ID A0A087YDI3_POEFO Unreviewed; 1130 AA.
AC A0A087YDI3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 {ECO:0000313|Ensembl:ENSPFOP00000016086.2};
GN Name=MAGI3 {ECO:0000313|Ensembl:ENSPFOP00000016086.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016086.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016086.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; AYCK01002395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01002396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007547024.1; XM_007546962.2.
DR AlphaFoldDB; A0A087YDI3; -.
DR STRING; 48698.ENSPFOP00000016086; -.
DR Ensembl; ENSPFOT00000016108.2; ENSPFOP00000016086.2; ENSPFOG00000015969.2.
DR GeneID; 103134631; -.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000156496; -.
DR OMA; MHDERYN; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
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 284..317
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 330..363
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 406..475
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 588..651
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 739..827
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 868..955
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1027..1109
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 217..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 123994 MW; 0C5A0411D1B2835E CRC64;
MSRTLKKKKH WSTKVVECAV SWGSLGDFGS VVEILGGAEL GQFPYIGQMK LDVLVCHVGK
LPYYGDVLLE VNGTPVSGLT NRDTLAVIRH FREPIRLKTV KPGKVLNTDL RHYLSLQFQK
GSLDHKLQQI IRDNLYLRTI PCTTRLPREG EVPGVDYNFI SVGDFRILEE SGLLLESGTY
DGNYYGTPKP PAEPNLVQPD LVDQVLFDED FSGEVPRKRT TSVSKMDRKD SAVPEEEDDD
ERPPLVNGLP EHKDWRKTVP SYNQSSSTMD FRTWSSLPRD DSLEPLPYNW EMAYTETGMV
YFIDHNTKTT TWLDPRLAKK AKPPEKCEDG ELPYGWEEID DPQYGTYYVD HINQRTQFEN
PVLEAKKKLS KDTASIQQAA TASSQGKGSM LGFTADPSQL KGEMYHTALK KSSQGFGFTI
IGGDRTDEFL QVKNVLSDGP AAQDNKMGSG DVIVEINGTC VLGKTHPEVV QMFQSIPINQ
YVDMVLCRGY PLPPDVDLNN DDPLPPPPPP PATQPQQPLH GGEVVTAVPL INGQPLLVKG
DVLHGSSQEL HYVTTDASGR PVVAALPNGR QPDQGEGATG MLQPELVSVP LVKGPGGFGF
AIADCPLGQK VKMILDAQWC RGLQKGDVIK EINRQNVQSL SHAKVVDILK DFPVGSEVSV
LVLRGGQTSP VKTLKPRQEM TASTETLDTI ADATPQALPY HSNTSTLRSS DSPKRDATEM
YLKSKALLES RQPHTKDIDV FLKRDIETGF GFRVLGGEGP QQPNVFPQVY IGAIVPSGAA
EKDGRLRAGD ELIGIDGVMV KGRSHKQVLD LMTNAARNGQ VMLTVRRKVI YREATDEDIQ
EMTPVLVNGS PKLPRLPMPS ALDHESFDIT LHRKENEGFG FVILTSKSKP PYGVIPHKIG
RIIEGSPTDR CGLLHVGDRI SAVNGRSIIE LSHNDIVQLI KEAGTVVTLT VVPEDEYKGP
PSGASSAKQS PALQHRPIGQ RSALHDERYN LDMEDKRDGV NWSDHKTLPP GEQGTLCVTG
PNQGCLTVEL ERGPRGFGFS LRGGTEYNMG LYILRLAEDG PAQLDGRIHV GDEIVEINGE
PARGISHTRA IDLIQAGGNK VVLLLRPGAG LAQDGSNTAS TTCYYTEHQH
//
