ID A0A3Q1FS91_9TELE Unreviewed; 1471 AA.
AC A0A3Q1FS91;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:ENSAPOP00000018512.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018512.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000018512.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 80966.ENSAPOP00000018512; -.
DR Ensembl; ENSAPOT00000028142.1; ENSAPOP00000018512.1; ENSAPOG00000021907.1.
DR GeneTree; ENSGT00940000156496; -.
DR InParanoid; A0A3Q1FS91; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd22541; SP5_N; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
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 585..648
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 769..852
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 904..991
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1047..1129
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 375..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1471
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 668..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1471 AA; 160417 MW; 1EB0D4B48FCFFB60 CRC64;
MSKTLKKKKH WSTKVQECTV SWGGSGELVT VVEVRGGAEL GEFPYLGHIV LEAMVCHTGR
FPSGGDVLLE VNGTPVSGLT NRDTLAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQV IRDNLYLRTI PCTTRQPREG EVPGVDYNFI SVGEFRELEE SGLLLESGTY
DGNYYGTPKP PAEPSPVQPD LVDQVLFDEE FDTEVQRKRT TSVSKMDRKD SAAPEEEEED
ERPPMVNGLA EHKDKAEWRK TVPSYNQSAG AMDLRVWNTQ DESQEPLPKN WEMAYTETGM
VYFIDHNSKT TTWLDPRLAK KAKPPEKCEE GELPYGWEKI EDPQYGTYYV DHINQKTQFE
NPVLEAKRKL SVDTPIAAPP PAATPSAEEP GRGARGFTRD PSQLQGSILQ TALRKSPQGF
GFTIIGGDRP DEFLQVKNVL PDGPAAHDNK IASGDVIVDI NGTCVLGKTH ADVVQMFQSI
PINQYVDMVL CRGYPLPEDS SSSEEASGGV GTSKDTSPSP STSTPQDPHY TIPDGGSLPR
QTAAVPPMTN GGRHHHHPHQ HHHHLPHALN QEGPDPTLLQ PELVSVPLVK GPGGFGFAIA
DCPLGQKVKM ILDAQWCRGL LKGDVIKEIN RQNVQTLSHS QVVDILKDLP VGSEVNVLVL
RGGQTSPVKS LKPCTAPMSH TVSQPTPHQT PHPVPQQLSH PSSQPIIQQQ RQEMISSTET
LSQPEMQPSP LSFPANTLRS SSPKPDASEL YLKSRAILDS KPPNTKDLDV FIKRNQESGF
GFRVLGGEGP DQPVYIGAIV PLGAAEKDGR LRAGDELLCI DGVPVKGKSH KQVLELMTNA
ARNGQVMLTV RRKLAHTDGG AEDESSQQPH QVASALVNSS PKMPRVEVSN TVQPGQSSRL
ECFDVTLHRK DNEGFGFVIL TSKNKPPPGV IPHKIGRIIE GSPTDRIGQM KVGDRISAVN
GRSIMELSHN DIVQLIKDAG NSVTLTVVPE DDSAPPSGTN SAKQSPSAQH RAVGQQPPSY
PDRNGDSDAR REMGTLIASG PKQGCFVVEL ERSQRGFGFS LRGGKEYNMG LFILRLAEDG
PALKDGRIHV GDQIVEINGE ATQGITHTRA IELIQAGGSK VHLLLRPGQG LVPDHSSKDK
VTIPTSSFPR LSVSDGQSSP ASPSSVSLST SELSPSSPKI SAPDEFSGGD GRVSWSPAAG
QEHGRQANRS RGQQLSDHNH KRTTSPSAQA RKTSRSDSKS GSPRRAAEGW MDHVVRSQSP
RKQERGHSGS LEDMSKERKA QGQRDHHSSS PRKGSKREND PAGPLRNLEE PQSPRRPAGQ
QPHVASGEEK DWRYKEEDAP YWQERGAKES GDKSGGTGER HRKGKRAEQE AAAQKSYSQV
HRERSGSDAD SGTLGRRSGR EKGDKEYRES KYPGPAEDGI RKDPRGSSSS IQDPSCNGTT
ASKKAPITPG PWKVPSSAKI QSQVDTTYAD V
//
