ID A0A2Y9DE38_TRIMA Unreviewed; 1671 AA.
AC A0A2Y9DE38;
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 X2 {ECO:0000313|RefSeq:XP_004372695.1};
GN Name=LOC101350122 {ECO:0000313|RefSeq:XP_004372695.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004372695.1};
RN [1] {ECO:0000313|RefSeq:XP_004372695.1}
RP IDENTIFICATION.
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_004372695.1; XM_004372638.3.
DR GeneID; 101350122; -.
DR KEGG; tmu:101350122; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000248480; 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 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:UP000248480};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 11..98
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 174..252
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 409..490
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 504..572
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 678..779
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1537..1671
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 105..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..852
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 187274 MW; 30A5DF702922F228 CRC64;
MEETAIWEQH TVTLHRAPGF GFGIAISGGR DNPHFQSGET SIVISDVLKG GPAEGQLQEN
DRVAMVNGVS MDNVEHAFAV QQLRKSGKNA KITIRRKKKI HIPVAHTDPG LVSDHEEDSY
DEEVHDPRSV HGGLVNRRNE KNWSRDRSAS RERSLSPRSD RRSVASSQPA KPTKVTLVKS
RKNEEYGLRL ASHIFVKEIS QDSLAARDGN IQEGDVVLKI NGTVTENMSL TDAKTLIERS
KGKLKMVVQR DERATLLNVP DLSDSIHSAN ASERDDISEI QSLASDHSTR SHDRPPGRSQ
SRSPDQRSEP SDHSRHSPQQ PSNGSLRSRE EERIPKPGAV STPVKHADDH TPKTVEEVIV
ERNEKQAPSL PEPKPVYAQV GQPDVDLPVS PSDGVLPNST HEDGILRPSM KLVKFRKGDS
VGLRLAGGND VGIFVAGVQE DSPAAKEGLE EGDQILRVNN VDFTNIIREE AVLFLLDLPK
GEEVTILAQK KKDVYRRIVE SDVGDSFYIR THFEYEKESP YGLSFNKGEV FRVVDTLYNG
KLGSWLAIRI GKNHKEVERG IIPNKNRAEQ LASVQYTLPK TAGGDRADFW RFRGLRSSKR
NLRKSREDLS AQPVQTKFPA YERVVLREAG FLRPVTIFGP IADVAREKLA REEPDIYQIA
KSEPRDAGTD QRSSGIIRLH TIKQIIDQDK HALLDVTPNA VDRLNYAQWY PIVVFLNPDS
KQGVKTMRMR LCPESRKSAR KLYERSHKLR KNNHHLFTTT INLNSMNDGW YGALKEAIQQ
QQNQLVWVSE GKADGATSDD LDLHDDRLSY LSAPGSEYSM YSTDSRHTSD YEDTDTEGGA
YTDQELDETL NDEVGTPPES AITRSSEPVR EDSSGMHHEN QTYPPYSPQA QPQPIHRIDS
PGFKTASQQV YRKDPHPEEI MRQNHVLKQP AIAHPGPRPD KEPNLSYEPQ LPYVEQQASR
DLEQPPYRYD TSSYTDQFSR NYDHRLRYED RIPTYEEQWS YYDDKQLYQP RPFDNQHPRD
LDSRQHSEES AERGYFPRFE EPAPLSYDSR PRYEQPPRTS TLRHEEQPTP GYDVHNRYRP
EAQPYPSAGP KSSEPKQYFD QYPRSYEQVP SQGFTSKAGQ YEPLHGAAIV PPLIPSSQHK
PEVPPSNTKP LPPPPTLTEE EEDPAMKPQS VLTRVKMFEN KRSASLESKK DINDAASFKP
PEVASKPPGA PIIGPKPAPQ NQFSEHDKTL YRIPEPQKPQ LKPPEDIVRS NHYDPEEDEE
YYRKQLSYFD RRSFESKPTA GHLPEPAKPV HSQSQPNFSS YSSKGKPEVD AADRSFGEKR
YDPVQTPPPP PLPSQYTQPA QPATSASLAL HTRAKGAHGE GNSVSLDFQN SLVSKPDPPP
SQNKPATFRP SNREDTAQST FYPPKSFPDK APVNGAEQTQ KTVTPAYNRF TPKPYTSSAR
PFERKFESPK FSHNLLPSET AHKSDLPSKA PTSPKTLLKT HSSAQPPEFD SGVETFSIHA
DKPKYQINNT STVPKAIPVS PSAVEEDEDE DGHTVVATAR GIFNSNGGVL SSVETGVSII
IPQGAIPEGI EQEIYFKVCR DNSILPPLDK EKGETLLSPL VMCGPHGLKF LKPVELRLPH
CASMTPDGWS FALKSSTSSS GDPKTWQNKC LPGDPNYLVG ANCVSVLIDH F
//
