ID A0A3Q3EXJ4_9LABR Unreviewed; 1272 AA.
AC A0A3Q3EXJ4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1-like {ECO:0000313|Ensembl:ENSLBEP00000012079.1};
GN Name=MAGI1 {ECO:0000313|Ensembl:ENSLBEP00000012079.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000012079.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000012079.1}
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}.
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DR AlphaFoldDB; A0A3Q3EXJ4; -.
DR Ensembl; ENSLBET00000012707.1; ENSLBEP00000012079.1; ENSLBEG00000009222.1.
DR GeneTree; ENSGT00940000155820; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF77; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 1.
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; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 93..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 296..345
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 372..405
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 482..551
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 651..729
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 834..916
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 995..1079
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1135..1217
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 200..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 138156 MW; 7B8E879109E17940 CRC64;
MSKVLQKKNH WINKVNDCAL NPDACGELNV ELLGGAENGE FAYIGQVRED AALYQDGKLS
KGELVLEVEG LAVSGLPLYD ILAVIKCCQG PVRLKTVRQG HKLNKDLKHY LSLRFPKSSP
DHELQKIIRA NLYRHAVPCT TRPPRDGEVP GVDYNFLSVE DFLELEESGT LLEIGTYDGN
YYGTPKPPRQ PIIGTVILSD AGSQQSTPKR TKSYNDMQNA RVVPADDDDD DQASEMNNSF
TGNPNDPDES RGGILRPYPV RDNAPPCGLN NAATSTSESG QQTLAEPQVS PEDPLGTLPE
NWEMAYTENG ELYFIDTAKA HHPDMAVYFQ SFHNTKTTSW LDPRCRDKAS RPLEECDDDE
EGIHTEELEA DLELPPGWER IEDPVYGVYY VDHINRKTQY ENPVLEARRR KILEQQQPQP
PEEWIEEHSS AAAPLANYAP NHLETYRDPQ GPPALPPGPA GIKRGKPFFT RNPAELKGTF
INTKLKKSRR GFGFTVVGGD EPDEFLQIKS LVLDGPAAVD GKMETGDVIV SVNDTIVLGY
THAQVVKIFQ SIPIGSMVDL ALCRGYPLPF DPDDPNTSLV TSVAILDKEP IIVNGQETFD
SPSNQGGPIN GMRDPRPHSP SADVASNGSH GYSSDVVTLA SSIATQPELI TIHMEKGDKG
FGFTIADSLT GGGQRVKQIV DYPRCRGLKE GDILMEVNKR NVQNMSHNQV VDLLSKCPRG
SEVTMLVQRG VVQAKRSPKL VHQLERKDSQ SSSQHSVCSH RSTHADSPSH PSSAMPSEAV
APTPAAPTQP LPGLPPLDPA DGTLTLQKKP DPFKIWAQSR SMYESRLPDC QEQDIFLWRK
DTGFGFRILG GNEPGEPIYI GHIVKYGAAD EDGRLRSGDE LICVDGTAVV GKSHQLVVQL
MQQAAKQGHV NLTVRRKSPG YGVSKGEGDV PPSPASSHHS STQAPSLTEG KRTPQGSQNS
LNTVSSGSGS TSGIGSGGGG GSGSAVVPAS LQPYDVEIQR GENEGFGFVI VSSVSRPDAG
TTFGRIIEGS PADRCGKLKV GDRILAVNCC SITNKSHSDI VNLIKEAGNT VSLRIIPGDE
SSNASLLTNA EKIATITTTH TPQQTTESRN NSKSKGAPPP PPTQSQTSQD AEFYSVDLER
DSKGFGFSLR GGREYNMDLY VLRLAEDGAA VRNGKMRVGD EILEINGEST KNMKHSRAIE
LIKNGGRRAR LVLKRGDGSV PEYAMMAPHL AVGTMRNDKM GEPCFYLMGQ NQTTTAAVTG
TLPHPGHKTL RK
//
