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Q9JK71 (MAGI3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
Alternative name(s):
Membrane-associated guanylate kinase inverted 3
Short name=MAGI-3
Scaffolding-like protein
Gene names
Name:Magi3
Synonyms:Slipr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2. Ref.1

Subunit structure

Interacts with ADRB1, BAI1, LPAR2/EDG4, FZD4, FZD7, GRIN2B, TGFA and VANGL2 By similarity. Interacts with PTEN. Interacts with ADRB1, PTPRB and unidentified tyrosine phosphorylated proteins. Ref.1 Ref.2 Ref.3

Subcellular location

Cell membrane; Peripheral membrane protein. Cell junctiontight junction. Nucleus. Note: Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions. Ref.1 Ref.3

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 6 PDZ (DHR) domains.

Contains 2 WW domains.

Sequence caution

The sequence AAF66069.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Adrb1P180903EBI-696226,EBI-991303
PTENP604843EBI-696226,EBI-696162From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14701470Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
PRO_0000341409

Regions

Domain18 – 10891PDZ 1
Domain116 – 290175Guanylate kinase-like
Domain296 – 32934WW 1
Domain342 – 37534WW 2
Domain413 – 49583PDZ 2
Domain581 – 65777PDZ 3
Domain729 – 81183PDZ 4
Domain852 – 93988PDZ 5
Domain1022 – 110483PDZ 6
Nucleotide binding123 – 1308ATP By similarity
Region18 – 10891Interaction with ADRB1 and TGFA
Region413 – 49583Interaction with PTEN By similarity
Region729 – 81183Interaction with BAI1 By similarity
Region852 – 93988Interaction with LPAR2 and GRIN2B By similarity
Compositional bias6 – 94Poly-Lys
Compositional bias240 – 2456Poly-Glu

Amino acid modifications

Modified residue2361Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JK71 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 70E2AFFCE5EA8480

FASTA1,470160,563
        10         20         30         40         50         60 
MSKTLKKKKH WLSKVQECAV SWAGPPGDLG AEIRGGAERG EFPYLGRLRD EPGGGGGTCC 

        70         80         90        100        110        120 
VVSGKAPSPG DVLLEVNGTP VSGLTNRDTL AVIRHFREPI RLKTVKPGKV INKDLRHYLS 

       130        140        150        160        170        180 
LQFQKGSIDH KLQQVIRDNL YLITIPCTTR APRDGEVPGV DYNFISVEQF KALEESGALL 

       190        200        210        220        230        240 
ESGTYDGNFY GTPKPPAEPS PFQPDPVDQV LFDNEFDTES QRKRTTSVSK MERMDSSLPE 

       250        260        270        280        290        300 
EEEDEDKEAV NGSGSMETRE MHSESSDCWM KTVPSYNQTN RSMDFRNYMM RDENLEPLPK 

       310        320        330        340        350        360 
NWEMAYTDTG TIYFIDHNTK TTTWLDPRLC KKAKAPEDCE DGELPYGWEK IEDPQYGTYY 

       370        380        390        400        410        420 
VDHLNQKTQF ENPVEEAKRK KQIGQAETHS AKTDVERAHF TRDPSQLKGV LVRASLKKST 

       430        440        450        460        470        480 
MGFGFTIIGG DRPDEFLQVK NVLKDGPAAQ DGKMAPGDVI VDINGNCVLG HTHADVVQMF 

       490        500        510        520        530        540 
QLVPVNQYVN LTLCRGYALP DDSEDPVVDI VAATPVINGQ SLAKGEACMS TQDFKLGAMV 

       550        560        570        580        590        600 
LDQNGKSGKL LSSDRLNGPS DSNEQRASLA SSGSSQPELV TIPLVKGPKG FGFAIADSPT 

       610        620        630        640        650        660 
GQKVKMILDS QWCQGLQKGD IIKEIYHQNV QNLTHLQVVE VLKQFPVGAD VPLLILRGGP 

       670        680        690        700        710        720 
CSPTKTAKMK TDTKETSGSL ETINEPTPQP MPFPPSIIRS GSPKLDPSEV YLKSKTLYED 

       730        740        750        760        770        780 
KPPNTKDLDV FLRKQESGFG FRVLGGDGPD QSIYIGAIIP LGAAEKDGRL RAADELMCID 

       790        800        810        820        830        840 
GIPVKGKSHK QVLDLMTTAA RNGHVLLTVR RKIFYGEKQP EDESPQAFSQ SGSPRLNRTE 

       850        860        870        880        890        900 
LPTRSAPQES YDVILQRKEN EGFGFVILTS KSKPPPGVIP HKIGRVIDGS PADRCGRLKV 

       910        920        930        940        950        960 
GDHISAVNGQ SIVDLSHDNI VQLIKDAGVT VTLTVVAEEE HHGPPSGTNS ARQSPALQHR 

       970        980        990       1000       1010       1020 
PMGQAQATHI PGDRTALEGE VGKDVCSSYR HSWSDHKHLA QPDTAVISVV GSRHSQSLGC 

      1030       1040       1050       1060       1070       1080 
YPVELERGPR GFGFSLRGGK EYNMGLFILR LAEDGPAIKD GRIHVGDQIV EINGEPTQGI 

      1090       1100       1110       1120       1130       1140 
THTRAIELIQ AGGNKVLLLL RPGTGLIPDH GDWDIYSPSS SNVIYDEQPP PLPSSHSAAT 

      1150       1160       1170       1180       1190       1200 
FEESHVPVTE DSLIRVQTCE KAEELKDTVQ EKKSTLNGSQ PEMKYQSIQK NVSKKDPSRS 

      1210       1220       1230       1240       1250       1260 
HGHGDKNLLK GENGVTRRGR SASPKKSVNR HSEEHLEKIP RPLRSDPKGK SRDRSLSPRK 

      1270       1280       1290       1300       1310       1320 
GENKGQVTIK AGSGQDPCRK DRGRSSSPRK QQKIGGNSLS NTEGKLSEAG SRRAAGLSSD 

      1330       1340       1350       1360       1370       1380 
SPEQLPEGKE KSGVSRKDLK LSQLGKNRTR SPEKRSSKVD EASLPSKKTS DTASRVVSEK 

      1390       1400       1410       1420       1430       1440 
EKGRKPGTGE RSRDKTGESV QTSAKPLTQE AGEKMALSKA SEVTDRGKER AGGAPESSSP 

      1450       1460       1470 
VKKAPITPGP WRVPRANKVT GTAGMADKQL 

« Hide

References

[1]"Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase beta (RPTP beta) and tyrosine-phosphorylated proteins."
Adamsky K., Arnold K., Sabanay H., Peles E.
J. Cell Sci. 116:1279-1289(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTPRB.
[2]"Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases."
Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R.
J. Biol. Chem. 280:28936-28943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTEN.
[3]"Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins."
He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., Castleberry A.M., Hall R.A.
J. Biol. Chem. 281:2820-2827(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ADRB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF255614 mRNA. Translation: AAF66069.1. Frameshift.
RefSeqNP_620784.2. NM_139084.2.
UniGeneRn.228785.

3D structure databases

ProteinModelPortalQ9JK71.
SMRQ9JK71. Positions 292-335, 343-383, 400-506, 570-662, 726-816, 1016-1111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid251439. 3 interactions.
IntActQ9JK71. 2 interactions.
STRING10116.ENSRNOP00000026952.

PTM databases

PhosphoSiteQ9JK71.

Proteomic databases

PaxDbQ9JK71.
PRIDEQ9JK71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID245903.
KEGGrno:245903.
UCSCRGD:621362. rat.

Organism-specific databases

CTD260425.
RGD621362. Magi3.

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000113463.
HOVERGENHBG007091.
InParanoidQ9JK71.
KOK06112.
PhylomeDBQ9JK71.

Gene expression databases

GenevestigatorQ9JK71.

Family and domain databases

Gene3D2.30.42.10. 6 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR001202. WW_dom.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 4 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 6 hits.
SM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 6 hits.
SSF51045. SSF51045. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 6 hits.
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio623144.
PROQ9JK71.

Entry information

Entry nameMAGI3_RAT
AccessionPrimary (citable) accession number: Q9JK71
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families