ID A0A1S3L0G0_SALSA Unreviewed; 1225 AA.
AC A0A1S3L0G0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Tight junction protein ZO-2-like isoform X2 {ECO:0000313|RefSeq:XP_013984305.1};
GN Name=LOC106563322 {ECO:0000313|RefSeq:XP_013984305.1};
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_013984305.1};
RN [1] {ECO:0000313|RefSeq:XP_013984305.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013984305.1};
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_013984305.1; XM_014128830.1.
DR AlphaFoldDB; A0A1S3L0G0; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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 37..124
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 350..428
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 562..628
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 657..725
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 763..931
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 129..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 138389 MW; 38F7AB526B29DAB3 CRC64;
MKTVLHLHRK WIHTYKAIRI LQGLSPVMEE TVWEQYTVTL QRDPKMGFGI AVSGGRDNPN
EESGEMSIVV SDVLQGGPAD GLLFENDRVV QVNAIPMDNV PHSFAVQTLR KCGKVAKVTV
KRPRKVPVNL LKRAPSPDDR VFSNDYNDDY DYEQDRRSVY SGRSSHQDRD HSQERGGYTD
AGYQGRGFDR DYGRDDRGRS MERDLHPDRQ YRRDGSMGRT LDRERSPDRR YKSDLTLDRD
HSPDRRYRSE RALDRDPSPD RRFRSERTLD RTNSPDRRYR AGHSPARSHG RDHSFERNRE
RVPSDHDHRK EQMKRSGSRE RLDRSPSPTA MPVPKARPPR EQEPLEEPLN VLLLKNRPNE
EYGLRLGSQL FIKEMTSTGL ACRDGNLQEG DIILKINGTV TENLSLSDAG KLIEKSRGKL
QLVVQRDRRQ VLVRIPPLAD SDSELDDISE IESYRSYSPQ DDRRAPHSDL SSHSSNERLR
DKPREEPPSR LAKMGAMPTP FAMPARKPAR VVEDTPLLPA ERVEPRPETP PAPAVTVAPK
VHAAPKVPLT PSIEDQEIYG PNTVMVRFQK GESVGLRLAG GNDVGIFIAG IQEDSPAEQE
GLHTGDQIMK VNNMDFRGMV REDAVLYLLE IPKGDDVTIL AQSKPDVYKD ILASGRGDSF
FIRTHFEYEK EVPQSLPFSR GEIFNVTDTL YDGKLGNWLA IRTDKDNQLL EKGIIPNKSR
AEQMSNVQNA QRGTANDRGD FWRLRGQRAA KKKDLRKSRE DLTATPVTTR FSAYERVVLR
EAGFRRPVVV FGPIADAVNE KLANDLPEEF VIAKTEPKDA GADKSSGVVR LNTIRQIIEQ
DRHALLDVTP KAVDTLNYTQ WYPIVVFLNP DSKGGIKTMR NRLVPGSSRS ARKLYEQAVK
MRKTCSHLFT ATVDLNSAND GWYGSVKDSI RAQQERAVWI CEGKLDGSEE ELDIHDDHMS
YLSAMSADYL SMDSRLTSDF DDTADEGGAY TDNELDEPMD EPHQPVSAIS RSSEPVLPEE
RPHPAPIPRM RRSGSREVLR DPSPPPTFVP EPPKVRVQSR GGYDSHSSST ISSDAAGGSK
PAPPPVALKP TLRALGQSSE DYSVQGGEDP ANRSFIGKVK AFEKMDHLAR AQRMLELQEA
EQARLEIAQK HPDIYAVPVK LPKPNRPQPI GSSSNPEPQT QSSRPPYSDS RGHYDDDEEE
YRRQLANQTR RGYYSNPQKY KDTEM
//
