ID A0A2Y9T597_PHYMC Unreviewed; 1688 AA.
AC A0A2Y9T597;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tight junction protein ZO-1 isoform X5 {ECO:0000313|RefSeq:XP_023985498.1};
GN Name=TJP1 {ECO:0000313|RefSeq:XP_023985498.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985498.1};
RN [1] {ECO:0000313|RefSeq:XP_023985498.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985498.1};
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_023985498.1; XM_024129730.3.
DR Proteomes; UP000248484; Chromosome 11.
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:SF28; POLYCHAETOID, ISOFORM O; 1.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 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:UP000248484};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 23..110
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 186..264
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 421..502
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 516..584
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 690..791
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1554..1688
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 103..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 188546 MW; 3DBF925527E17C93 CRC64;
MSARAAAAKN TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD
PEPVSENEED SYDEEVHDPR SGRGGLVNRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ
PARPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
GRSHDRPPRH SRSRSPDQRS EPSDHSRQSP QQPSNGSLRS REEERISKPG AVSTPVKHAD
DHTPKTVEEV IVERNEKQTP NLPEPKPVYA QVGQPDVDLP VSPSDGILPN ATHEDGILRP
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH DHQTYPPYSP
QAQPQPVHRI DSPGLKTASQ QVYRKDPYPE EVMRQNHVLK QPAVAHPGQR LDKEPSLSYE
PQPPYAERQA SRDLEQPAYR YDSSNYADQF PRNYDHRLRY DDCIPAYEEQ WSYYDDKQPY
QPRPSFDNQH PRDLDSRQHP EESSERGYFP RFEEPTPLSY ESRPRYDPPL RTSTLRHEEQ
PAPGFDVHGR YRPDAQPYSS TGPKASEPKQ YFDQYPRSYE QVPPQGFTSK AGPGHYEPLH
GAALVPPQHK PEVPPASTKP LPPPPALAEE EEDPAMKPQS VLTRVKMFEN KRSASVENKK
DENHNSGFKP PEVTSKPAGA PILGPKAPAQ NQLIEHDRTL HRIPEPQKPQ MKPPEDIVRS
NHYDPEEDEE YYRKQLSYFD RRSFESKPSA HVPASHLSEP TKPVHSQSQP QFSSYSSKGK
SAEAEAVDRP FGEKRYEPLQ ATPPPPPPPA QYSQATQPGP STTLSLHSHT KGTLGEGNSM
SLDFQSSLVS KPDPPPSQNK PAAYRPANRE DAAQSAFYPQ KSFPDKAPAN GAEQTQKTIT
PAYNRFTPKP YTSSARPFER KFESPKFSHN LLTSETTHKP DLPSKAPTSP KTLVKAHGST
QPPEFDSGVE TFSVHADNKP KYQVNSISTG PKAVPVSSSA VEEDEDEDGH TVVATARGVF
NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC
GPHGLKFLKP VELRLPHCAS MTPDGWSFAL KSSDSSSGDP KTWQNKCLPG DPNYLVGANC
VSVLIDHF
//
