ID A0A2K5CG14_AOTNA Unreviewed; 1756 AA.
AC A0A2K5CG14;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Tight junction protein 1 {ECO:0000313|Ensembl:ENSANAP00000007653.1};
GN Name=TJP1 {ECO:0000313|Ensembl:ENSANAP00000007653.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000007653.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000007653.1}
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 STRING; 37293.ENSANAP00000007653; -.
DR Ensembl; ENSANAT00000025431.1; ENSANAP00000007653.1; ENSANAG00000021487.1.
DR GeneTree; ENSGT00940000155164; -.
DR OMA; QPVHRID; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:UP000233020};
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 1622..1756
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 90..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..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..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
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 907..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 196552 MW; C5B70D77C59A6483 CRC64;
MGETAIWEQH TVTLHRAPGF GFGIAISGGR DNPHFQSGET SIVISDVLKG GPAEGQLQEN
DRVAMVNGVS MDNVEHAFAV QQLRKSGKNA KITIRRKKKV QIPVSRPDPE PVSDNEEDSY
DDEIHDPRSS RSGVVNRRSE KMWPRERSAS RERSLSPRSD RRSVASSQPA KPTKVTLVKS
RKNEEYGLRL ASHIFVKEIS QDSLAARDGN IQEGDVVLKI NGTVTENMSL TDAKTLIERS
KGKLKMVVQR DERATLLNVP DLSDSIHSAN ASERDDISEI QSLASDHSGR SHDRPPRCSR
SRSPDQRSEP SDHSRYSPQQ ASNGSHRSRD EERISKPGAV STPVKHADDH TPKIVEEVTV
ERNEKQTPSL PEPKPVYAQV GQPDVDLPVS PSDGVLPNST HEDGILRPSM KLVKFRKGDS
VGLRLAGGND VGIFVAGVLE 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
PGFKPASQQK AEASSPVPYL SPETNPASST SAVNHNVNLT NVRLEEPTPA PSTSYSPQAD
SLRTPSTEAA HIMLRDQEPS LSSHVDPTKA YRKDPYPEEM MRQNHVFKQP AIGHPGHRPD
KEPNVTYEPQ FPYVEKQASR DLEQPTYRYE SSSYTDQFSR NYDHHLRYED RVPMYEEQWS
YYDDKQPYPS RPPFDNQHSR DLDSRQHPEE SSERGYFPRF EEPAPLSYDR RPRYEQAPRA
SALRHEEQPA AGYDTHSRHR PEAQPYPLAG PKTTEPKQYF EQYSRSYDQV PPQGFASRAG
HFEPLHGAAA IPPLIPSSQH KPEALPSNTK PLPPPPTLTE EEEDPAMKPQ SVLTRVKMFE
NKRSASLETK KDVNDTVGFK PPEVASKPQG APIIGPKPTS QNQFSEHDKT LYRIPEPQKP
QVKPPEDIIR SNHYDPEEDE EYYRKQLSYF DRRSFENKPP AHIPASHLSE PTKPAHSQNQ
SNFSSYSSKG KPTEADVVDR SFGEKRYEPI QATPPPPPLP SQYTQPPQPV TSTSLHIHSK
GAHGEGNPVS LDFQNSLVSK PDPPPSQNKP ATFGPPNRED TAQPAFYPQK SFTDKAPVNG
AEQTQKTVTP AYNRFTPKPY TSSARPFERK FESPKFNHNL LPSETAHKSD LSSKSPTSPK
TLVKSHSLAQ PPEFDSGVET FSIHAEKPKY QINNISTVPK AIPVSPSAVE DDEDEDGHTV
VATARGIFNS NGGVLSSIET GVSIIIPQGA IPEGVEQEIY FKVCRDNSIL PPLDKEKGET
LLSPLVMCGP HGLKFLKPVE LRLPHCASMT PDGWSFALKS SDSSSGDPKT WQNKCLPGDP
NYLVGANCVS VLIDHF
//
