ID A0A1U8CV79_MESAU Unreviewed; 1832 AA.
AC A0A1U8CV79;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tight junction protein ZO-1 isoform X3 {ECO:0000313|RefSeq:XP_012979349.2};
GN Name=Tjp1 {ECO:0000313|RefSeq:XP_012979349.2};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012979349.2};
RN [1] {ECO:0000313|RefSeq:XP_012979349.2}
RP IDENTIFICATION.
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_012979349.2; XM_013123895.2.
DR Proteomes; UP000189706; Unplaced.
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: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:UP000189706};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 90..177
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 253..331
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 488..569
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 583..651
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 757..858
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1698..1832
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 169..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..931
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1832 AA; 204460 MW; 1F71B38FA34C6078 CRC64;
MKYQKYLTVL QMAIGVTPSN RGSLLPLKRK LWVTPSSENP NGATSGVSQG KPSLRRIKGR
LHRSKSLDSI DFCELTSTAM EETAIWEQHT VTLHRAPGFG FGIAISGGRD NPHFQSGETS
IVISDVLKGG PAEGQLQEND RVAMVNGVSM DNVEHAFAVQ QLRKSGKNAK ITIRRKKKVQ
IPVSRPDPEP VSDNEDDSYD EEVHDPRSGR GASVNRRSEK SWARDRSASR ERSLSPRSDR
RSVASSQPAK PTKVTLVKSR KNEEYGLRLA SHIFVKEISQ DSLAARDGNI QEGDVVLKIN
GTVTENMSLT DAKTLIERSK GKLKMVVQRD ERATLLNVPD LSDSIHSANA SERDDISEIQ
SLASDHSVRS HDRPPRRSQS RSPDQRSEPS DHSRQSPQQP SNGSLRSREE ERISKPGAVS
TPVKHVDDHA TKAVEEVTVE KNEKQAPTLP EPKPVYAQVG QPDVDLPVSP SDGVLPNSTH
EDGILRPSMK LVKFRKGDSV GLRLAGGNDV GIFVAGVLED SPAAKEGLEE GDQILRVNNV
DFTNIIREEA VLFLLDLPKG EEVTILAQKK KDVYRRIVES DVGDSFYIRT HFEYEKESPY
GLSFNKGEVF RVVDTLYNGK LGSWLAIRIG KNHKEVERGI IPNKNRAEQL ASVQYTLPKT
AGGDRADFWR FRGLRSSKRN LRKSREDLSA QPVQTKFPAY ERVVLREAGF LRPVTIFGPI
ADVAREKLAR EEPDIYQIAK SEPRDAGTDH RSSGIIRLHT IKQIIDQDKH ALLDVTPNAV
DRLNYAQWYP IVVFLNPDSK QGVKTMRMRL CPESRKSARK LYERSHKLRK NNHHLFTTTI
NLNSMNDGWY GALKEAIQQQ QNQLVWVSEG KADGATSDDL DLHDDRLSYL SAPGSEYSMY
STDSRHTSDY EDTDTEGGAY TDQELDETLN DEVGTPPESA ITRSSEPVRE DSSGMHHENQ
TYPPYSPQAQ PQPIHRIESP GLKTASQQKA EASSPVPYLS PATNAASPAS AAGPNVKLTN
VRLEESTPAP PTSHAPQADS LRAPSTEAAH TMLRDEGPSL SPHVDPTKVY RKEPYPEEMM
RQNHILKQHA LGHPGQRLDK EPNVAYEPQL PYIEKQASRD LEQPAYRYDS SGYTDQFSRN
YDHRLRYEDR IPTYEDQWSY YDDKQPYQPR PFDNQHPRDL DSRQHPDEPS ERGYFPRFEE
PASLSYDNRP RYEQLPRTST LRHEEPPSSG YEVHNRYRPE AQPYSSSGPK SSEPKQNFDQ
YPRSYEQVPS QGFTSKTGHY EPLHGAAVAP PLLPSSQHKP EALPPATKPQ PPHPTLVEEE
EDPAMKPQSV LTRVKMFENK RSASLENKKD VNDTASFKLP EVASKPPSAS LAGPKPAPQS
QFSEHDKTLY RLPEPQKPQV KPPEDIVRSN HYDPEEDEEY YRKQLSYFDR RSFETKPPAH
IPASHHPEPA KPVHSQSQPN FSSYSSKGKP DTDTVDRSFS EKRYDPTQAT PPPPPLPSQY
SQPAPPVCGS SLHVHSKGAQ GEGNSVSLDF QNSYMSKPDP PPAQSKPAVF RPPAREDTAQ
TFYPQKGFPE KAPVNGTEQP PKTVTPAYNR FTPKPYTSAA RPFERKFDSP KFNHNLLPSE
TVHKPELSSK TPTSPKTLMK AHSSAQPPEF DSGVETFSIH ADKPKYQINN ISTMPKAVPV
SPSAVEEDED EDGHTVVATA RGIFNSNGGV LSSIETGVSI IIPQGAIPEG IEQEIYFKVC
RDNSILPPLD KEKGETLLSP LVMCGPHGLK FLKPVELRLP HCASMTPDGW SFALKSSDSS
SGDPKTWQNK CLPGDPNYLV GANCVSVLID HF
//
