GenomeNet

Database: UniProt
Entry: G3UJ07_LOXAF
LinkDB: G3UJ07_LOXAF
Original site: G3UJ07_LOXAF 
ID   G3UJ07_LOXAF            Unreviewed;      1185 AA.
AC   G3UJ07;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Tight junction protein 1 {ECO:0000313|Ensembl:ENSLAFP00000027815.1};
GN   Name=TJP1 {ECO:0000313|Ensembl:ENSLAFP00000027815.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000027815.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000027815.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027815.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000027815.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027815.1};
RG   Ensembl;
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   AlphaFoldDB; G3UJ07; -.
DR   Ensembl; ENSLAFT00000029465.1; ENSLAFP00000027815.1; ENSLAFG00000002222.4.
DR   GeneTree; ENSGT00940000155164; -.
DR   HOGENOM; CLU_006234_1_0_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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; 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   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   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01598; ZONOCCLUDNS1.
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:UP000007646};
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          296..374
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          504..585
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          599..667
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          773..874
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          189..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1129..1158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..943
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..975
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1058
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  133220 MW;  8F2AB82CBED61850 CRC64;
     MEETAIWEQH TVTLHRAPGF GFGIAISGGR DNPHFQSGET SIVISDVLKG GPAEGQLQEN
     DRVAMVNGVS MDNVEHAFAV QQLRKSGKNA KICISLIKAI IFCPLASSCP LPPGPAGDLV
     GQVHGSAFRV GKTHRRWISA HSKVSTLVHI WSIGKEELGK LGQLRNSRTD ARRRDLSLER
     KLKIVEVEKA ERRSQRGSVD RSTMQQRLKT LSKTGINPPR DADRDYARSD PEPVSDHEED
     SYDEEVRDPR SVRSGQVNRR NEKSWTRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV
     KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE
     RSKGKLKMVV QRDERATLLN VPDLSDNISE IQSLASDHSN RSHDRPPRRS RSRSPDQRTG
     STFLKEAPPL RSREEERTPK PGAVSTPVKH VDDHTPKTVE EVTVERNEKQ APTLPEPKPV
     YAQVGQPDVD LPVSPSDGVL PKPSMKLVKF RKGDSVGLRL AGGNDVGIFV AGVLEDSPAA
     KEGLEEGDQI LRVNNVDFTN IIREEAVLFL LDLPKGEEVT ILAQKKKDVY RRIVESDVGD
     SFYIRTHFEY EKESPYGLSF NKGEVFRVVD TLYNGKLGSW LAIRIGKNHK EVERGIIPNK
     NRAEQLASVQ YTLPKTAGGD RADFWRFRGL RSSKRNLRKS REDLSAQPVQ TKFPAYERVV
     LREAGFLRPV TIFGPIADVA REKLAREEPD IYQIAKSEPR DAGTDQRSSG IIRLHTIKQI
     IDQDKHALLD VTPNAVDRLN YAQWYPIVVF LNPDSKQGVK TMRMRLCPES RKSARKLYER
     SHKLRKNNHH LFTTTINLNS MNDGWYGALK EAIQQQQNQL VWVSEGKMRG IGWATDDRLS
     YLSAPGSEYS MYSTDSRHTS DYEDTDTEGG AYTDQELDET LNDEVGTPPE SAITRSSEPV
     REDSSGLHPE NQTYPPYSPQ AQPQPIHRID SPGFKTASQQ YPRSYEQVPS QGFTSKAGQY
     EPLHGAAIVP PLMPSSQHKP EVPPQNTKPL PPPPALTEEE EDPAMKPQSV LTRVKMFENK
     SEHDKTLYRF SEIYQVEHAQ IAICQPLVNL LQISTKILHC VSGLPAATRS RIPEPQKPQP
     KLPEDIVRSN HYDPEEDEEY YRKQLSYFDR RSFESKPSAH IPAGH
//
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