GenomeNet

Database: UniProt
Entry: A0A493TLX1_ANAPP
LinkDB: A0A493TLX1_ANAPP
Original site: A0A493TLX1_ANAPP 
ID   A0A493TLX1_ANAPP        Unreviewed;      1183 AA.
AC   A0A493TLX1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Tight junction protein 2 {ECO:0000313|Ensembl:ENSAPLP00000026788.1};
GN   Name=TJP2 {ECO:0000313|Ensembl:ENSAPLP00000026788.1};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000026788.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000026788.1, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000026788.1}
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   AlphaFoldDB; A0A493TLX1; -.
DR   Ensembl; ENSAPLT00000034655.1; ENSAPLP00000026788.1; ENSAPLG00000002087.2.
DR   GeneTree; ENSGT00940000158634; -.
DR   Proteomes; UP000016666; Chromosome Z.
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; cd12027; SH3_ZO-2; 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; IPR005419; ZO-2.
DR   InterPro; IPR035598; ZO-2_SH3.
DR   PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR   PANTHER; PTHR13865:SF26; TIGHT JUNCTION PROTEIN ZO-2; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01599; ZONOCCLUDNS2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 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.
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:UP000016666};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          34..121
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          296..374
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          500..581
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          595..660
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          681..867
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..972
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1024
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1183 AA;  132476 MW;  DE8599D01221E422 CRC64;
     MGATQGSAGR EPRGPAAGEE QAPGMEELIW EQYTVTLQKD SKRGFGIAVS GGRDNPHFEN
     GETSIVISDV LPGGPADGLL QENDRVVIVN GTPMENVPHS FAVQQLRKSG KVATIVVKRP
     RKVQAAALRR SPSLDYEDRA LDVMDDHADF DGKSARSGYS ERSWRSGNGG RSQSWGNSLD
     QSYRDDEDRG RNKSRDRSRE YSRDRSRGRS VDRSLDRDYG RDRSRGRSID RDGGYERDYR
     GDYSPPSYSH GSQPDPRYVR EVRSRSRDRL RSRSPSPEMH HQHEYLGPQD QNGPISVLLT
     KGKHNEEYGL RLGSQIFIKE MTSTGLATKD GNLHEGDIIL KINGTVTENM SLSDARKLIE
     KSRGKLQLVV LRDRKQTLLN IPSLNDSDSE MDDISEIESN RSFSPQDDRL HHSDVDSHSS
     NEKLKEKPNA KDDSSSRMSR MGAMPTPFKS TGDIASAAVT VVDTNKEPKY QDDTAVSQPK
     PVARTILKPS PEDEAIYGPN TKMVRFKKGD SVGLRLAGGN DVGIFIAGIQ EGTSADQEGL
     QEGDQILKVN TQDFRGIVRE DAVLYLLEIP KGETVTILAQ SKYEVYRDIM ACGRGDSFFI
     RSHFECDKES PQSLAFTRGE IFRVVDTLYD GKLGNWLAVR IGNELEKGLI PNKSRAEQMA
     SVQNAQKDGS SDRADFWRTR GQRSGGKKNL RKSREDLTAI VSVSTKFPAY ERVQLREAGF
     KRPVVIFGPI ADVAMEKLSN DLPHLYQTAK TEPRDAGSEK STGVVRLNTV RQIIEQDKHA
     LLDVTPKAVD LLNYTQWFPI VVFFNPDSKQ GVKIMRQRLC STSNKSSRKL YEQANKLKKN
     CSHLFTATIN LNSANDSWYG SLKDTIQQQQ GEAVWVSEGK MDGMEDDADD RMSYLTAMGA
     DYLSCDSRLI SDLEDTDGEG GAYTDNELDE TMDEPRISSV SRSSEPAHHE ENIRKLSSEP
     RAQLRKAGSR EILREPSPPP AFKPEPPKGK LQNKEDQYDI PKNSDSKTSS INASSETSTA
     SVKAAPPVSA KPAFGRPILR NTQQAVPAAE EEEEKLEEEG SEQENTPKSV QRKVKIFEEM
     NQKAKIQRMQ ELQEAQNARL EIAQKHPDIY AVPVKTQKSE QNWPQPMSCR PPEPQKPPTR
     PYLENRGSCG SDAEEEEEYR RQLSDHSKKG YYAQPSRYRD TEL
//
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