ID A0A0G2JEG6_MOUSE Unreviewed; 1400 AA.
AC A0A0G2JEG6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2 {ECO:0000313|Ensembl:ENSMUSP00000142764.2};
GN Name=Magi2 {ECO:0000313|Ensembl:ENSMUSP00000142764.2,
GN ECO:0000313|MGI:MGI:1354953};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000142764.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:18034455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000142764.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142764.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000142764.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142764.2};
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 RefSeq; XP_006535808.1; XM_006535745.3.
DR SMR; A0A0G2JEG6; -.
DR ProteomicsDB; 363252; -.
DR Antibodypedia; 2880; 300 antibodies from 33 providers.
DR Ensembl; ENSMUST00000197443.5; ENSMUSP00000142764.2; ENSMUSG00000040003.19.
DR GeneID; 50791; -.
DR AGR; MGI:1354953; -.
DR CTD; 9863; -.
DR MGI; MGI:1354953; Magi2.
DR VEuPathDB; HostDB:ENSMUSG00000040003; -.
DR GeneTree; ENSGT00940000155057; -.
DR OrthoDB; 2902917at2759; -.
DR BioGRID-ORCS; 50791; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Magi2; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000040003; Expressed in rostral migratory stream and 204 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JEG6; baseline and differential.
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:SF27; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 6.
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 1: Evidence at protein level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|MaxQB:A0A0G2JEG6,
KW ECO:0007829|PeptideAtlas:A0A0G2JEG6};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 17..101
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 109..185
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 301..334
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 347..380
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 425..494
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 604..667
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 763..845
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 905..995
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1125..1207
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 203..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 153456 MW; D3B51FE551AAEF3A CRC64;
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EEFMELEKSG ALLESGTYED
NYYGTPKPPA EPAPLLNVTD QILPGATPSA EGKRKRNKSV TNMEKASIEP PEEEEEERPV
VNGNGVVITP ESSEHEDKSA GASGETPSQP YPAPVYSQPE ELKDQMDDTK PTKPEENEDS
DPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECKENELP YGWEKIDDPI
YGTYYVDHIN RRTQFENPVL EAKRKLQQHN MPHTELGAKP LQAPGFREKP LFTRDASQLK
GTFLSTTLKK SNMGFGFTII GGDEPDEFLQ VKSVIPDGPA AQDGKMETGD VIVYINEVCV
LGHTHADVVK LFQSVPIGQS VNLVLCRGYP LPFDPEDPAN SMVPPLAIME RPPPVMVNGR
HNYETYLEYI SRTSQSVPDI TDRPPHSLHS MPADGQLDGT YPPPVHDDNV SMASSGATQA
ELMTLTIVKG AQGFGFTIAD SPTGQRVKQI LDIQGCPGLC EGDLIVEINQ QNVQNLSHTE
VVDILKDCPV GSETSLIIHR GGFFSPWKTP KPMMDRWENQ GSPQTSLSAP AVPQNLPFPP
ALHRSSFPDS TEAFDPRKPD PYELYEKSRA IYESRRPDYK ELDVHLRRME SGFGFRILGG
DEPGQPILIG AVIAMGSADR DGRLHPGDEL VYVDGIPVAG KTHRYVIDLM HHAARNGQVN
LTVRRKVLCG GEPCPENGRS PGSVSTHHSS PRSDYATYSN SNHAAPSSNA SPPEGFASHS
LQTSDVVIHR KENEGFGFVI ISSLNRPESG ATITVPHKIG RIIDGSPADR CAKLKVGDRI
LAVNGQSIIN MPHADIVKLI KDAGLSVTLR IIPQEELNSP TSAPSSEKQS PMAQQHSPLA
QQSPLAQPSP ATPNSPVAQP APPQPLQLQG HENSYRSEVK ARQDVKPDIR QPPFTDYRQP
PLDYRQPPGG DYSQPPPLDY RQHSPDTRQY PLSDYRQPQD FDYFTVDMEK GAKGFGFSIR
GGREYKMDLY VLRLAEDGPA IRNGRMRVGD QIIEINGEST RDMTHARAIE LIKSGGRRVR
LLLKRGTGQV PEYDEPHAWS AAAAAAPGLP EVGVSLEDIL SPFSPSHPAP PSDPSHQIGP
DPTWDIQREH DVRKPKELSA GGQKKQRLGE QRERSASPQR SARPRLEEVP GGQGRPEAGR
PASEAADGKE ALRGRREGLG AAGAREAEAK VGVRSGARPA ARPTGGGPAR KATMAPGPWK
VPGSDKLPGA LQPGASAAGR
//
