ID M3WG89_FELCA Unreviewed; 1928 AA.
AC M3WG89;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Tight junction protein 1 {ECO:0000313|Ensembl:ENSFCAP00000011174.5};
GN Name=TJP1 {ECO:0000313|Ensembl:ENSFCAP00000011174.5,
GN ECO:0000313|VGNC:VGNC:66199};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000011174.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000011174.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011174.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000011174.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011174.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000011174.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011174.5};
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 EMBL; AANG04000441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; 9685-ENSFCAP00000011174; -.
DR Ensembl; ENSFCAT00000012047.6; ENSFCAP00000011174.5; ENSFCAG00000012043.6.
DR VGNC; VGNC:66199; TJP1.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000155164; -.
DR HOGENOM; CLU_001538_1_0_1; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000012043; Expressed in embryonic head and 10 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 GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd01671; CARD; 1.
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; 1.10.533.10; Death Domain, Fas; 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; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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; PF00619; CARD; 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; SSF47986; DEATH domain; 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:UP000011712};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 250..337
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 413..491
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 647..728
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 742..810
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 916..1017
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1794..1928
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1090
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1928 AA; 216874 MW; 01290509348479CC CRC64;
MSLPADVRVV QSLPSEATEQ RGPGGRSFSS SAGVEMGEAG ARPWFYCCES TTQAEREQRT
KQLLEMPLSY KERILKEFNI SQVLPRLVYD GVFSLKEYRE ILSWHCHPRR VESFFLKLCS
KGPKAFCAFC SHLEEFCPYL LTCFFLYYQE QTYRILQEAS TAEEKARVGT QPEPSDVLET
EDQEQSLQLF NKVTPSSENP NGATSSVSQG KPSLRRIKGR LHRSKSLDSI DFCELTNTAM
EETAIWEQHT VTLHRAPGFG FGIAISGGRD NPHFQSGETS IVISDVLKGG PAEGQLQEND
RVAMVNGVSM DNVEHAFAVQ QLRKSGKNAK ITIRRKKKVQ IPVSRPDPEP VSEKEDDSYD
EEVHDPRSSR GGLVSRRSEK SWARDRSASR ERSLSPRSDR RSVASSQPAK PTKVTLVKSR
KNEEYGLRLA SHIFVKEISQ DSLAARDGNI QEGDVVLKIN GTVTENMSLT DAKTLIERSK
GKLKMVVQRD ERATLLNVPD LSDSIHSANA SERDDISEIQ SLASDHSGRS HDRPPRHSRS
RSPDQRSEPS DHSRHSPQQP SSGSLRSREE ERISKPGAVS TPVKHADDHT PKTEEVVVER
NEKQAPTLPE PKPVYAQVGQ PDVDLPVSPS DGVLPNSTHE DGILRPSMKL VKFRKGDSVG
LRLAGGNDVG IFVAGVLEDS PAAKEGLEEG DQILRVNNVD FTNIIREEAV LFLLDLPKGE
EVTILAQKKK DVYRRIVESD VGDSFYIRTH FEYEKESPYG LSFNKGEVFR VVDTLYNGKL
GSWLAIRIGK NHKEVERGII PNKNRAEQLA SVQYTLPKTA GGDRADFWRF RGLRSSKRNL
RKSREDLSAQ PVQTKFPAYE RVVLREAGFL RPVTIFGPIA DVAREKLARE EPDIYQIAKS
EPRDAGTDQR SSGIIRLHTI KQIIDQDKHA LLDVTPNAVD RLNYAQWYPI VVFLNPDSKQ
GVKTMRMRLC PESRKSARKL YERSHKLRKN NHHLFTTTIN LNSMNDGWYG ALKEAIQQQQ
NQLVWVSEGK ADGATSDDLD LHDDRLSYLS APGSEYSMYS TDSRHTSDYE DTDTEGGAYT
DQELDETLND EVGTPPESAI TRSSEPVRED SSGMHHENQT YPPYSPQAQP QPIHRIDSPG
FKTASQQVYR KDPYPEEMMR QNHVLKQPPV GHPGQRPDKE PNLSYESQPP YVEKQASRDL
EQPVYRYDSS GYPDQFSRNY DHRLRYEERI PTYEEQWSYY DDKQPYQPRP SFDNQHPRDL
DSRQHPEESS ERGYYPRFEE PAPLPYDSRP RYDQPPRTST LRHEEQPTPG YDMHNRYRPE
AQSYSSAGPK ASEPKQYFDQ YPRSYEQVPS QGFTSKAGHY EPLHGAAVIP PLVPTSQHKP
EVLPSNTKPL PPPPSLTEEE EDPAMKPQSV LTRVKMFENK RSASMENKKD ENHTAGFKPP
EVASKPPGAA IVGPKATPQN QFSEHDKTLY RIPEPQKPQM KPPEDIVRSN HYDPEEDEEY
YRKQLSYFDR RSFENKPSTH IPTGHLSEPA KPVHSQNQPN FSSYSSKFLG SYPSYDYLKR
TVKWGKSPEA DTADRSFGEK RYEPIQATPP PPPLPSQYAQ TSSSLALHTH AKGAHGEGNS
VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTVQSTFYP QKSFPDKAPV NGGEQTQKTV
TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK PDLSSKAPTS PKTLVKAHSV
AQPPEFDSGV ETFSIHADKP KYQMNNVSTV PKAVPVSPSA VEEDEDEDGH TVVATARGVF
NSNGGVLSSI ETGVSIIIPQ GAIPEGIEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC
GPHGLKFLKP VELRLPHCAS MTPDGWSFAL KSSDSSSGDP KTWQNKCLPG DPNYLVGANC
VSVLIDHF
//
