ID A0A096LSV9_POEFO Unreviewed; 1462 AA.
AC A0A096LSV9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2b {ECO:0000313|Ensembl:ENSPFOP00000022250.1};
GN Name=MAGI2 {ECO:0000313|Ensembl:ENSPFOP00000022250.1};
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:ENSPFOP00000022250.1, 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:ENSPFOP00000022250.1}
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; AYCK01001904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01001905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01001906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000028028.1; ENSPFOP00000022250.1; ENSPFOG00000016872.2.
DR GeneTree; ENSGT00940000155057; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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; IPR041489; PDZ_6.
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:SF78; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF17820; PDZ_6; 1.
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; 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 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 92..185
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 311..344
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 357..390
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 437..507
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 598..663
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 774..864
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 921..1011
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1164..1246
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 177..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 158266 MW; 55473945FCE00768 CRC64;
MSKSLKKKNH WTNKVHEAVI TRGKEGELGF ELKGGAENGQ FPYFGEVKQG KGLIQSGKLA
QDELLLEVND MPVAGLTTRD VLAVIKHCKD PVRFKCVKQV GGVVDKDLRH YLNLRFSKGS
VDHDHQQIIR DNLYLRTVPC TTRQPKEGEV PGVDYNFVSV ERFMELEQSG ALLESGTYED
NFYGTPKPPA EPSPAAPPLN VSEALLPGAR PSAQGKRKRN QSVSNMEQRA SLEPPEEEEE
ESPVVNGNGV AITPESSEHE DKSTDASGEV AAEGSSQAPA SSEPPTEGEE APKSPSKSPS
KVPDADEEEL GPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECREDELP
YGWEKIDDPI YGSYYVDHIN RRTQFENPVL EAKRRLEQQR QMQSQGLSAL PLPTIYRGMK
KPLFTRDPTQ LKGTFLSTAL QKSNMGFGFT IIGGDEPDEF LQVKSVIPDG PAAQDGKMDT
AGDVIVYIND ICVLGTTHAD VVKLFQSVPI GQSVTLVLCR GYPLPFDPED PNAAASASLT
PIGLEHRPLV VNGRGSYDPY LEYLSASAHT PRDDNVSMAS SGAAGVAGAT GQGPELLTVT
MVKGAEGFGF TIADSPTGQR VKQVLEPGSQ GASGLIEGDL ILEVNQQPVA SAGHGRVVEM
LKECPVGAEA TLLIQRAGTG HISPWKASKQ VFNQWDPQGS PQTNLSGPVL PPGTPFPNQP
HHRTSVPDST EGFDLNKPDP YDLYEKSRAI YESRPPQVPK CPITPKSPEY EEVEVHLLRE
KTGFGFRILG GDEAVQAVSP DARDKIVIGA IIENTPAERD GRLRPGDELI SVDKNVVAGK
PHKYVIDLMH AAARNGQVSL TVRRRVQMPG EPCPVNGRSP GSVSTQHSSP RSDAASAPVP
VTTNAPAATS APEGTGLQTS DVVIHRKENE GFGFVIISSL NRPENTAVIT VPHKIGRIIE
GSPADRCGKL KVGDRILAVN GQSIISMPHA DIVKLIKDAG LTVTLHIIPE ESSQSGPNSE
KQSPMTQKHS PQTQPSPVAQ PNQGGTQTAA HTNQTVGGPP APAASQPAPA GTQQSPVAQP
SGLPPQLYLH DGRYFRSEVK ARQDVKPDFR HPPFTDYRQP PVDYRHPPVT DYRQPPTLDY
RHPPGLLDFR QHPAAVLQDY DYFTVELEKS AKGFGFSIRG GREYSMDLFV LRLAEDGPAI
RNGRMRVGDQ IIEINGDSTR DMTHARAIEL IKAGGRRVRL LLKRGTGQVP EYATDCASPW
DSLSTAHSAL QEVTLEPHLN PLLPSHPASS PDSPHRLHLE AKVCMADKVP LLTDHSSIRR
AIGGRSTEQK CVNVGQGTLQ GSGEVNPAPG EKPPRALPHK AVMGRSTDRR ERQKESCSPC
LNLNGASLGG DGPVGLQERL MSRNLFPRED EKAGGHSGVC CPSKTIEGPP ARSAAASPGP
WNIPGPDKLP GTLRSWTSTV SR
//
