ID F1M4A0_RAT Unreviewed; 1725 AA.
AC F1M4A0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Tight junction protein 1 {ECO:0000313|Ensembl:ENSRNOP00000014988.7};
GN Name=Tjp1 {ECO:0000313|Ensembl:ENSRNOP00000014988.7,
GN ECO:0000313|RGD:1306305};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000014988.7, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000014988.7, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014988.7,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4] {ECO:0000313|Ensembl:ENSRNOP00000014988.7}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014988.7};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- INTERACTION:
CC F1M4A0; Q6P6T5: Ocln; NbExp=2; IntAct=EBI-15783773, EBI-15348891;
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 IntAct; F1M4A0; 2.
DR Ensembl; ENSRNOT00000014988.8; ENSRNOP00000014988.7; ENSRNOG00000011077.8.
DR RGD; 1306305; Tjp1.
DR VEuPathDB; HostDB:ENSRNOG00000011077; -.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000155164; -.
DR OrthoDB; 2904077at2759; -.
DR TreeFam; TF315957; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000011077; Expressed in lung and 19 other cell types or tissues.
DR ExpressionAtlas; F1M4A0; baseline and differential.
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 1: Evidence at protein level;
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:UP000002494};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 2..90
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 166..244
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 401..482
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 496..564
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 670..771
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1611..1725
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 82..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..844
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1415
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1725 AA; 193023 MW; 7651C54E49426B3E CRC64;
MIVTCNHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG
VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD PDPVSDNEDD SYDEDVHDPR
SGRGALANRR GEKSWARDRS ASRDRSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE RSKGKLKMVV
QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS VRSHDRPPRR SQSRSPDQRS
EPSDHSTQSP QQPSNGSLRS REEERMSKPG AVSTPVKHVD DHTPKAVEEV TVEKHEKQTP
TLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG
NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY NGKLGSWLAI
RIGKNHKEVE RGIVPNKNRA EQLASVQYTL PKTAGGDRAD FWRFRGLRSS KRNLRKSRED
LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK LAREEPDIYQ IAKSEPRDAG
TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR
MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG GAYTDQELDE
TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP QAQPQAIHRI DSPGLKTASQ
QKAEASSPVP YLSPETNPAS SASAVKHNVN LTNVNLEEPT PAPPTSHVSQ ADCLGAPSPE
APHTMLRDEG VSLPSHVDPA KVYRKEPYPE EMMRQNHILK QPALGHPGQR LDKEPNPAYD
PQLPYVEKQA SRDLEQPPYR YESSSYTDQF SRNYDHRLRF EDRVPTYEDQ WSYYDDKQPY
PTRPFDTQHP RDLDSRQHPE EASERGYFQR FEEPAPLPYD SRPRYEQLPR TSTLRHEEQP
TSGYEVHNRY RPEAQPYAPA GPKSSEPKQY FDQYPRSYEQ VPPPGFTSKT GHYEPLHGAA
VVPPLIPSSQ HKPEVLPSAT KPQPPPPALT EEEEDPAMKP QSVLTRVKMF ENKRSASLEN
KKDVNDTASF KPPEVASKPP SASLVGPKPV SQTQFSEHDK TLYRLPEPQK PQAKPPEDIV
RSNHYDPEED EEYYRKQLSY FDRRSFESKP PAHIPAGHHS EPAKPVHSQS QPNFSSYSSK
GKPETDAMDR SFSEKRYDPT QAMPPPPPLP SQYSQPVPPL SNSSLHIHSK AAQSEGNSVS
LDFQNSYISK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS FPDKASVNGA EQTQKTITPA
YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL SSKPPPSPKT LMKAHSSTQP
PEFDSGVETF SVHTDKPKYQ INNISTMPKA VPVSPSAVEE DEDEDGHTVV ATARGIFNSN
GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH
GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV LIDHF
//
