Tight junction protein ZO-1 - Mus musculus (Mouse)

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P39447 (ZO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tight junction protein ZO-1

Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1

Gene names

Name:	Tjp1
Synonyms:	Zo1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells By similarity.
Subunit structure	Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with CGN/cingulin, CALM, CXADR, GJD3, HSPA4 and UBN1. Interacts (via ZU5 domain) with CDC42BPB. Interacts (via PDZ domain) with GJA1 By similarity. Interacts with OCLN, claudins, GJA12 and KIRREL1. Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts (via ZU5 domain) with GCOM1. Ref.3 Ref.4 Ref.5 Ref.11
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction › tight junction By similarity. Cell junction › gap junction. Cytoplasm › myofibril › sarcomere › I band. Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells By similarity. Ref.11
Domain	The second PDZ domain mediates interaction with GJA12. Ref.4
Post-translational modification	Phosphorylated. Dephosphorylated by PTPRJ By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain. Contains 1 ZU5 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Gap junction Membrane Tight junction
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blastocyst formation Inferred from mutant phenotype. Source: MGI
Cellular component	I band Inferred from electronic annotation. Source: UniProtKB-SubCell cell-cell adherens junction Inferred from direct assay. Source: MGI gap junction Inferred from electronic annotation. Source: UniProtKB-SubCell intercellular canaliculus Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI tight junction Inferred from direct assay. Source: UniProtKB
Molecular function	protein domain specific binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Actn4	P57780	6	EBI-79508,EBI-445071

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1745

1745

Tight junction protein ZO-1

PRO_0000094541

Regions

Domain

23 – 110

PDZ 1

Domain

186 – 264

PDZ 2

Domain

421 – 502

PDZ 3

Domain

516 – 584

SH3

Domain

610 – 791

182

Guanylate kinase-like

Domain

1629 – 1721

ZU5

Compositional bias

1242 – 1247

Poly-Pro

Compositional bias

1424 – 1430

Poly-Pro

Amino acid modifications

Modified residue

125

Phosphoserine Ref.9

Modified residue

131

Phosphoserine By similarity

Modified residue

132

Phosphotyrosine By similarity

Modified residue

166

Phosphoserine By similarity

Modified residue

168

Phosphoserine By similarity

Modified residue

175

Phosphoserine Ref.7 Ref.9

Modified residue

178

Phosphoserine Ref.9

Modified residue

179

Phosphoserine Ref.9

Modified residue

275

Phosphoserine By similarity

Modified residue

277

Phosphoserine By similarity

Modified residue

280

Phosphoserine By similarity

Modified residue

284

Phosphoserine Ref.7

Modified residue

297

Phosphoserine Ref.7

Modified residue

300

Phosphoserine Ref.7 Ref.9

Modified residue

329

Phosphoserine By similarity

Modified residue

337

Phosphoserine By similarity

Modified residue

353

Phosphoserine By similarity

Modified residue

354

Phosphothreonine By similarity

Modified residue

402

Phosphoserine By similarity

Modified residue

617

Phosphoserine Ref.7 Ref.9

Modified residue

868

Phosphothreonine By similarity

Modified residue

912

Phosphoserine Ref.8 Ref.9

Modified residue

927

Phosphoserine By similarity

Modified residue

1139

Phosphotyrosine Ref.6

Modified residue

1164

Phosphotyrosine Ref.10

Modified residue

1353

Phosphotyrosine Ref.6

Modified residue

1365

Phosphoserine By similarity

Modified residue

1542

Phosphoserine By similarity

Modified residue

1614

Phosphoserine By similarity

Modified residue

1616

Phosphoserine By similarity

Experimental info

Sequence conflict

202

L → P in BAA03274. Ref.1

Sequence conflict

222

N → D in BAA03274. Ref.1

Sequence conflict

676

P → L in BAA03274. Ref.1

Sequence conflict

985

V → G in BAA03274. Ref.1

Sequence conflict

1237

P → R in BAA03274. Ref.1

Sequence conflict

1395

S → P in BAA03274. Ref.1

Sequence conflict

1584

D → G in BAA03274. Ref.1

Secondary structure

1745

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P39447 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 002B96F5A998B5CD
Show »

FASTA

1,745

194,742

        10         20         30         40         50         60 
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 

        70         80         90        100        110        120 
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD 

       130        140        150        160        170        180 
PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ 

       190        200        210        220        230        240 
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 

       250        260        270        280        290        300 
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 

       310        320        330        340        350        360 
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD 

       370        380        390        400        410        420 
DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP 

       430        440        450        460        470        480 
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 

       490        500        510        520        530        540 
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 

       550        560        570        580        590        600 
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 

       610        620        630        640        650        660 
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 

       670        680        690        700        710        720 
LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 

       730        740        750        760        770        780 
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 

       790        800        810        820        830        840 
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 

       850        860        870        880        890        900 
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 

       910        920        930        940        950        960 
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS VTNVSLEEPA 

       970        980        990       1000       1010       1020 
PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA KVYRKEPYSE EMMRQNHILK 

      1030       1040       1050       1060       1070       1080 
QPALGHPGQR PDKEPNLAYE PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF 

      1090       1100       1110       1120       1130       1140 
EDRIPTYEDQ WSYYDDKQPY QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD 

      1150       1160       1170       1180       1190       1200 
SRTRYEQLPR TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ 

      1210       1220       1230       1240       1250       1260 
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT EEEEDPAMKP 

      1270       1280       1290       1300       1310       1320 
QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK 

      1330       1340       1350       1360       1370       1380 
TLYRLPEPQK PQVKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS 

      1390       1400       1410       1420       1430       1440 
EPAKPVHSQS QPNFSSYSSK GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL 

      1450       1460       1470       1480       1490       1500 
SSSSLHIHSK GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS 

      1510       1520       1530       1540       1550       1560 
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL 

      1570       1580       1590       1600       1610       1620 
SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE 

      1630       1640       1650       1660       1670       1680 
DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP 

      1690       1700       1710       1720       1730       1740 
PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV 


LIDHF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy." Itoh M., Nagafuchi A., Yonemura S., Yasuda-Kitani T., Tsukita S., Tsukita S. J. Cell Biol. 121:491-502(1993) [PubMed: 8486731] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[3]	"NEPH1 defines a novel family of podocin interacting proteins." Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G. FASEB J. 17:115-117(2003) [PubMed: 12424224] [Abstract] Cited for: INTERACTION WITH KIRREL1. Strain: Swiss Webster. Tissue: Brain.
[4]	"Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain." Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M., Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I. Neuroscience 126:611-630(2004) [PubMed: 15183511] [Abstract] Cited for: INTERACTION WITH GJA12, DOMAIN.
[5]	"Bves modulates epithelial integrity through an interaction at the tight junction." Osler M.E., Chang M.S., Bader D.M. J. Cell Sci. 118:4667-4678(2005) [PubMed: 16188940] [Abstract] Cited for: INTERACTION WITH BVES.
[6]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-284; SER-297; SER-300 AND SER-617, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178; SER-179; SER-300; SER-617 AND SER-912, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1164, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[11]	"Myozap, a novel intercalated disc protein, activates serum response factor-dependent signaling and is required to maintain cardiac function in vivo." Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R., Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A., Olson E.N., Frey N. Circ. Res. 106:880-890(2010) [PubMed: 20093627] [Abstract] Cited for: INTERACTION WITH GCOM1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1." Umetsu Y., Goda N., Taniguchi R., Satomura K., Ikegami T., Furuse M., Hiroaki H. Biomol. NMR. Assign. 5:207-210(2011) [PubMed: 21431884] [Abstract] Cited for: STRUCTURE BY NMR OF 18-110.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D14340 mRNA. Translation: BAA03274.1.
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.

IPI

IPI00135971.

PIR

A46431.

RefSeq

NP_033412.2. NM_009386.2.

UniGene

Mm.4342.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RRM	NMR	-	A	18-110	[»]

ProteinModelPortal

P39447.

SMR

P39447. Positions 18-110, 185-264, 421-802, 1626-1745.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30946N.

IntAct

P39447. 6 interactions.

MINT

MINT-113090.

STRING

P39447.

PTM databases

PhosphoSite

P39447.

Proteomic databases

PRIDE

P39447.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.

GeneID

21872.

KEGG

mmu:21872.

UCSC

uc009hgp.2. mouse.

Organism-specific databases

CTD

7082.

MGI

MGI:98759. Tjp1.

Phylogenomic databases

eggNOG

roNOG11407.

HOVERGEN

HBG007849.

OrthoDB

EOG4WSW8R.

Gene expression databases

ArrayExpress

P39447.

Bgee

P39447.

CleanEx

MM_TJP1.

Genevestigator

P39447.

GermOnline

ENSMUSG00000030516. Mus musculus.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR001478. PDZ/DHR/GLGF.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view]

K05701.

PANTHER

PTHR13865:SF9. ZonOcculS1. 1 hit.

Pfam

PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]

PRINTS

PR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.

SMART

SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 3 hits.
SSF50044. SH3. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. False negative.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

301376.

SOURCE

Search...

Entry information

Entry name

ZO1_MOUSE

Accession

Primary (citable) accession number: P39447
Secondary accession number(s): E9QK00

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents