ID A0A3B4Y8N9_SERLL Unreviewed; 1243 AA.
AC A0A3B4Y8N9;
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-2-like {ECO:0000313|Ensembl:ENSSLDP00000019539.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000019539.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000019539.1}
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 AlphaFoldDB; A0A3B4Y8N9; -.
DR Ensembl; ENSSLDT00000020195.1; ENSSLDP00000019539.1; ENSSLDG00000015219.1.
DR GeneTree; ENSGT00940000158634; -.
DR Proteomes; UP000261360; 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 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 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 SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 33..120
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 366..444
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 576..641
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 670..738
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 778..945
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 122..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 140884 MW; D06591E690C53D6E CRC64;
MPVNGGGLLS LSRYATQYFA NPVMEETVWE QYTVTLQRDP KMGFGIAVSG GRDNPNDESG
ETSIVVSDVL QGGPADGLLF ENDRVVQVNA IPMEGAIHSF AVQTLRKCGK VAKITVKRPR
KVPVNLMNRP PSPDDRVFNN DYNDDYNYEQ DRRSVYSARS GGGRDHSLER ERGGGYMDSG
YQTRERDYDR DYDRRERGRS MERDLSPDRQ YRRDGSRGRT LDRERSPDRR YKSDHTLDRD
YSPDRRYRSE RALDREHSPD RRYRSERALD REYSPDRRYR SERMLDRTSP DLRYRRDSHS
PGRGHGRDNS FERGRERIPS DPKKYDEPVK RSGSRDRLDR SPSPAAMPIP LPRPVRDLDP
LDKPMNVLLL KNRPNEEYGL RLGSQLFIKE MTSTGLASRD GNLQEGDIIL KINGTVTENL
SLSDAGKLIE KSRGKLQLVV QRDKQQVLIR VPPMVDSDSE LDDISEIESY RSYSPQDDRR
GHHSDLSSHS SNERLREKPS REEPPNRLAK MGAMPTPFRV PDRTVEDTPP LQTEREDPRP
ETPPVPAVTA APKVHAPPRV PVKPSIEDQE VYGPNTVKVR FQKGDSVGLR LAGGNDVGIF
IAGVQEDSAA EQEGLRTGDQ IMKVNNMDFR GMVREDAVLY LLEMPKGEDV TLLAQSKPEV
YKDILASGRG DSFFIRTHFE YEKEAPQSLP FSRGEIFKVT DTLYDGKLGN WLAIRTDKDN
QLLEKGIIPN KSRAEQMSNV QNAARAASGN DRGDFWRLRG QRAAKKKDLR KSREDLSTAP
VTTRFPAYER VVLREAGFRR PVVIFGPISD AVNEKLANDM PNEFVVAKTE PKDAGSEKSS
GVVRLNTIRQ IIEQDRHALL DVTPKAVDTL NYTQWYPIVI FLNPDSKQGV KTMRNRLLPG
SSRSARKLYE QSVKLRKTCS HLFTAAIDLN SANDAWYGSV KDSIQEQQDR AVWVCEGKLD
GSEEDLDLHD DRMSYLSAMS ADYLSMDSRL TSDYEDTADE GGAYTDNELD EPLDEPQPVS
AISRSSEPVL PDEKLHPEPR TRMRRSGSRE VLNREPSPPP SFVPEPPKVR TQTRTDSSRS
YDSHSSSTIS SDAAGGNKPL PPPVALKPSI PRLNHPTEEP SPAKEEEDPA KKSFLGKIQA
FEKMDHLARA QRMLELQEAE NARLEIAQKH PDIYAVPIKL PKPNLNRPQP IGSSSNPEAQ
TPSRPPYSET RGHDSEEADY RRQLLDQTKR GYYNPQKYKD TEL
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