDT
LYNGKLGSWL AIRIGKNHQE VERGIIPNKN RAEQLSSVQY TLPKTAGGDR ADFWRFRGLR
SSKRNLRKSR EDLSSQPVQT KFPAYERVVL REAGFLRPVV IFGPIADVAR EKLSREEPDL
FELAKSEPRD AGTDQRSSGI IRLHTIKQII DRDKHAVLDI TPNAVDRLNY AQWYPIVVFL
NPDNKQGVKN MRTRLCPESR KSARKLYERA IKLRKNNHHL FTTTINLNNM NDGWYGALKE
TIQQQQNQLV WVSEGKADGT TEDDLDIHDD RLSYLSAPGS EYSMYSTDSR HTSDYEDTDT
EGGAYTDQEL DETLNDEVGL PTEPAITRSS EPVREDPPVI QDTPGYPGYQ HPVQPDPASR
IDPAGFKMAA PQQMYKKDLY NMEDPVRINH GLKPSMSYSH QPPYQDKQPY REYDHPPYGY
DGGGYGEPKP HNTDSHLHYD NRVPHYNEQW PPYDQQTSSS QPAGYQTGHQ QPMGYNPRSP
YEDGPGRDYS PPQPRYDEAS PVGYDGRPRH SKPGPIRYDE PPPPPPAGYD ARSPYETEPL
GFPINSPRSP EPPKQYYGDS GLRPTYIPGP PNRGYKPGIH DPMINSEPTI PPPKPETLPS
PGEPVVTPGS KPLPPPPRED LDEDPAMKPQ SVLNRVKMFE NKRSMQEALK RHTLLAFQSA
DVPKPVSAPG PVLKANSLSN LEQEKSTYRA PEPQKPHTKP LDDVVRSNHY DPDEDEEYYR
KQLSYFDRRS FDSKAMGQPA PGINRFHDLP KPAQLSYPYN RYKNVAHAGR VSPVEKRYEP
LPQISPSSQY GPPASAIPPN TLLYLSDCIL LTFPANSIPE PLSSPNPKPE LAPLRPASRD
EPTPGGYLPP RGLPDKSPVN GTDAAPPKTL GAPAPTSYNR YVPKPYTSSA RPFERKFESP
KFNHNLLPND TQVKTDLLSK PSVVSSGSSG KPQLSPQPLD HDSGLDTFTR TMDNRPKYQH
NNINTIPKAI PVSPSALEDD DEDEGHTVVA TARGIFNCNG GVLSSIETGV SIIIPQGAIP
ESVEQEIYFK VCRDNSILPP LDKEKGETLL SPLVMCGPHG LKFLKPVELR LPHCASMTPD
GDPKTWQNKS LPGDPNYLVG ANCVSVLIDH F
//
