MAGI1_RAT
ID MAGI1_RAT Reviewed; 1255 AA.
AC Q4L1J4; Q4L1J5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1;
DE AltName: Full=BAI1-associated protein 1;
DE Short=BAP-1;
DE AltName: Full=Membrane-associated guanylate kinase inverted 1;
DE Short=MAGI-1;
GN Name=Magi1; Synonyms=Baiap1, Bap1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RA Tanemoto M., Abe T., Ito S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH IGSF5 AND NPHS1.
RX PubMed=16155592; DOI=10.1038/labinvest.3700347;
RA Hirabayashi S., Mori H., Kansaku A., Kurihara H., Sakai T., Shimizu F.,
RA Kawachi H., Hata Y.;
RT "MAGI-1 is a component of the glomerular slit diaphragm that is tightly
RT associated with nephrin.";
RL Lab. Invest. 85:1528-1543(2005).
RN [3]
RP INTERACTION WITH DDN.
RX PubMed=16751601; DOI=10.1093/jb/mvj105;
RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
RT "CIN85 is localized at synapses and forms a complex with S-SCAM via
RT dendrin.";
RL J. Biochem. 139:931-939(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, AND IDENTIFICATION BY
RP 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: May play a role as scaffolding protein at cell-cell
CC junctions. May regulate acid-induced ASIC3 currents by modulating its
CC expression at the cell surface.
CC -!- SUBUNIT: Interacts through its WW 2 domain with SYNPO and through its
CC PDZ 5 domain with ACTN4. Interacts with cytoplasmic domain of ADGRB1.
CC Interacts via its WW domains with DRPLA (By similarity). Interacts with
CC ESAM, LRP2 and CXADR. May interact with CTNNB1. Interacts through its
CC PDZ 1 domain with NET1 (By similarity). Interacts with ASIC3 and AMOT.
CC Interacts with FCHSD2 (By similarity). Interacts with IGSF5/JAM4 and
CC through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex
CC (PubMed:16155592). Interacts with DDN (PubMed:16751601). May interact
CC (via PDZ domain) with RAPGEF2 (By similarity). Interacts with DLL1 (By
CC similarity). Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16
CC heterodimer; this interaction may facilitate KCNJ10/KCNJ16 potassium
CC channel expression at the basolateral membrane in kidney tubular cells
CC (By similarity). Interacts with PRRG4 (via cytoplasmic domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q6RHR9,
CC ECO:0000250|UniProtKB:Q96QZ7, ECO:0000269|PubMed:16155592,
CC ECO:0000269|PubMed:16751601}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}. Note=Localizes to epithelial cells tight
CC junctions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4L1J4-1; Sequence=Displayed;
CC Name=2; Synonyms=NT-short isoform;
CC IsoId=Q4L1J4-2; Sequence=VSP_030762, VSP_030763, VSP_030764;
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DR EMBL; AY598951; AAT99088.1; -; mRNA.
DR EMBL; AY598952; AAT99089.1; -; mRNA.
DR RefSeq; NP_001025216.1; NM_001030045.1. [Q4L1J4-1]
DR AlphaFoldDB; Q4L1J4; -.
DR BMRB; Q4L1J4; -.
DR SMR; Q4L1J4; -.
DR BioGRID; 271569; 4.
DR IntAct; Q4L1J4; 7.
DR MINT; Q4L1J4; -.
DR STRING; 10116.ENSRNOP00000065881; -.
DR iPTMnet; Q4L1J4; -.
DR PhosphoSitePlus; Q4L1J4; -.
DR PaxDb; Q4L1J4; -.
DR PRIDE; Q4L1J4; -.
DR GeneID; 500261; -.
DR KEGG; rno:500261; -.
DR UCSC; RGD:1586025; rat. [Q4L1J4-1]
DR CTD; 9223; -.
DR RGD; 1586025; Magi1.
DR eggNOG; KOG3209; Eukaryota.
DR InParanoid; Q4L1J4; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q4L1J4; -.
DR PRO; PR:Q4L1J4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
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; IPR030033; MAGI1.
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:SF12; PTHR10316:SF12; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 5.
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 Alternative splicing; ATP-binding; Cell junction; Cytoplasm; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Tight junction.
FT CHAIN 1..1255
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 1"
FT /id="PRO_0000316294"
FT DOMAIN 17..105
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 96..287
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 300..333
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 359..392
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 471..553
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 642..720
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 840..922
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 997..1093
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1151..1233
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 208..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6RHR9"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030762"
FT VAR_SEQ 212..216
FT /note="SGSKQ -> MHREA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030763"
FT VAR_SEQ 803..833
FT /note="DRPMSPSPASGLSKGERDREINSTNFGECQI -> NRL (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030764"
FT CONFLICT 323
FT /note="A -> T (in Ref. 1; AAT99088)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="E -> K (in Ref. 1; AAT99088)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="G -> E (in Ref. 1; AAT99088)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="T -> A (in Ref. 1; AAT99088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1255 AA; 136327 MW; 1024AC37A6C44802 CRC64;
MSKVIQKKNH WTGRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAA EAAGLPGGGE
GPKLAEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL EQSGTLLEVG
TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHTENEE
EEDVPEMNSS FTADSGDQDE PTLQEATLPP VNSSALAAPI TDPSQKFPQY LPLSAEDNLG
PLPENWEMAY TENGEVYFID HNAKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE
LPAGWEKIED PVYGVYYVDH INRKTQYENP VLEAKRKRQL EQQQQQQQHQ QQPQQPQPPQ
PEEWTEDHAS VVPPVAPSHP PSNPEPAREA PLQGKPFFTR NPSELEGKFI HTKLRKSSRG
FGFTVVGGDE PDEFLQIKSL VLDGPAALDG KMETGDVIVS VNDTCVLGHT HAQVVKIFQS
IPIGASVDLE LCRGYPLPFD PDDPNTSLVT SVAILDKEPI IVNGQETYDS PASHSSKTGK
VSNMKDARPS SPADVASNSS HGYPNDTVSL ASSIATQPEL ITVHIVKGPM GFGFTIADSP
GGGGQRVKQI VDSPRCRGLK EGDLIVEVNK RNVQALTHNQ VVDMLIECPK GSEVTLLVQR
GGLPVPKKSP KSQPLERKDS QNSSQHSVSS LRSLHTASPS HSAQVLPEYP PADVPAPDQT
DSSGQKKPDP FKIWAQSRSM YEDRPMSPSP ASGLSKGERD REINSTNFGE CQIPDYQEQD
IFLWRKETGF GFRILGGNEP GEPIYIGHIV PLGAADTDGR LRSGDELICV DGTPVIGKSH
QLVVQLMQQA AKQGHVNLTV RRKVVFTVPK AENEVPSPAS SHHSSNQPAS LTEEKRTPQG
SQNSLNTVSS GSGSTSGIGS GGGGGSGVVS AVLQPYDVEI RRGENEGFGF VIVSSVSRPE
AGTTFAGNAC VAMPHKIGRI IEGSPADRCG KLKVGDRILA VNGCSITNKS HSDIVNLIKE
AGNTVTLRII PGDESSNATL LTNAEKIATI TTTHAPSQQG TQETRTTTKP KPDSQFEFKG
PQATQEQDFY TVELERGAKG FGFSLRGGRE YNMDLYVLRL AEDGPAERCG KMRIGDEILE
INGETTKNMK HSRAIELIKN GGRRVRLFLR RGDGSVPEYG GSNYENIPSF PGMTP
