MAGI3_XENTR
ID MAGI3_XENTR Reviewed; 1107 AA.
AC A1A5G4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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;
GN Name=magi3;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby
CC regulating various cellular and signaling processes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; BC128638; AAI28639.1; -; mRNA.
DR RefSeq; NP_001090712.1; NM_001097243.1.
DR AlphaFoldDB; A1A5G4; -.
DR SMR; A1A5G4; -.
DR PaxDb; A1A5G4; -.
DR GeneID; 100036692; -.
DR KEGG; xtr:100036692; -.
DR CTD; 260425; -.
DR Xenbase; XB-GENE-981179; magi3.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR InParanoid; A1A5G4; -.
DR OrthoDB; 284488at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1107
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 3"
FT /id="PRO_0000341411"
FT DOMAIN 17..102
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 110..284
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 289..322
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 335..368
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 407..489
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 577..653
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 727..809
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 853..940
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1003..1085
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 210..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
SQ SEQUENCE 1107 AA; 121840 MW; E1EA1EF7D0F4D083 CRC64;
MSKTLKKKKH WLSKVQECGL SGVGGDPCSL LEIRGGAEHG EFPYLGRQRE DVASFIVGKV
PSQGDVLLEV NGTPVSGLTH RDTLAVIRHF REPIRLKTVK PGKVINKDLR HYLSLQFQKG
SIDHKLQQVI RDNLYLRTIP CTTRSPRDGE VPGVDYNFIS VEQFKALEDS GVLLESGTYD
GNFYGTPKPP AEPNPFQADP VDQVLFDGEF DTETQRKRTT SVSKMQRTDS SLPEEEDEEE
REAVNGSSGS TDHRDRQEPS EWGKTVPSYN QTNSSMDFRN YLTRDENLEP LPKNWEMAYT
EAGMIYFIDH NTKTTTWLDP RLCKKAKAPE DCEDGELPYG WEKIEDPQYG TYYVDHINQK
TQFDNPVLEA KRKKQLNPAP SEGTVHQEPE NSQFTRDPSQ LKGALLHTSL KKSAMGFGFT
IIGGDRPDEF LQVKNVLKDG PAAQDGKIAP GDVIVDINGT CVLGHTHAEV VQMFQLIPIN
QYVNMTLCRG YPLPEDSDDP VADIVNTVPP IINGQMLTQG DINMGSQELK SGVIDLDQRG
KPGLMVVNGR LNGPSLDIQD QRTSMASSGN SLPELVTIPL LKGPKGFGFA IADSPMGQKV
KMILDSQWCP GLQKGDVIKE ICHQNVQNLT HIQVVEVLKQ FPVGAEVPLL ILRGGPPSPS
KVTKVKSDKQ ELMGSIEAIA PGEPLPQPLP FPPNLARSCS PKLDPSEVYK KSKNIFEDKP
PNTKDLDVFL RKQESGFGFR VLGGDGPDQA IYIGAIIPLG AAEKDGRLRA ADELICIDGV
PVKGKSHKQV LDLMTNAARN GHVLLTVRRQ IYYTDKQQEE EELQHTPPAH NGSPRLNRIE
VSAIPKLPAE AYDVILQRKD NEGFGFVILT SKNKPPPGVI PHKIGRVIEG SPADRCRKLK
VGDRISAVNG QSIVELSHDN IVQLIKDAGN TVTLTVIAEE EHRGPPSGSN SARQSPAPQH
RPMGQTQPTY GTLDRYSWSD HKADCGPALP AGSWQALSVG CYPVELERGP RGFGFSLRGG
KEYNMGLFIL RLAEDGPAIK DGRIHVGDQI VEINNEPTQG ITHTRAIELI QAGGSKVLLL
LRPGTGLIPD YSLAPSSLCS YVKPDQQ
