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Database: UniProt
Entry: G1SFD3_RABIT
LinkDB: G1SFD3_RABIT
Original site: G1SFD3_RABIT 
ID   G1SFD3_RABIT            Unreviewed;      1210 AA.
AC   G1SFD3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 2 {ECO:0000313|Ensembl:ENSOCUP00000001212.3};
GN   Name=MAGI2 {ECO:0000313|Ensembl:ENSOCUP00000001212.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001212.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000001212.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001212.3,
RC   ECO:0000313|Proteomes:UP000001811};
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:ENSOCUP00000001212.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001212.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   EMBL; AAGW02038579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02038588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1SFD3; -.
DR   Ensembl; ENSOCUT00000001407.4; ENSOCUP00000001212.3; ENSOCUG00000001407.4.
DR   eggNOG; KOG3209; Eukaryota.
DR   GeneTree; ENSGT00940000155057; -.
DR   HOGENOM; CLU_004562_1_0_1; -.
DR   TreeFam; TF316816; -.
DR   Proteomes; UP000001811; Chromosome 7.
DR   Bgee; ENSOCUG00000001407; Expressed in frontal cortex and 13 other cell types or tissues.
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; 4.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.30.42.10; -; 5.
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; PF16663; MAGI_u1; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00228; PDZ; 4.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 4.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50106; PDZ; 4.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          139..172
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          185..218
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          264..333
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          443..506
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          602..684
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          904..986
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..814
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  131334 MW;  256381BB27B4A776 CRC64;
     MELEKSGALL ESGTYEDNYY GTPKPPAEPA PLLLNVTDQI LPGATPSAEG KRKRNKSVSN
     MEKASVEPPE EEEEERPVVN GNGVVVTPES SEQEDKSAGA SGETPSQPYP APVYSQPEEL
     KEHMEDTKPT KPEESEDSDP LPDNWEMAYT EKGEVYFIDH NTKTTSWLDP RLAKKAKPPE
     ECKGNELPYG WEKIDDPIYG TYYVDHINRR TQFENPVLEA KRKLQQQHNM PHTELGPKPL
     QAPGFREKPL FTRDASQLKG TFLSTTLKKS NMGFGFTIIG GDEPDEFLQV KSVIPDGPAA
     QDGKMETGDV IVYINEVCVL GHTHADVVKL FQSVPIGQSV NLVLCRGYPL PFDPEDPANS
     LVPPLAIMER PPPVMVNGRH NYETYLEYIS RTSQSVPDIT DRPPQSLHSM PADGQLDGTY
     PPPVHDDNVS MASSGATQAE LMTLTIVKGA QGFGFTIADS PTGQRVKQIL DIQGCPGLCE
     GDLIVEINQQ NVQNLSHTEV VDILKDCPVG SETSLIIHRG GFFSPWKTPK PIPDRWENQG
     SPQTSLSAPA GPQNLPFPPA LHRSSFPDSA EAFDPRKPDP YELYEKSRAI YESRRPDYKE
     LDVHLRRMES GFGFRILGGD EPGQPILIGA VIAMGSADRD GRLHPGDELV YVDGIPVAGK
     THRYVIDLMH HAARNGQVNL TVRRKVLCGG EPCPENGRSP GSVSTHHSSP RSDYTTYANS
     NHAASSSNAS PPEGFASHSL QTSDVVIHRK ENEGFGFVII SSLNRPESGS TIKLNSPASA
     PSSEKQSPSA QQHSPSAQPS PATPNSPVAQ PAPPQPLQLQ GHESSYRSEV KARQDVKPDI
     RQPPFTDYRQ PPLDYRQPPG GDFQQPPPVE YRQPPLLDYR QHSPDTRQYP LSDYRQPQDF
     DYFTVDMEKG AKGFGFSIRG GREYKMDLYV LRLAEDGPAI RNGRMRVGDQ IIEINGESTR
     DMTHARAIEL IKSGGRRVRL LLKRGTGQVP EYDEPSAWSA AAAAAPGLPQ VGVSLEDILS
     PFSPSHPAPP SDPSLQIGPD PTWDIKREHD VRKPKELSAG GQKKQRLGEQ RERSASPQRA
     ARPRLEEAPG GQGRPEAGRP ASEARAPGPA AADAADATRA GGQEGPRAAA APEPGRREGP
     GAAAAFGGVG GVSAREAEAR AGARAGSRPG PRPPGVAPAR KASVAPGPWR VPGSDKLPGV
     LKPGASAAGR
//
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