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Protein

Tight junction protein ZO-1

Gene

TJP1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  • bicellular tight junction assembly Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tight junction protein ZO-1
Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1
Gene namesi
Name:TJP1
Synonyms:ZO1
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell surface Source: MGI
  • cytoplasmic vesicle Source: UniProtKB
  • gap junction Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Gap junction, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17691769Tight junction protein ZO-1PRO_0000094539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei174 – 1741PhosphoserineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei184 – 1841PhosphothreonineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei266 – 2661PhosphothreonineBy similarity
Modified residuei274 – 2741PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineBy similarity
Modified residuei279 – 2791PhosphoserineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei289 – 2891PhosphoserineBy similarity
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei336 – 3361PhosphoserineBy similarity
Modified residuei352 – 3521PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei808 – 8081PhosphothreonineBy similarity
Modified residuei809 – 8091PhosphoserineBy similarity
Modified residuei820 – 8201PhosphoserineBy similarity
Modified residuei821 – 8211PhosphotyrosineBy similarity
Modified residuei823 – 8231PhosphoserineBy similarity
Modified residuei847 – 8471PhosphothreonineBy similarity
Modified residuei853 – 8531PhosphothreonineBy similarity
Modified residuei860 – 8601PhosphothreonineBy similarity
Modified residuei867 – 8671PhosphothreonineBy similarity
Modified residuei911 – 9111PhosphoserineBy similarity
Modified residuei967 – 9671PhosphoserineBy similarity
Modified residuei1070 – 10701PhosphoserineBy similarity
Modified residuei1138 – 11381PhosphoserineBy similarity
Modified residuei1139 – 11391PhosphotyrosineBy similarity
Modified residuei1164 – 11641PhosphotyrosineBy similarity
Modified residuei1353 – 13531PhosphotyrosineBy similarity
Modified residuei1365 – 13651PhosphoserineBy similarity
Modified residuei1546 – 15461PhosphoserineBy similarity
Modified residuei1618 – 16181PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO97758.
PRIDEiO97758.

Interactioni

Subunit structurei

Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1. Interacts (via ZU5 domain) with CDC42BPB and MYZAP. Interacts (via PDZ domain) with GJA1. Interacts (via PDZ domains) with ANKRD2 (By similarity). Interacts with BVES (via the C-terminus cytoplasmic tail) (By similarity). Interacts with HSPA4 and KIRREL1 (By similarity) (PubMed:16407410). Interacts with DLL1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA4Q2TFN93EBI-6988333,EBI-8002398

Protein-protein interaction databases

BioGridi139675. 2 interactions.
IntActiO97758. 8 interactions.
MINTiMINT-1778189.
STRINGi9615.ENSCAFP00000042731.

Structurei

3D structure databases

ProteinModelPortaliO97758.
SMRiO97758. Positions 18-110, 184-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11088PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini185 – 26379PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini420 – 50182PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini515 – 58369SH3PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 790182Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST
Domaini1633 – 1745113ZU5PROSITE-ProRule annotationAdd
BLAST

Domaini

The second PDZ domain mediates interaction with GJA12.By similarity

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 ZU5 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG3580. Eukaryota.
ENOG410XQP3. LUCA.
HOGENOMiHOG000230923.
HOVERGENiHBG007849.
InParanoidiO97758.
KOiK05701.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005418. ZO-1.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O97758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSARAAAAKN TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG
60 70 80 90 100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK
110 120 130 140 150
NAKITIRRKK KVQIPVSRPD PEPVSENEDS YDEEVHDPRS SRGGLVSRRS
160 170 180 190 200
EKSWARDRSA SRERSLSPRS DRRSVASSQP PKPTKVTLVK SRKNEEYGLR
210 220 230 240 250
LASHIFVKEI SQDSLAARDG NIQEGDVVLK INGTVTENMS LTDAKTLIER
260 270 280 290 300
SKGKLKMVVQ RDERATLLNV PDLSDSIHSA NASERDDISE IQSLASDHSG
310 320 330 340 350
RSHDRPPRHS RSRSPDQRSE PSDHSRHSPQ QPSSGSLRSR EEERISKPGA
360 370 380 390 400
VSTPVKHADD HTHKTVEEVV VERNEKQAPS LPEPKPVYAQ VGQPDVDLPV
410 420 430 440 450
SPSDGVLPNS THEDGILRPS MKLVKFRKGD SVGLRLAGGN DVGIFVAGVL
460 470 480 490 500
EDSPAAKEGL EEGDQILRVN NVDFTNIIRE EAVLFLLDLP KGEEVTILAQ
510 520 530 540 550
KKKDVYRRIV ESDVGDSFYI RTHFEYEKES PYGLSFNKGE VFRVVDTLYN
560 570 580 590 600
GKLGSWLAIR IGKNHKEVER GIIPNKNRAE QLASVQYTLP KTAGGDRADF
610 620 630 640 650
WRFRGLRSSK RNLRKSREDL SAQPVQTKFP AYERVVLREA GFLRPVTIFG
660 670 680 690 700
PIADVAREKL AREEPDIYQI AKSEPRDAGT DQRSSGIIRL HTIKQIIDQD
710 720 730 740 750
KHALLDVTPN AVDRLNYAQW YPIVVFLNPD SKQGVKTMRM RLCPESRKSA
760 770 780 790 800
RKLYERSHKL RKNNHHLFTT TINLNSMNDG WYGALKEAIQ QQQNQLVWVS
810 820 830 840 850
EGKADGATSD DLDLHDDRLS YLSAPGSEYS MYSTDSRHTS DYEDTDTEGG
860 870 880 890 900
AYTDQELDET LNDEVGTPPE SAITRSSEPV REDSSGMHHE NQTYPPYSPQ
910 920 930 940 950
AQPQPIHRID SPGFKTASQQ KAEASSPVPY LSPETNPASS TSAVNHNVTL
960 970 980 990 1000
TNVRLEGPTP APSTSYSPQA DSLRTPSTEA AHIMLRDQEP SLPSHVEPAK
1010 1020 1030 1040 1050
VYRKDPYPEE MMRQNHVLKQ PAVGHPGQRP DKEPNLSYES QPPYVEKQAN
1060 1070 1080 1090 1100
RDLEQPTYRY DSSSYTDQFS RNYDHRLRYE ERIPTYEEQW SYYDDKQPYQ
1110 1120 1130 1140 1150
PRPSLDNQHP RDLDSRQHPE ESSERGSYPR FEEPAPLSYD SRPRYDQPPR
1160 1170 1180 1190 1200
TSTLRHEEQP TPGYDMHNRY RPEAQSYSSA GPKASEPKQY FDQYPRSYEQ
1210 1220 1230 1240 1250
VPSQGFSSKA GHYEPLHGAA VVPPLIPASQ HKPEVLPSNT KPLPPPPTLT
1260 1270 1280 1290 1300
EEEEDPAMKP QSVLTRVKMF ENKRSASLEN KKDENHTAGF KPPEVASKPP
1310 1320 1330 1340 1350
GAPIIGPKPT PQNQFSEHDK TLYRIPEPQK PQMKPPEDIV RSNHYDPEED
1360 1370 1380 1390 1400
EEYYRKQLSY FDRRSFENKP STHIPAGHLS EPAKPVHSQN QTNFSSYSSK
1410 1420 1430 1440 1450
GKSPEADAPD RSFGEKRYEP VQATPPPPPL PSQYAQPSQP GTSSSLALHT
1460 1470 1480 1490 1500
HAKGAHGEGN SISLDFQNSL VSKPDPPPSQ NKPATFRPPN REDTVQSTFY
1510 1520 1530 1540 1550
PQKSFPDKAP VNGAEQTQKT VTPAYNRFTP KPYTSSARPF ERKFESPKFN
1560 1570 1580 1590 1600
HNLLPSETAH KPDLSSKAPA SPKTLAKAHS RAQPPEFDSG VETFSIHADK
1610 1620 1630 1640 1650
PKYQMNNLST VPKAIPVSPS AVEEDEDEDG HTVVATARGV FNNNGGVLSS
1660 1670 1680 1690 1700
IETGVSIIIP QGAIPEGVEQ EIYFKVCRDN SILPPLDKEK GETLLSPLVM
1710 1720 1730 1740 1750
CGPHGLKFLK PVELRLPHCA SMTPDGWSFA LKSSDSSSGD PKTWQNKCLP
1760
GDPNYLVGAN CVSVLIDHF
Length:1,769
Mass (Da):197,607
Last modified:May 1, 1999 - v1
Checksum:i181E9F36CEBC96EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55935 mRNA. Translation: AAD11529.1.
RefSeqiNP_001003140.1. NM_001003140.1.
UniGeneiCfa.3616.

Genome annotation databases

GeneIDi403752.
KEGGicfa:403752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55935 mRNA. Translation: AAD11529.1.
RefSeqiNP_001003140.1. NM_001003140.1.
UniGeneiCfa.3616.

3D structure databases

ProteinModelPortaliO97758.
SMRiO97758. Positions 18-110, 184-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi139675. 2 interactions.
IntActiO97758. 8 interactions.
MINTiMINT-1778189.
STRINGi9615.ENSCAFP00000042731.

Proteomic databases

PaxDbiO97758.
PRIDEiO97758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403752.
KEGGicfa:403752.

Organism-specific databases

CTDi7082.

Phylogenomic databases

eggNOGiKOG3580. Eukaryota.
ENOG410XQP3. LUCA.
HOGENOMiHOG000230923.
HOVERGENiHBG007849.
InParanoidiO97758.
KOiK05701.

Miscellaneous databases

NextBioi20817254.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZO.
IPR005418. ZO-1.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Cocker spaniel.
    Tissue: Kidney.
  2. "The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB."
    Tsapara A., Matter K., Balda M.S.
    Mol. Biol. Cell 17:1322-1330(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPA4.

Entry informationi

Entry nameiZO1_CANLF
AccessioniPrimary (citable) accession number: O97758
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.