ID A0A1S3KUJ6_SALSA Unreviewed; 1915 AA.
AC A0A1S3KUJ6;
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-1-like isoform X1 {ECO:0000313|RefSeq:XP_013982285.1};
DE SubName: Full=Tight junction protein ZO-1-like isoform X2 {ECO:0000313|RefSeq:XP_013982286.1};
GN Name=LOC106562151 {ECO:0000313|RefSeq:XP_013982285.1,
GN ECO:0000313|RefSeq:XP_013982286.1};
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_013982285.1};
RN [1] {ECO:0000313|RefSeq:XP_013982285.1, ECO:0000313|RefSeq:XP_013982286.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013982285.1,
RC ECO:0000313|RefSeq:XP_013982286.1};
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_013982285.1; XM_014126810.1.
DR RefSeq; XP_013982286.1; XM_014126811.1.
DR KEGG; sasa:106562151; -.
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 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:UP000087266};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 147..234
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 329..408
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 578..659
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 673..741
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 856..957
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1781..1915
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 227..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1486..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 210944 MW; 79422A344CBBCE23 CRC64;
MKYQKYITVM QMAMGVTAIN RDNCIPPKRQ MWVTPTDGLS GIGATGIGTA ASSAAITEAQ
DSAEAAAEDA AAARAAARAG AMCGSGAIGG CSVMFATSTL SLPMTQGKPS LRRIKGRIHR
SKSLDSIDLL DSNSAAMEET VIWEQHTVTL HRAPGFGFGI AISGGRDNPH FQSGETSIVI
SDVLKGGPAE GLLSENDRVV MVNAVSMDNV EHAYAVQQLR KSGKNAKITI RRKRRVQIPV
SHPGDRETMS EHEEEDTDED DGYEQHSGRS GPTSAYGAAS GGTASRRTND RERERSNSSR
REHSASRERS ISPHSGRSQG SSTPSRPAKV TLVKSRKNEV EYGLRLASHI FVKDISPESL
AARDGNIQEG DVVLKINGTV TENLSLIDAK KLIERSKGKL KMVVQRDDRA TLLNIPDMDD
SIPSGNNSDR DDISEIHSLT SDHSTRSHDR ARGSRSRSPT RSEPSDPSRH SPRQISNGSW
RLKNAGTFLH RILPLHRSRD EERISKPGVM STPVKGSQEA LIQAISDQPL AREDKLPPLP
EPKPVYAQPG QPDVDLPVSP SDAPVPSAGH DDSILRPSMK LVKFKKGESV GLRLAGGNDV
GIFVAGVLED SPAAKEGLEE GDQILRVNNV DFANIIREEA VLFLLDLPRG EEVTILAQKK
KDVYRRIVES DVGDSFYIRT HFEYEKESPY GLSFNKGEVF RVVDTLYNGK LGSWLAIRIG
KNHQEVERGI IPNKNRAEQL SSVQYTLPKT PGGDRADFWR FRGLRTSKRN LRKSREDLSA
QPVQTKFPAY ERVVLREAGF LRPVVIFGSI ADVAREKLAR EEPDLFELAK TQQHEGVEKS
EPKDAGKDQR SSGIIRLHTI KQIIDRDRHA VLDITPNAVD RLNYAQWYPI VVFLNPDSKQ
GVKTMRTRLC PESRKSARKL YERALKLRKN NHHLFTTTIN MNNMNDGWYG ALKETIQQQQ
NQLVWVSEGK ADGAPDDDLD LHDDRLSYLS APGSEYSMYS TDSRHTSDYE DTDTEGGAYT
DQELDETLND EVGLPTEPAI TRSSEPVRED PPVIQEPLRY GGYQHTVQPD PLNRIDPAGF
KAPVAQQNEK AEAVPATMPI LPQQPEQPVL LAETEAAPTA VNNTVNGVAG LSHGLSLGPI
AAPQSKPNPG PGPEADRLRM PTPDLAQPLA PAPTLEPEPL QSGPPSSEPQ MYKKDPYLEE
PVRVNHGGVK PSPAMGPPMT YESQPPYQDQ HPYRDYDHPP NRYDGGGYLE PKYRNFDSQL
HHEKNVPHYD DQWPPYNQQT SGPPPHQQQH PPGPGYDPRL SYEDGPERDY SPPQLRYDET
PLGYNGRPRY GKPAGPGPIR YDEPPPSVPG GYAPLRYDQE PHPYPPATRS PEPPKQYYQG
EPAQRPGPAY NQAPPQHRGY KPPPQQYEPI MSFDAPVPAP KPQPEALRPS PGDTVITTAP
NPLPPPPRVE LEDDPAIRAQ SVLSRVKMFE NKRSVSVDRA KEAGDTVGLR SADLPTKPGA
CIPKANSLSN LDQEKSFRVP EPQKPREVSD DDIVRSNHYN PDEDEEYYRK QLSYFDRRSL
DAVKAPPQTT PVIATKPAAQ PQAHPGYNYP RAESVEKVSP VERRYEPVPQ VTPAAPPAIL
PKPTSPEDPH DSPKADTVTT NYLPQKSYPE KSPVNGTAMK DQPKAPANTS YNRYVPKPYT
NSAKPFERKF DSPKFNHNLL PNNKTDLAPA IKAPANSTAP AKPQISPQPT DLDSGLDTFT
RTMDNRSKYQ HNNINAVPKA IPVSPSALED DDEDEGHTVV ATARGVFNCN GGVLSSIETG
VSIIIPQGAI PEGVEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH GLKFLKPVEL
RLPHCASMTP DGWSFALKSS DSSSGDPKSW QNQSLPGDPN YLVGANCVSV LIDHF
//
