ID G1PQF0_MYOLU Unreviewed; 1101 AA.
AC G1PQF0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2 {ECO:0000313|Ensembl:ENSMLUP00000013294.2};
GN Name=MAGI2 {ECO:0000313|Ensembl:ENSMLUP00000013294.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013294.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013294.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000013294.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAPE02009875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02009882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PQF0; -.
DR STRING; 59463.ENSMLUP00000013294; -.
DR Ensembl; ENSMLUT00000014610.2; ENSMLUP00000013294.2; ENSMLUG00000014602.2.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000155057; -.
DR HOGENOM; CLU_004562_2_0_1; -.
DR InParanoid; G1PQF0; -.
DR OMA; XYRSEVK; -.
DR TreeFam; TF316816; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0070699; F:type II activin receptor binding; ISS:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 5.
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; PF16663; MAGI_u1; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 125..158
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 171..204
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 249..318
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 428..491
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 601..683
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 743..833
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 963..1045
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 29..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 121363 MW; 87371C41B92107F0 CRC64;
FADNYYGTPK PPAEPAPLLL NVTDQILPGA TASAEGKRKR NKSVSNMEKA SIEPPEEEEE
ERPVVNGNGV VVTPESSEHE DKSAGASGET PSQPYPAPVY SQPEELKEQM DDAKPTKPEE
NEESDPLPDN WEMAYTEKGE VYFIDHNTKT TSWLDPRLAK KAKPPEECKE NELPYGWEKI
DDPIYGTYYV DHINRRTQFE NPVLEAKRKL QQHNMPHTDL GTKPLQAPGF REKPLFTRDA
SQLKGTFLST TLKKSNMGFG FTIIGGDEPD EFLQVKSVIP DGPAAQDGKM ETGDVIVYIN
EVCVLGHTHA DVVKLFQSVP IGQSVSLVLC RGYPLPFDPE DPANSLVPPL AIMERPPPVM
VNGRHNYETY LEYISRTSQS VPDITDRPPH SLHSMPADGQ LDGTYPPPVH DDNVSMASSG
ATQAELMTLT IVKGAQGFGF TIADSPTGQR VKQILDIQGC PGLCEGDLIV EINQQNVQNL
SHTEVVDILK DCPIGSETSL IIHRGGFFSP WKSPKPIMDR WENQGSPQTS LSAPAIPQNL
PFPPALHRSS FPDSTEAFDP RKPDPYELYE KSRAIYESRQ QVPPRTSFRM DSSGPDYKEL
DVHLRRMESG FGFRILGGDE PGQPILIGAV IAMGSADRDG RLHPGDELVY VDGIPVAGKT
HRYVIDLMHH AARNGQVNLT VRRKVLCGGE PCPENGRSPG SVSTHHSSPR SDYATYTNSN
HAAPSGSASP PEGFASHSLQ TSDVVIHRKE NEGFGFVIIS SLNRPESGST ITVPHKIGRI
IDGSPADRCA KLKVGDRILA VNGQSIINMP HADIVKLIKD AGLSVTLRII PQEELNSPAS
APSSEKQSPM AQQHSPLAQQ SPLAQPSPAT PNSPVTQPAP PQPLQLQGHE NSYRSEVKAR
QDVKPDIRQP PFTDYRQPPL DYRQPPGGDY QQPPPLDYRQ HSPDTRQYPL SDYRQPQDFD
YFTVDMEKGA KGFGFSIRGG REYKMDLYVL RLAEDGPAIR NGRMRVGDQI IEINGESTRD
MTHARAIELI KSGGRRVRLL LKRGTGQVPE YGMVPSSLSM CMKSDKHGSP YFYLLGHPKD
TVYSNKTPLA IPVFPSLLCG N
//
