ID A0A3B5BFM3_9TELE Unreviewed; 1478 AA.
AC A0A3B5BFM3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 {ECO:0000256|ARBA:ARBA00016171};
DE AltName: Full=Membrane-associated guanylate kinase inverted 3 {ECO:0000256|ARBA:ARBA00033438};
GN Name=MAGI3 {ECO:0000313|Ensembl:ENSSPAP00000024997.1};
GN Synonyms=magi3 {ECO:0000313|RefSeq:XP_008291510.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000024997.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000024997.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008291510.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR RefSeq; XP_008291510.1; XM_008293288.1.
DR STRING; 144197.ENSSPAP00000024997; -.
DR Ensembl; ENSSPAT00000025406.1; ENSSPAP00000024997.1; ENSSPAG00000018898.1.
DR GeneID; 103365754; -.
DR CTD; 561689; -.
DR GeneTree; ENSGT00940000156496; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR CDD; cd00992; PDZ_signaling; 5.
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 3: Inferred from homology;
KW Kinase {ECO:0000313|RefSeq:XP_008291510.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000313|RefSeq:XP_008291510.1}.
FT DOMAIN 65..103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 111..187
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 285..318
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 331..364
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 410..479
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 587..650
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 771..854
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 906..993
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1054..1136
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 216..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 160927 MW; F6A1942741D4E704 CRC64;
MSKTLKKKKH WSTKVQECTV SWGGSGELVT VVEVRGGAEL GEFPYLGHIV SEAMVCHTGR
FPGSGDVLLE VNGTPVSGLT NRDTLAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQV IRDNLYLRTI PCTTRQPREG EVPGVDYNFI SVGEFRDLEE SGLLLESGTY
DGNYYGTPKP PAEPSPVQPD LVDQVLFDEE FDTEVQRKRT TSVSKMDRKD SAAPEEEEED
ERPPMVNGLA EHKDKAEWRK TVPSYNQSAG AMDLRVWNTQ DESQEPLPKN WEMAYTETGM
VYFIDHNSKT TTWLDPRLAK KAKPPEKCEE GELPYGWEKI EDPQYGTYYV DHINQKTQFE
NPVLEAKRKL SVDVPIAAPP PAATPSAEEP SRGVRGFTRD PSQLQGSILQ TALRKSPQGF
GFTIIGGDRP DEFLQVKNVL PDGPAAHDNK IASGDVIVDI NGACVLGKTH ADVVQMFQSI
PINQYVDMVL CRGYPLPEDS SSSEDASGGV GTSKDTSPSP STSTPQDPHY TVPDGGTLPR
QTAAVPPMTN GGRHHHHAHP HQHHHHLPHA LNQEGPDPTL LQPELVSVPL VKGPGGFGFA
IADCPLGQKV KMILDAQWCR GLLKGDVIKE INRQNVQTLS HSQVVDILKD LPVGSEVNVL
VLRGGQTSPV KSLKPCTAPM SHSVSQPTPH QAPHPATQQL PHPSSQPIMQ QQRQEMISST
ETLSQPEVQP SPLSFPANTL RSSSPKPDAS ELYLKSRAML DSKPPNTKDL DVFIKRNQES
GFGFRVLGGE GPDQPVYIGA IVPLGAAEKD GRLRAGDELL CIDGVPVKGK SHKQVLELMT
NAARNGQVML TVRRKLAHTD GGTEEESGQQ PQQVASALVN SSPKMPRVEV PNSVQPGQSS
RPECFDVTLQ RKDNEGFGFV ILTSKNKPPP GVIPHKIGRI IEGSPTDRIG QMKVGDRISA
VNGRSIMELS HNDIVQLIKD AGNSVTLTVV PEDDSAPPSG TNSAKQSPSA QHRAVGQQPP
SYPDRNGDSD ARNSLAQKEM GALIASGPKQ GCFVVELERS QRGFGFSLRG GKEYNMGLFI
LRLAEDGPAL KDGRIHVGDQ IVEINGEATQ GITHTRAIEL IQAGGSKVHL LLRPGQGLVP
DHSSKDKVTI PTSSFPRLSV SDGQSSPASP SSVSLSTSEL SPSSPKISAP DEFSGGDGRV
SGSPGAGQEH GRQANRSRGQ QLSHHNHKRT TSPGAQARKT GRSDSKSGSP RRATEGWTDH
VESSQSPRKT DRGHGGSLED MGKERKAQGQ RDYHSSSPRK GSKRENDLTG PLRNLEEPQS
PRRPAGQQPN VASGEEKDWR YREEDATYWQ ERGGKESGDK SWGTSERHRK GKRAEQEAAA
QKSYSQEHRE RSGSDADSGT LSRRSGRGKA DKEYRESRYP GPAEDVSRKD PRGSSSSIQD
PSCNGTTTSK KAPITPGPWK VPSSAKIQSQ ADTTYADV
//
