TJAP1_MOUSE
ID TJAP1_MOUSE Reviewed; 549 AA.
AC Q9DCD5; I7H459; Q8CFL7; Q8R5I2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tight junction-associated protein 1;
DE AltName: Full=Protein incorporated later into tight junctions;
DE AltName: Full=Tight junction protein 4;
GN Name=Tjap1 {ECO:0000312|MGI:MGI:1921344};
GN Synonyms=Pilt {ECO:0000303|PubMed:22841714}, Tjp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAM29296.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ARF6,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAM29296.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAM29296.1};
RX PubMed=22841714; DOI=10.1016/j.febslet.2012.07.051;
RA Tamaki H., Sanda M., Katsumata O., Hara Y., Fukaya M., Sakagami H.;
RT "Pilt is a coiled-coil domain-containing protein that localizes at the
RT trans-Golgi complex and regulates its structure.";
RL FEBS Lett. 586:3064-3070(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 355-549, AND SUBCELLULAR LOCATION.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11602598; DOI=10.1074/jbc.m107335200;
RA Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K., Takeuchi M.,
RA Takai Y.;
RT "Pilt, a novel peripheral membrane protein at tight junctions in epithelial
RT cells.";
RL J. Biol. Chem. 276:48350-48355(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in regulating the structure of the Golgi
CC apparatus. {ECO:0000269|PubMed:22841714}.
CC -!- SUBUNIT: Interacts with DLG1 (By similarity). Interacts with ARF6 (GTP-
CC bound form) (PubMed:22841714). {ECO:0000250|UniProtKB:Q5JTD0,
CC ECO:0000269|PubMed:22841714}.
CC -!- INTERACTION:
CC Q9DCD5; P62331: Arf6; NbExp=2; IntAct=EBI-775733, EBI-988682;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:11602598, ECO:0000269|PubMed:22841714}. Cell
CC junction, tight junction {ECO:0000269|PubMed:11602598}. Cell membrane
CC {ECO:0000269|PubMed:22841714}; Peripheral membrane protein
CC {ECO:0000305}. Note=Recruited to tight junctions (TJ) during late
CC stages of maturation of the TJ complexes. Excluded from adherens
CC junctions and desmosomes. {ECO:0000269|PubMed:11602598}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DCD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DCD5-2; Sequence=VSP_060915;
CC -!- TISSUE SPECIFICITY: Widely expressed including in adult thymus, heart,
CC lung, liver, small intestine, kidney, spleen, testis and skeletal
CC muscle and in embryonic brain but not detected in adult brain (at
CC protein level). {ECO:0000269|PubMed:22841714}.
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DR EMBL; AB712252; BAM29296.1; -; mRNA.
DR EMBL; AK002882; BAB22429.1; -; mRNA.
DR EMBL; AK169889; BAE41438.1; -; mRNA.
DR EMBL; AC116739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023316; AAH23316.1; -; mRNA.
DR EMBL; AF465982; AAL76253.1; -; mRNA.
DR CCDS; CCDS28824.1; -. [Q9DCD5-2]
DR RefSeq; NP_001239402.1; NM_001252473.1. [Q9DCD5-2]
DR RefSeq; NP_001239403.1; NM_001252474.1. [Q9DCD5-2]
DR RefSeq; NP_001239404.1; NM_001252475.1. [Q9DCD5-2]
DR RefSeq; NP_083027.1; NM_028751.3. [Q9DCD5-2]
DR RefSeq; XP_011244964.1; XM_011246662.2. [Q9DCD5-1]
DR RefSeq; XP_011244965.1; XM_011246663.2. [Q9DCD5-1]
DR RefSeq; XP_011244966.1; XM_011246664.2. [Q9DCD5-1]
DR RefSeq; XP_011244967.1; XM_011246665.2. [Q9DCD5-1]
DR RefSeq; XP_011244968.1; XM_011246666.2. [Q9DCD5-1]
DR RefSeq; XP_011244969.1; XM_011246667.2. [Q9DCD5-1]
DR RefSeq; XP_011244970.1; XM_011246668.2. [Q9DCD5-1]
DR RefSeq; XP_011244971.1; XM_011246669.2. [Q9DCD5-1]
DR RefSeq; XP_011244972.1; XM_011246670.2. [Q9DCD5-1]
DR RefSeq; XP_011244973.1; XM_011246671.2. [Q9DCD5-1]
DR RefSeq; XP_011244974.1; XM_011246672.2. [Q9DCD5-1]
DR RefSeq; XP_011244975.1; XM_011246673.2. [Q9DCD5-1]
DR RefSeq; XP_011244976.1; XM_011246674.2. [Q9DCD5-1]
DR RefSeq; XP_011244977.1; XM_011246675.2. [Q9DCD5-1]
DR RefSeq; XP_011244978.1; XM_011246676.1. [Q9DCD5-1]
DR RefSeq; XP_011244979.1; XM_011246677.2. [Q9DCD5-2]
DR AlphaFoldDB; Q9DCD5; -.
DR SMR; Q9DCD5; -.
DR BioGRID; 216487; 4.
DR IntAct; Q9DCD5; 3.
DR MINT; Q9DCD5; -.
DR STRING; 10090.ENSMUSP00000130710; -.
DR iPTMnet; Q9DCD5; -.
DR PhosphoSitePlus; Q9DCD5; -.
DR EPD; Q9DCD5; -.
DR jPOST; Q9DCD5; -.
DR MaxQB; Q9DCD5; -.
DR PaxDb; Q9DCD5; -.
DR PRIDE; Q9DCD5; -.
DR ProteomicsDB; 259511; -.
DR ProteomicsDB; 332631; -.
DR Antibodypedia; 16501; 141 antibodies from 24 providers.
DR DNASU; 74094; -.
DR Ensembl; ENSMUST00000012440; ENSMUSP00000012440; ENSMUSG00000012296. [Q9DCD5-2]
DR Ensembl; ENSMUST00000164342; ENSMUSP00000130710; ENSMUSG00000012296. [Q9DCD5-2]
DR Ensembl; ENSMUST00000180283; ENSMUSP00000137220; ENSMUSG00000012296. [Q9DCD5-2]
DR Ensembl; ENSMUST00000225080; ENSMUSP00000153327; ENSMUSG00000012296. [Q9DCD5-2]
DR Ensembl; ENSMUST00000225413; ENSMUSP00000153632; ENSMUSG00000012296. [Q9DCD5-1]
DR GeneID; 74094; -.
DR KEGG; mmu:74094; -.
DR UCSC; uc008csf.2; mouse. [Q9DCD5-1]
DR UCSC; uc033hee.1; mouse.
DR CTD; 93643; -.
DR MGI; MGI:1921344; Tjap1.
DR VEuPathDB; HostDB:ENSMUSG00000012296; -.
DR eggNOG; ENOG502QRZ1; Eukaryota.
DR GeneTree; ENSGT00940000161543; -.
DR HOGENOM; CLU_032139_0_0_1; -.
DR InParanoid; Q9DCD5; -.
DR OMA; SQSWIFA; -.
DR OrthoDB; 443898at2759; -.
DR PhylomeDB; Q9DCD5; -.
DR TreeFam; TF331612; -.
DR BioGRID-ORCS; 74094; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tjap1; mouse.
DR PRO; PR:Q9DCD5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DCD5; protein.
DR Bgee; ENSMUSG00000012296; Expressed in hindlimb stylopod muscle and 237 other tissues.
DR ExpressionAtlas; Q9DCD5; baseline and differential.
DR Genevisible; Q9DCD5; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR InterPro; IPR028179; Tjap1.
DR InterPro; IPR043441; Tjap1/BEGAIN.
DR InterPro; IPR043470; Tjap1_dom.
DR PANTHER; PTHR28664; PTHR28664; 1.
DR PANTHER; PTHR28664:SF3; PTHR28664:SF3; 1.
DR Pfam; PF15453; Pilt; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..549
FT /note="Tight junction-associated protein 1"
FT /id="PRO_0000072551"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..171
FT /evidence="ECO:0000255"
FT COMPBIAS 11..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTD0"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTD0"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTD0"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTD0"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTD0"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 120..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060915"
FT CONFLICT 365
FT /note="A -> S (in Ref. 2; BAE41438 and 4; AAH23316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 60520 MW; 267C34C0BC7EB85A CRC64;
MSSAAPAKKP YRKAPPEHRE LRLEIPVSRL EQEESLTDAE RMKLLQQENE ELRKRLASAT
RRTEALEREL EIGQDCLELE LGQSREELDK FKDKFRRLQN SYTASQRTNQ ELEDKLHALA
SLSHSWIFAI KKAEMDRKTL DWEIVELTNK LLDARNTINK LEELNERYRL DCNLAVQLLK
CNKSHFRNHK LADLPCELQD MVRKHLRSGQ EVASPSPSPS SSLSPGAVVP TSVIARVLEK
PESLLLNSAQ SGSAGRPLAE DVFVHVDMSG GDPASPPAPG SPNGECCSVS TAGGSPEEEL
PLPAFDKLSP YPTPSPPHPL YPGRKVIEFS EDKIRIPRNS PLPNCTYATR QAISLSLVED
GSERAHRSSV PSSPASAQGS PHHQPSPAPS ALSAPASSAS SEEDLLASWQ RAFVDRTPPP
AAVVQRTAFG RDSLPELQLH FSPGHSTAPP PSPHRERGLV LPAEPDSGFP QDEEEEMLNL
PVSPEEERQS LLPDKEGTEE ASGPSHVDGR AWPLPSPSRP QRSPKRMGVH HLHRKDSLTQ
AQEQGTVLS
