ID A0A1S3M6M3_SALSA Unreviewed; 1191 AA.
AC A0A1S3M6M3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tight junction protein ZO-2-like {ECO:0000313|RefSeq:XP_013998842.1};
GN Name=LOC106570821 {ECO:0000313|RefSeq:XP_013998842.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013998842.1};
RN [1] {ECO:0000313|RefSeq:XP_013998842.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013998842.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_013998842.1; XM_014143367.1.
DR AlphaFoldDB; A0A1S3M6M3; -.
DR STRING; 8030.ENSSSAP00000047515; -.
DR PaxDb; 8030-ENSSSAP00000047515; -.
DR KEGG; sasa:106570821; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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 InterPro; IPR005419; ZO-2.
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 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:UP000087266};
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 314..392
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 449..529
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 543..611
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 749..851
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 116..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 130827 MW; BCC88F35DA9AD1B2 CRC64;
MPVKGVGKVA AYPSKGEAIG SSGMEETVWE QHTVNLQRDS KMGFGIAVSG GRDNPNADNG
EMSIIVSDVL QGGPADGLLF EKDRVIQVNS ILMDNVPHSF AVQQLRKCGK TAKITVKRPR
KVALPSLKHP PSPGGESRDF GTTRYYDADD NQSDGGWQRG NGGPGYTHEP RDLTPDNKNY
LDPDYGSRGN RGRSRGRSQE RASPSPEHRR DNSKGRALDR EPPSPEKLRY PRERSRGSST
DRERGEGGGG SPGGRSYGRG DSYERGGGRY GDVGGTGGRM VKSKSRDQLQ EPSSPDLPRG
GGARDLEPLE KPVNVLLVKN RPNEEYGLRL GSQIFIKEMT STGLATKDGN LQEGDIILKI
NGTVTENLSL NDAGKLIEKS RGKLQLVIQR DRRQILIRIP PLVDSDSEPD DISEMESYHS
YSPQEDRRSR QSDLSSHSSN ERDYPRANTV MVSFQKGDSV GLRLAGGNDV GIFIAGVQEG
SPAEEEGLRT GDQIMKVNKV DFRGIVREEA VLCLLEIPKG EDVTILAQSK PDVYNDILVS
GRGDSFFIRT HFEYERETPQ SLAFSRGEIF KVVDTLYDGK LGNWLAIRTG KDKQLLEKGI
IPNKSRADQM ASVQNSHKAA GMDRADFWRL RGQRAAKRKD LRKSREDVST TPIATRFPAY
ERVVLREVDG ASPVDGASPV DGASSVDGAS PVDGASSVDG ASPVDGASPV AQLSNNTVSV
FCVRLSLRLC PPSETEPKDA GSEKSSGVVR LNTIRQIIEQ DKHALLDVTP KAVDTLNYSQ
WYPIVIFFNP DSKPGVKAMR QRVIPGSNRS ARKLYEQAVK LRKTCSHLFS ATIEVNSVND
AWYGSVKDSI REQQTQAVWV SEGKLDGTGT DLDLHDDRMS YLSAMSADYL SMDSRLASDY
DDTADEGGAY TDNEPDNEPA DQLPVSAISR SSEPVLAEEI LRRCSPEIRG GIRRVGSREV
LSSASPAHAF VPDPPKVKLL FRDEVVPPRG VVGAYDAPPS RGYDSHSSSP ASNDPPPLPR
SLNSFGKAKP LALQPPVTLK PSYNIQDPTS STAPVTVAPM GPEEPEENPE DPSLRSFLGK
VKAFEKMDHF ARAQRMLELQ EAHNARLEIA QKHPDIYAVP LKTQKLDHSR PQPIGSSSHP
EPQTHPSKLP YSESRGFYLS DEEEEYRRQL AEHTKRGYYQ VNNQKYQDTE L
//
