MAGI2_RAT
ID MAGI2_RAT Reviewed; 1277 AA.
AC O88382; Q9R271;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;
DE AltName: Full=Atrophin-1-interacting protein 1;
DE Short=AIP-1;
DE AltName: Full=Membrane-associated guanylate kinase inverted 2;
DE Short=MAGI-2;
DE AltName: Full=Synaptic-scaffolding molecule;
DE Short=S-SCAM;
GN Name=Magi2; Synonyms=Acvrinp1, Aip1, Sscam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH DLGAP1; NLGN1 AND GRIN2A.
RX PubMed=9694864; DOI=10.1074/jbc.273.33.21105;
RA Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M.,
RA Toyoda A., Suedhof T.C., Takai Y.;
RT "A novel multiple PDZ domain-containing molecule interacting with N-methyl-
RT d-aspartate receptors and neuronal cell adhesion proteins.";
RL J. Biol. Chem. 273:21105-21110(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORM
RP 3).
RX PubMed=10644767; DOI=10.1074/jbc.275.4.2966;
RA Hirao K., Hata Y., Yao I., Deguchi M., Kawabe H., Mizoguchi A., Takai Y.;
RT "Three isoforms of synaptic scaffolding molecule and their
RT characterization: multimerization between the isoforms and their
RT interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95-associated
RT protein.";
RL J. Biol. Chem. 275:2966-2972(2000).
RN [3]
RP INTERACTION WITH CTNND2.
RX PubMed=10080919; DOI=10.1006/bbrc.1999.0364;
RA Ide N., Hata Y., Deguchi M., Hirao K., Yao I., Takai Y.;
RT "Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat
RT protein/delta-catenin.";
RL Biochem. Biophys. Res. Commun. 256:456-461(1999).
RN [4]
RP INTERACTION WITH RAPGEF2.
RX PubMed=10548487; DOI=10.1006/bbrc.1999.1619;
RA Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T., Mizoguchi A.,
RA Takai Y.;
RT "nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein
RT that interacts with synaptic scaffolding molecule (S-SCAM).";
RL Biochem. Biophys. Res. Commun. 265:38-44(1999).
RN [5]
RP INTERACTION WITH MAGUIN-1.
RX PubMed=10207009; DOI=10.1074/jbc.274.17.11889;
RA Yao I., Hata Y., Ide N., Hirao K., Deguchi M., Nishioka H., Mizoguchi A.,
RA Takai Y.;
RT "MAGUIN, a novel neuronal membrane-associated guanylate kinase-interacting
RT protein.";
RL J. Biol. Chem. 274:11889-11896(1999).
RN [6]
RP INTERACTION WITH GRID2.
RX PubMed=12589829; DOI=10.1016/s0006-291x(03)00070-6;
RA Yap C.C., Muto Y., Kishida H., Hashikawa T., Yano R.;
RT "PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2
RT protein.";
RL Biochem. Biophys. Res. Commun. 301:1122-1128(2003).
RN [7]
RP INTERACTION WITH PTEN.
RX PubMed=15951562; DOI=10.1074/jbc.m504761200;
RA Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA Antonarakis S.E., Pulido R.;
RT "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT stability and phosphorylation by microtubule-associated serine/threonine
RT kinases.";
RL J. Biol. Chem. 280:28936-28943(2005).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH ACTN4; CASK; IQGAP1; NPHS1; SPTAN1 AND
RP SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Renal glomerulus;
RX PubMed=15994232; DOI=10.1073/pnas.0504166102;
RA Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G.;
RT "Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and
RT alpha-actinin are components of the nephrin multiprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005).
RN [9]
RP INTERACTION WITH DDN.
RX PubMed=16751601; DOI=10.1093/jb/mvj105;
RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
RT "CIN85 is localized at synapses and forms a complex with S-SCAM via
RT dendrin.";
RL J. Biochem. 139:931-939(2006).
RN [10]
RP INTERACTION WITH DDN.
RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x;
RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.;
RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
RT transport and synaptic anchoring.";
RL J. Neurochem. 96:1659-1666(2006).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH KIDINS220; RAPGEF2 AND NTRK1,
RP INTERACTION WITH RAPGEF2 AND KIDINS220, AND SUBCELLULAR LOCATION.
RX PubMed=17724123; DOI=10.1083/jcb.200610073;
RA Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.;
RT "Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes,
RT leading to sustained activation of Rap1 and ERK and neurite outgrowth.";
RL J. Cell Biol. 178:843-860(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686; SER-884 AND SER-885, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH IGSF9B AND NLGN2.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
CC -!- FUNCTION: Seems to act as scaffold molecule at synaptic junctions by
CC assembling neurotransmitter receptors and cell adhesion proteins
CC (PubMed:9694864). Plays a role in nerve growth factor (NGF)-induced
CC recruitment of RAPGEF2 to late endosomes and neurite outgrowth
CC (PubMed:17724123). May play a role in regulating activin-mediated
CC signaling in neuronal cells (By similarity). Enhances the ability of
CC PTEN to suppress AKT1 activation (By similarity). Plays a role in
CC receptor-mediated clathrin-dependent endocytosis which is required for
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q86UL8,
CC ECO:0000250|UniProtKB:Q9WVQ1, ECO:0000269|PubMed:17724123,
CC ECO:0000269|PubMed:9694864}.
CC -!- SUBUNIT: Interacts (via its WW domains) with DRPLA (By similarity).
CC Interacts with CTNNB1, ACVR2A, SMAD2 and SMAD3 (By similarity). Part of
CC a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity).
CC May interact with HTR2A and IGSF9 (By similarity). Interacts with HTR4
CC (By similarity). Interacts (via guanylate kinase domain) with DLGAP1
CC (PubMed:9694864). Interacts (via PDZ domains) with GRIN2A, GRID2 and
CC NLGN1 (PubMed:9694864, PubMed:12589829). Interacts with CTNND2
CC (PubMed:10080919). Interacts with MAGUIN-1 (PubMed:10207009). Interacts
CC (via its second PDZ domain) with PTEN (via unphosphorylated C-
CC terminus); this interaction diminishes the degradation rate of PTEN
CC (PubMed:15951562). Found in a complex, at least composed of KIDINS220,
CC MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late
CC endosomes in a NGF-dependent manner (PubMed:17724123). Interacts with
CC RAPGEF2; the interaction occurs before or after nerve growth factor
CC (NGF) stimulation (PubMed:10548487). Isoform 1 interacts (via PDZ
CC domain) with KIDINS220 isoform 2 (via C-terminal domain)
CC (PubMed:17724123). Interacts with DDN (PubMed:16751601,
CC PubMed:16464232). Identified in a complex with ACTN4, CASK, IQGAP1,
CC NPHS1, SPTAN1 and SPTBN1 (PubMed:15994232). Interacts with DLL1 (By
CC similarity). Found in a complex with IGSF9B and NLGN2; the interaction
CC with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains, while the
CC interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2 domains
CC (PubMed:23751499). Interacts (via PDZ 6 domain) with USH1G (via SAM
CC domain); the interaction is triggered by phosphorylation of USH1G by
CC CK2 and negatively regulates MAGI2-mediated endocytosis (By
CC similarity). {ECO:0000250|UniProtKB:Q9WVQ1,
CC ECO:0000269|PubMed:10080919, ECO:0000269|PubMed:10207009,
CC ECO:0000269|PubMed:10548487, ECO:0000269|PubMed:12589829,
CC ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:15994232,
CC ECO:0000269|PubMed:16464232, ECO:0000269|PubMed:16751601,
CC ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:23751499,
CC ECO:0000269|PubMed:9694864}.
CC -!- INTERACTION:
CC O88382; P97836: Dlgap1; NbExp=3; IntAct=EBI-696179, EBI-80901;
CC O88382; Q8R4T5: Tamalin; NbExp=5; IntAct=EBI-696179, EBI-7361884;
CC O88382; P34998: CRHR1; Xeno; NbExp=2; IntAct=EBI-696179, EBI-3870393;
CC O88382; O94850: DDN; Xeno; NbExp=3; IntAct=EBI-696179, EBI-5240523;
CC O88382; P60484: PTEN; Xeno; NbExp=3; IntAct=EBI-696179, EBI-696162;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Synapse, synaptosome.
CC Cell membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q9WVQ1}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q9WVQ1}. Note=Membrane-associated
CC in synaptosomes. Localized diffusely in the cytoplasm before nerve
CC growth factor (NGF) stimulation. Recruited to late endosomes after NGF
CC stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=alpha;
CC IsoId=O88382-1; Sequence=Displayed;
CC Name=2; Synonyms=beta;
CC IsoId=O88382-2; Sequence=VSP_008438;
CC Name=3; Synonyms=gamma;
CC IsoId=O88382-3; Sequence=VSP_008439;
CC -!- TISSUE SPECIFICITY: Expressed in the foot process layer of podocytes of
CC the kidney glomeruli but not in tubules (at protein level). Expressed
CC in the brain. {ECO:0000269|PubMed:15994232,
CC ECO:0000269|PubMed:9694864}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the late capillary loop stage of
CC glomerulogenesis. First detected in junctional complexes in podocytes
CC after their migration to the base of cells. Up-regulated upon foot
CC process differentiation. {ECO:0000269|PubMed:15994232}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AF034863; AAC31124.1; -; mRNA.
DR EMBL; AF130819; AAD31015.1; -; mRNA.
DR PIR; T14152; T14152.
DR RefSeq; NP_446073.1; NM_053621.1. [O88382-1]
DR AlphaFoldDB; O88382; -.
DR SMR; O88382; -.
DR BioGRID; 250241; 7.
DR CORUM; O88382; -.
DR IntAct; O88382; 28.
DR MINT; O88382; -.
DR STRING; 10116.ENSRNOP00000059912; -.
DR iPTMnet; O88382; -.
DR PhosphoSitePlus; O88382; -.
DR PaxDb; O88382; -.
DR PRIDE; O88382; -.
DR GeneID; 113970; -.
DR KEGG; rno:113970; -.
DR CTD; 9863; -.
DR RGD; 621855; Magi2.
DR eggNOG; KOG3209; Eukaryota.
DR InParanoid; O88382; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; O88382; -.
DR PRO; PR:O88382; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0070697; F:activin receptor binding; ISO:RGD.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0098879; F:structural constituent of postsynaptic specialization; IDA:SynGO.
DR GO; GO:0070699; F:type II activin receptor binding; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IC: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; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:UniProtKB.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISO:RGD.
DR GO; GO:0072015; P:podocyte development; IEP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP: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:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0043113; P:receptor clustering; IDA:RGD.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030036; MAGI2.
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:SF27; PTHR10316:SF27; 1.
DR Pfam; PF00625; Guanylate_kin; 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; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
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 Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..1277
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 2"
FT /id="PRO_0000094588"
FT DOMAIN 17..101
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 109..283
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 302..335
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 348..381
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 426..510
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 605..683
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 778..860
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 920..1010
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1141..1223
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 205..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..381
FT /note="Interaction with DDN"
FT /evidence="ECO:0000250"
FT REGION 556..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 827
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVQ1"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008439"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10644767"
FT /id="VSP_008438"
FT CONFLICT 645
FT /note="L -> F (in Ref. 2; AAD31015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1277 AA; 141072 MW; E1A435FF35549DF9 CRC64;
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED
NYYGTPKPPA EPAPLLLNVT DQILPGATPS AEGKRKRNKS VTNMEKASIE PPEEEEEERP
VVNGNGVVIT PESSEHEDKS AGASGETPSQ PYPAPVYSQP EELKDQMDDT KSTKPEENED
SDPLPDNWEM AYTEKGEVYF IDHNTKTTSW LDPRLAKKAK PAEECKENEL PYGWEKIDDP
IYGTYYVDHI NRRTQFENPV LEAKRKLQQH NMPHTELGTK PLQAPGFREK PLFTRDASQL
KGTFLSTTLK KSNMGFGFTI IGGDEPDEFL QVKSVIPDGP AAQDGKMETG DVIVYINEVC
VLGHTHADVV KLFQSVPIGQ SVNLVLCRGY PLPFDPEDPA NSMVPPLAIM ERPPPVMVNG
RHNYETYLEY ISRTSQSVPD ITDRPPHSLH SMPADGQLDG TYPPPVHDDN VSVASSGATQ
AELMTLTIVK GAKGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHT
EVVDILKDCP VGSETSLIIH RGGFFSPWKT PKPMVDRWEN QGSPQTSLSA PAVPQSLPFP
PALHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRQQVP PRTSFRMDSS GPDYKELDVH
LRRMESGFGF RILGGDEPGQ PILIGAVIAM GSADRDGRLH PGDELVYVDG IPVAGKTHRY
VIDLMHHAAR NGQVNLTVRR KVLCGGEPCP ENGRSPGSVS THHSSPRSDY ATYANSNHAA
PSNNASPPEG FASHSLQTSD VIIHRKENEG FGFVIISSLN RPESGATITV PHKIGRIIDG
SPADRCAKLK VGDRILAVNG QSIINMPHAD IVKLIKDAGL SVTLRIIPQE ELNNPTSAPS
SEKQSPMAQQ HSPLAQQHSP LAQPSPATPN SPVAQPAPPQ PLQLQGHENS YRSEVKARQD
VKPDIRQPPF TDYRQPPLDY RQPPGGDYSQ PSPLDYRQHS PDTRQYPLSD YRQPQDFDYF
TVDMEKGAKG FGFSIRGGRE YKMDLYVLRL AEDGPAIRNG RMRVGDQIIE INGESTRDMT
HARAIELIKS GGRRVRLLLK RGTGQVPEYG MVPSSLSMCM KSDKHGSPYF YLLGHPKDTT
NPTPGALPLP PPQACRK
