ID A0A3P8P9Y9_ASTCA Unreviewed; 1924 AA.
AC A0A3P8P9Y9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Tight junction protein 1b {ECO:0000313|Ensembl:ENSACLP00000013841.1};
GN Name=TJP1 {ECO:0000313|Ensembl:ENSACLP00000013841.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000013841.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000013841.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000013841.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSACLT00000014177.1; ENSACLP00000013841.1; ENSACLG00000009394.1.
DR GeneTree; ENSGT00940000155164; -.
DR Proteomes; UP000265100; Chromosome 7.
DR Bgee; ENSACLG00000009394; Expressed in camera-type eye and 8 other cell types or tissues.
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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 270..357
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 446..525
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 678..759
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 773..841
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 947..1048
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1790..1924
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1924 AA; 214292 MW; 07FEBCAE2E39067F CRC64;
MNRSLDPPSS SPPSSPPSQS LPSDYTVHTL SPLPHTHGRL DAAAFLRECF QPWAGRRRQE
EGDNVQILTV VIKKNTKKKI LKKSQFGWIG GVFARAKKQR KKKTRSECHC RHGSQRYGTF
LSAPRGVFSL SVLQRWKWRC DAEHGRRSGG GCQGLKKYMI TCAFLWVGFL VAVDSTMVNY
QKYITVMQLA LGVTASNKEH CLPPRKRMWI HPSPTAGSGT AASSVSTSQG KPSLRRIKGR
IHRSKSLDSI DLLDSNSAAM EETVIWEQHT VTLHRAPGFG FGIAISGGRD NPHFQSGETS
IVISDVLKGG PAEGLLQEND RVVMVNAVSM DNVEHAYAVQ QLRKSGKLAK ITIRRKRKVH
VPMGRLGERE TMSEHDEEED SYDEEIYETR SGRSGVYSGV GGTMGRRSGR SGGRRDRERE
RSGSRERSLS PRSDRRSHNL PPRPAKVTLV KSRKNEAEYG LRLASHIFVK DISPESLAAR
DGNIQEGDVV LKINGTVTEN LSLIDAKKLI ERSKGKLKMV VQRDERATLL NIPDLDDSIP
SANASDRDDI SDIHSLASDH SNRSHDRHRS SRSRSPDRRS EPSDHSRHSP PQISNGSHRS
RDDERASKPA STPAKLAEEV PLPKPKESGG REEKQLPPLP EPKPVYAQPG QPDVDLPVSP
SDAPVPTTAH DDSILRPSMK LVKFKKGESV GLRLAGGNDV GIFVAGVLED SPAAKEGLEE
GDQILRVNNV DFANIIREEA VLFLLDLPKG EEVTILAQKK KDVYRRIVES DVGDSFYIRT
HFEYEKESPY GLSFNKGEVF RVVDTLYNGK LGSWLAIRIG KNHQEVERGI IPNKNRAEQL
SSVQYTLPKT AGGDRADFWR FRGLRSSKRN LRKSREDLSS QPVQTKFPAY ERVVLREAGF
LRPVVIFGPI ADVAREKLSR EEPDLFELAK SEPRDAGTDQ RSSGIIRLHT IKQIIDRDKH
AVLDITPNAV DRLNYAQWYP IVVFLNPDNK QGVKNMRTRL CPESRKSARK LYERAIKLRK
NNHHLFTTTI NLNNMNDGWY GALKETIQQQ QNQLVWVSEG KADGTTEDDL DIHDDRLSYL
SAPGSEYSMY STDSRHTSDY EDTDTEGGAY TDQELDETLN DEVGLPTEPA ITRSSEPVRE
DPPVIQDTPG YPGYQHPVQP DPANRIDPAG FKMAAPQQMY KKDLYNMEDP VRINHSLKQS
MSYSHQPPYQ DKQPYREYDH PPYGYDGGGY TEPKPHNTDS HLHYDNRVPH YNEQWPPYDQ
QTSSSQPAGY QPGHQQPMGY NPRSPYEDGP GRDYSPPQPR YDEAPPVGYD GRPRHSKPGP
IRYDEPPPPP LPPAGYDARS PYEAETHSFP INSPRSPEPS KQYYGDSGLR STYMPGPPNR
GFKPGMHDAM RNSEPTIPPP KPEALPSPGD PAITPGSKPP PPPPQEDLDE DPAMKPQSVL
NRVKMFENKR SVSMDRAKEG GDSSVLRPAD IPKPVMAPGP VLKANSLSNL EQEKSSYRAP
EPQKPHTKPL DDVVRSNHYD PDEDEEYYRK QLSYFDRRSF DSKAMGQPAP GINRFHDLPK
PPQLSYPYNR VESVEKVSPV EKRYDPLPQI SPSSQYGPPA SAIPPATLPK LSPGDANSVP
EPLTSPNPKP ELTTLRPTSR DEPTPGSYLP PRGLPDKSPV NGTDAAPPKT LSTPAPTSYN
RYVPKPYTSA ARPFERKFES PKFNHNLLPN DTQVKTDLLS KPSVVSNSSG KPQLSPQPLD
HDSGLDTFTR TIDNRPKYQH NNINAIPKAI PVSPSALDDD DEDEGHTVVA TARGIFNCNG
GVLSSIETGV SIIIPQGAIP ESVEQEIYFK VCRDNSILPP LDKEKGETLL SPLVMCGPHG
LKFLKPVELR LPHCASMTPD GWSFALKSSD SSSGDPKTWQ NKSLPGDPNY LVGANCVSVL
IDHF
//
