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   08-NOV-2023, entry version 135.
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; 10116-ENSRNOP00000026952; -.
DR   GeneID; 245903; -.
DR   KEGG; rno:245903; -.
DR   UCSC; RGD:621362; rat.
DR   AGR; RGD:621362; -.
DR   CTD; 260425; -.
DR   RGD; 621362; Magi3.
DR   eggNOG; KOG0707; Eukaryota.
DR   eggNOG; KOG3209; Eukaryota.
DR   InParanoid; Q9JK71; -.
DR   OrthoDB; 2902917at2759; -.
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; IEA:UniProtKB-SubCell.
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:0019903; F:protein phosphatase binding; IPI:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd00992; PDZ_signaling; 6.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.30.42.10; -; 6.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
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; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR   PANTHER; PTHR10316:SF10; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 6.
DR   SUPFAM; SSF51045; WW domain; 2.
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
//