ID A0A3Q2VGG9_HAPBU Unreviewed; 1070 AA.
AC A0A3Q2VGG9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 3 {ECO:0000313|Ensembl:ENSHBUP00000010310.1};
GN Name=MAGI3 {ECO:0000313|Ensembl:ENSHBUP00000010310.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000010310.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000010310.1}
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q2VGG9; -.
DR Ensembl; ENSHBUT00000017136.1; ENSHBUP00000010310.1; ENSHBUG00000000329.1.
DR GeneTree; ENSGT00940000156496; -.
DR OMA; KWNGERA; -.
DR Proteomes; UP000264840; 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:SF65; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 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; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
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 287..320
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 333..366
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 393..462
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 550..613
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 704..787
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 825..912
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 977..1059
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 216..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..948
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"
SQ SEQUENCE 1070 AA; 116952 MW; 1C5BFABC4CEE4BBF CRC64;
MSRTLKKKKH WSTKVVECAV SWGNLGDFGS VVEVLGGAEL GQFPYLGQMK LDVLVCHVGK
LPYYGDVLLE VNGTPVSGLT NRDTLAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQI IRDNLYLRTI PCTTRLPREG EVPGVDYNFI SVGDFRILEE SGLLLESGTY
DGNYYGTPKP PAEPNLVQPD LVDQVLFDED FGGEVPRKRT TSVSKMDRKD SAVPEEEDDD
ERPPLVNGLP EHKEGADWRK AVPSYTQSSS TMDFRTWSSL PRDDSLEPLP FNWEMAYTET
GMVYFIDHNT KTTTWLDPRL AKKAKPPEKC EDGELPYGWE EIDDPQYGTY YVDHINQKTQ
FENPVLEAKK KLSKGGASGF TADPSQLKGE IYHTALKKSS QGFGFTIIGG DRTDEFLQVK
NVLSDGPAAQ DKKMASGDVI VEINGVCVLG KTHPEVVQMF QSIPINQYVD MVLCRGYPLP
PDVDLDKVVT AVPLINGQPL LVKGDVLHGS SQELHYVTTD ASGRPVVAAL PNGRQGGEAA
TVMLQPELVS VPLVKGPGGF GFAIADCPLG QKVKMILDAQ WCRGLQKGDV IKEINRQNVQ
SLSHAQVVDI LKDLPVGSEV NVLVTPTLRM LTLLPPSPLP APLTQEMTAS TETLDIVTDS
APQALPYHSN TSTLRSADSP KRDATEIYLK SKALLEKPHA KDIDVFLKRD IETGFGFRVL
GGEGPQQPVY IGAIVPNGAA EKDGRLRAGD ELIGIDGVMV KGRSHKQVLD LMTNAARNGQ
VMLTVRRKQN LAYEDPQEMA PVLVNGSPKL PRLPMPSALD HESFDITLHR KETEGFGFVI
LTSKSKPPHG VIPHKIGRII GGSPTDRCGL LHVGDRISAV NGLSIIELSH NDIVQLIKEA
GNVVTLTVVP EDEYKGPPSG ASSAKQSPAL QHRAMGQRSA LQDEKEGVNW SDHKTLSLGE
TGTLCVTGPN QVRGCLTVEL ERGPRGFGFS LRGGTEYNMG LYILRLAEDG PAQQDGRIHV
GDEIVEINGE PARGISHTRA IDLIQAGGNK VVLLLRPGAG LAQDASEYII
//
