MAGI3_RAT
ID MAGI3_RAT Reviewed; 1470 AA.
AC Q9JK71;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3;
DE AltName: Full=Membrane-associated guanylate kinase inverted 3;
DE Short=MAGI-3;
DE AltName: Full=Scaffolding-like protein;
GN Name=Magi3; Synonyms=Slipr;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH PTPRB.
RX PubMed=12615970; DOI=10.1242/jcs.00302;
RA Adamsky K., Arnold K., Sabanay H., Peles E.;
RT "Junctional protein MAGI-3 interacts with receptor tyrosine phosphatase
RT beta (RPTP beta) and tyrosine-phosphorylated proteins.";
RL J. Cell Sci. 116:1279-1289(2003).
RN [2]
RP INTERACTION WITH PTEN.
RX PubMed=15951562; DOI=10.1074/jbc.m504761200;
RA Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA Antonarakis S.E., Pulido R.;
RT "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT stability and phosphorylation by microtubule-associated serine/threonine
RT kinases.";
RL J. Biol. Chem. 280:28936-28943(2005).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ADRB1.
RX PubMed=16316992; DOI=10.1074/jbc.m509503200;
RA He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., Castleberry A.M.,
RA Hall R.A.;
RT "Proteomic analysis of beta1-adrenergic receptor interactions with PDZ
RT scaffold proteins.";
RL J. Biol. Chem. 281:2820-2827(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702; SER-833 AND SER-1321,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
CC -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby
CC regulating various cellular and signaling processes. Cooperates with
CC PTEN to modulate the kinase activity of AKT1. Its interaction with
CC PTPRB and tyrosine phosphorylated proteins suggests that it may link
CC receptor tyrosine phosphatase with its substrates at the plasma
CC membrane. In polarized epithelial cells, involved in efficient
CC trafficking of TGFA to the cell surface. Regulates the ability of LPAR2
CC to activate ERK and RhoA pathways. Regulates the JNK signaling cascade
CC via its interaction with FZD4 and VANGL2.
CC {ECO:0000269|PubMed:12615970}.
CC -!- SUBUNIT: Interacts with ADRB1, ADGRB1, LPAR2/EDG4, FZD4, FZD7, GRIN2B,
CC TGFA and VANGL2 (By similarity). Interacts with PTEN. Interacts with
CC ADRB1, PTPRB and unidentified tyrosine phosphorylated proteins.
CC Interacts with DLL1 (By similarity). Interacts with PRRG4 (via
CC cytoplasmic domain) (By similarity). {ECO:0000250|UniProtKB:Q5TCQ9,
CC ECO:0000250|UniProtKB:Q9EQJ9, ECO:0000269|PubMed:12615970,
CC ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:16316992}.
CC -!- INTERACTION:
CC Q9JK71; P18090: Adrb1; NbExp=3; IntAct=EBI-696226, EBI-991303;
CC Q9JK71; P60484: PTEN; Xeno; NbExp=3; IntAct=EBI-696226, EBI-696162;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Nucleus. Note=Concentrates in specific sites
CC at the plasma membrane and in the nucleus. In epithelial cells, it
CC localizes at tight junctions.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66069.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF255614; AAF66069.1; ALT_FRAME; mRNA.
DR RefSeq; NP_620784.2; NM_139084.2.
DR AlphaFoldDB; Q9JK71; -.
DR SMR; Q9JK71; -.
DR BioGRID; 251439; 3.
DR IntAct; Q9JK71; 2.
DR STRING; 10116.ENSRNOP00000026952; -.
DR iPTMnet; Q9JK71; -.
DR PhosphoSitePlus; Q9JK71; -.
DR PaxDb; Q9JK71; -.
DR PRIDE; Q9JK71; -.
DR GeneID; 245903; -.
DR KEGG; rno:245903; -.
DR UCSC; RGD:621362; rat.
DR CTD; 260425; -.
DR RGD; 621362; Magi3.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR InParanoid; Q9JK71; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q9JK71; -.
DR PRO; PR:Q9JK71; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005109; F:frizzled binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0046328; P:regulation of JNK cascade; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030035; MAGI3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF10; PTHR10316:SF10; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1470
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 3"
FT /id="PRO_0000341409"
FT DOMAIN 18..108
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 116..290
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 296..329
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 342..375
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 413..495
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 581..657
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 729..811
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 852..939
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1022..1104
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 18..108
FT /note="Interaction with ADRB1 and TGFA"
FT /evidence="ECO:0000269|PubMed:16316992"
FT REGION 184..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..495
FT /note="Interaction with PTEN"
FT /evidence="ECO:0000250"
FT REGION 550..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..811
FT /note="Interaction with ADGRB1"
FT /evidence="ECO:0000250"
FT REGION 818..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..939
FT /note="Interaction with LPAR2 and GRIN2B"
FT /evidence="ECO:0000250"
FT REGION 939..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQJ9"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TCQ9"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQJ9"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1470 AA; 160563 MW; 70E2AFFCE5EA8480 CRC64;
MSKTLKKKKH WLSKVQECAV SWAGPPGDLG AEIRGGAERG EFPYLGRLRD EPGGGGGTCC
VVSGKAPSPG DVLLEVNGTP VSGLTNRDTL AVIRHFREPI RLKTVKPGKV INKDLRHYLS
LQFQKGSIDH KLQQVIRDNL YLITIPCTTR APRDGEVPGV DYNFISVEQF KALEESGALL
ESGTYDGNFY GTPKPPAEPS PFQPDPVDQV LFDNEFDTES QRKRTTSVSK MERMDSSLPE
EEEDEDKEAV NGSGSMETRE MHSESSDCWM KTVPSYNQTN RSMDFRNYMM RDENLEPLPK
NWEMAYTDTG TIYFIDHNTK TTTWLDPRLC KKAKAPEDCE DGELPYGWEK IEDPQYGTYY
VDHLNQKTQF ENPVEEAKRK KQIGQAETHS AKTDVERAHF TRDPSQLKGV LVRASLKKST
MGFGFTIIGG DRPDEFLQVK NVLKDGPAAQ DGKMAPGDVI VDINGNCVLG HTHADVVQMF
QLVPVNQYVN LTLCRGYALP DDSEDPVVDI VAATPVINGQ SLAKGEACMS TQDFKLGAMV
LDQNGKSGKL LSSDRLNGPS DSNEQRASLA SSGSSQPELV TIPLVKGPKG FGFAIADSPT
GQKVKMILDS QWCQGLQKGD IIKEIYHQNV QNLTHLQVVE VLKQFPVGAD VPLLILRGGP
CSPTKTAKMK TDTKETSGSL ETINEPTPQP MPFPPSIIRS GSPKLDPSEV YLKSKTLYED
KPPNTKDLDV FLRKQESGFG FRVLGGDGPD QSIYIGAIIP LGAAEKDGRL RAADELMCID
GIPVKGKSHK QVLDLMTTAA RNGHVLLTVR RKIFYGEKQP EDESPQAFSQ SGSPRLNRTE
LPTRSAPQES YDVILQRKEN EGFGFVILTS KSKPPPGVIP HKIGRVIDGS PADRCGRLKV
GDHISAVNGQ SIVDLSHDNI VQLIKDAGVT VTLTVVAEEE HHGPPSGTNS ARQSPALQHR
PMGQAQATHI PGDRTALEGE VGKDVCSSYR HSWSDHKHLA QPDTAVISVV GSRHSQSLGC
YPVELERGPR GFGFSLRGGK EYNMGLFILR LAEDGPAIKD GRIHVGDQIV EINGEPTQGI
THTRAIELIQ AGGNKVLLLL RPGTGLIPDH GDWDIYSPSS SNVIYDEQPP PLPSSHSAAT
FEESHVPVTE DSLIRVQTCE KAEELKDTVQ EKKSTLNGSQ PEMKYQSIQK NVSKKDPSRS
HGHGDKNLLK GENGVTRRGR SASPKKSVNR HSEEHLEKIP RPLRSDPKGK SRDRSLSPRK
GENKGQVTIK AGSGQDPCRK DRGRSSSPRK QQKIGGNSLS NTEGKLSEAG SRRAAGLSSD
SPEQLPEGKE KSGVSRKDLK LSQLGKNRTR SPEKRSSKVD EASLPSKKTS DTASRVVSEK
EKGRKPGTGE RSRDKTGESV QTSAKPLTQE AGEKMALSKA SEVTDRGKER AGGAPESSSP
VKKAPITPGP WRVPRANKVT GTAGMADKQL
