AP2M1_RAT
ID AP2M1_RAT Reviewed; 435 AA.
AC P84092; P20172; P53679;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=AP-2 mu chain;
DE AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE AltName: Full=Adaptor-related protein complex 2 subunit mu;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Clathrin coat assembly protein AP50;
DE AltName: Full=Clathrin coat-associated protein AP50;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN Name=Ap2m1;
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].
RC TISSUE=Brain;
RX PubMed=3148444; DOI=10.1089/dna.1988.7.663;
RA Thurieau C., Brosius J., Burne C., Jolles P., Keen J.H., Mattaliano R.J.,
RA Chow E.P., Ramachandran K.L., Kirchhausen T.;
RT "Molecular cloning and complete amino acid sequence of AP50, an assembly
RT protein associated with clathrin-coated vesicles.";
RL DNA 7:663-669(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH EGFR AND TTGN1, AND MUTAGENESIS OF ASP-176 AND TRP-421.
RX PubMed=10228163; DOI=10.1093/emboj/18.9.2489;
RA Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.;
RT "Inhibition of the receptor-binding function of clathrin adaptor protein
RT AP-2 by dominant-negative mutant mu2 subunit and its effects on
RT endocytosis.";
RL EMBO J. 18:2489-2499(1999).
RN [4]
RP FUNCTION OF THE AP-2 COMPLEX, AND MUTAGENESIS OF THR-156.
RX PubMed=11516654; DOI=10.1016/s0960-9822(01)00240-8;
RA Olusanya O., Andrews P.D., Swedlow J.R., Smythe E.;
RT "Phosphorylation of threonine 156 of the mu2 subunit of the AP2 complex is
RT essential for endocytosis in vitro and in vivo.";
RL Curr. Biol. 11:896-900(2001).
RN [5]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in the
RT post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [6]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-435 IN COMPLEX WITH EGFR
RP INTERNALIZATION SIGNAL.
RX PubMed=9812899; DOI=10.1126/science.282.5392.1327;
RA Owen D.J., Evans P.R.;
RT "A structural explanation for the recognition of tyrosine-based endocytotic
RT signals.";
RL Science 282:1327-1332(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) OF 158-435 IN COMPLEX WITH SELP
RP INTERNALIZATION SIGNAL.
RX PubMed=11247301; DOI=10.1034/j.1600-0854.2001.020205.x;
RA Owen D.J., Setiadi H., Evans P.R., McEver R.P., Green S.A.;
RT "A third specificity-determining site in mu 2 adaptin for sequences
RT upstream of Yxx phi sorting motifs.";
RL Traffic 2:105-110(2001).
RN [9] {ECO:0007744|PDB:2VGL}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH AP2B1; AP2A2; AP2S1
RP AND INOSITOL HEXAKISPHOSPHATE.
RX PubMed=12086608; DOI=10.1016/s0092-8674(02)00735-3;
RA Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
RT "Molecular architecture and functional model of the endocytic AP2
RT complex.";
RL Cell 109:523-535(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 260-435 IN COMPLEX WITH EGFR
RP INTERNALIZATION SIGNAL.
RX PubMed=12121421; DOI=10.1034/j.1600-0854.2002.30808.x;
RA Boll W., Rapoport I., Brunner C., Modis Y., Prehn S., Kirchhausen T.;
RT "The mu2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and YppO
RT sorting signals at distinct sites.";
RL Traffic 3:590-600(2002).
RN [11] {ECO:0007744|PDB:2BP5}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH P2RX4 PEPTIDE, AND
RP FUNCTION.
RX PubMed=15985462; DOI=10.1242/jcs.02451;
RA Royle S.J., Qureshi O.S., Bobanovic L.K., Evans P.R., Owen D.J.,
RA Murrell-Lagnado R.D.;
RT "Non-canonical YXXGPhi endocytic motifs: recognition by AP2 and
RT preferential utilization in P2X4 receptors.";
RL J. Cell Sci. 118:3073-3080(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-435 IN COMPLEX WITH AP2A2;
RP AP2B1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
RX PubMed=19140243; DOI=10.1038/nature07422;
RA Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S.,
RA Owen D.J.;
RT "A structural explanation for the binding of endocytic dileucine motifs by
RT the AP2 complex.";
RL Nature 456:976-979(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 170-435 IN COMPLEX WITH DVL2,
RP FUNCTION, AND INTERACTION WITH DVL2.
RX PubMed=20947020; DOI=10.1016/j.str.2010.07.010;
RA Yu A., Xing Y., Harrison S.C., Kirchhausen T.;
RT "Structural analysis of the interaction between Dishevelled2 and clathrin
RT AP-2 adaptor, a critical step in noncanonical Wnt signaling.";
RL Structure 18:1311-1320(2010).
RN [14] {ECO:0007744|PDB:4UQI}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH AP2A2; AP2B1; AP2S1
RP AND INOSITOL HEXAKISPHOSPHATE.
RX PubMed=25061211; DOI=10.1126/science.1254836;
RA Kelly B.T., Graham S.C., Liska N., Dannhauser P.N., Honing S.,
RA Ungewickell E.J., Owen D.J.;
RT "Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-
RT activated switch.";
RL Science 345:459-463(2014).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2)
CC (PubMed:14745134, PubMed:15473838). Adaptor protein complexes function
CC in protein transport via transport vesicles in different membrane
CC traffic pathways (PubMed:14745134, PubMed:15473838). Adaptor protein
CC complexes are vesicle coat components and appear to be involved in
CC cargo selection and vesicle formation (PubMed:14745134,
CC PubMed:15473838). AP-2 is involved in clathrin-dependent endocytosis in
CC which cargo proteins are incorporated into vesicles surrounded by
CC clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion
CC with the early endosome (PubMed:14745134, PubMed:15473838). The
CC clathrin lattice serves as a mechanical scaffold but is itself unable
CC to bind directly to membrane components (PubMed:14745134,
CC PubMed:15473838). Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the lipid
CC and protein components of membranes are considered to be the major
CC clathrin adaptors contributing the CCV formation (PubMed:14745134,
CC PubMed:15473838). AP-2 also serves as a cargo receptor to selectively
CC sort the membrane proteins involved in receptor-mediated endocytosis
CC (PubMed:14745134, PubMed:15473838). AP-2 seems to play a role in the
CC recycling of synaptic vesicle membranes from the presynaptic surface
CC (By similarity). AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-
CC X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules (PubMed:15985462). AP-2 may also play a
CC role in maintaining normal post-endocytic trafficking through the ARF6-
CC regulated, non-clathrin pathway (By similarity). During long-term
CC potentiation in hippocampal neurons, AP-2 is responsible for the
CC endocytosis of ADAM10 (By similarity). The AP-2 mu (AP2M1) subunit
CC binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi
CC motifs (PubMed:15985462). The surface region interacting with to the Y-
CC X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible
CC through a conformational change following phosphorylation of AP-2 mu
CC subunit at Thr-156 in membrane-associated AP-2 (PubMed:15985462,
CC PubMed:11516654). The membrane-specific phosphorylation event appears
CC to involve assembled clathrin which activates the AP-2 mu kinase AAK1
CC (By similarity). Plays a role in endocytosis of frizzled family members
CC upon Wnt signaling (PubMed:20947020). {ECO:0000250|UniProtKB:Q96CW1,
CC ECO:0000269|PubMed:11516654, ECO:0000269|PubMed:14745134,
CC ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:15985462,
CC ECO:0000269|PubMed:20947020}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1) (PubMed:19140243). Interacts with
CC ATP6V1H and MEGF10 (By similarity). Interacts with EGFR and TTGN1
CC (PubMed:10228163, PubMed:9812899, PubMed:12121421). Interacts with F2R
CC (By similarity). Interacts with PIP5K1C; tyrosine phosphorylation of
CC PIP5K1C weakens the interaction (By similarity). Interacts with
CC KIAA0319; required for clathrin-mediated endocytosis of KIAA0319 (By
CC similarity). Interacts with DVL2 (via DEP domain) (PubMed:20947020).
CC Interacts with KCNQ1; mediates estrogen-induced internalization via
CC clathrin-coated vesicles (By similarity). Interacts with P2RX4 (via
CC internalization motif) (PubMed:15985462). Together with AP2A1 or AP2A2
CC and AP2B1, it interacts with ADAM10; this interaction facilitates
CC ADAM10 endocytosis from the plasma membrane during long-term
CC potentiation in hippocampal neurons (By similarity). Probably interacts
CC with ACE2 (via endocytic sorting signal motif); the interaction is
CC inhibited by ACE2 phosphorylation (By similarity). Interacts with
CC RALBP1; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P84091, ECO:0000250|UniProtKB:Q96CW1,
CC ECO:0000269|PubMed:10228163, ECO:0000269|PubMed:12121421,
CC ECO:0000269|PubMed:15985462, ECO:0000269|PubMed:19140243,
CC ECO:0000269|PubMed:20947020, ECO:0000269|PubMed:9812899}.
CC -!- INTERACTION:
CC P84092; P19491: Gria2; NbExp=2; IntAct=EBI-297693, EBI-77718;
CC P84092; P19814: Ttgn1; NbExp=4; IntAct=EBI-297693, EBI-541446;
CC P84092; P63010: AP2B1; Xeno; NbExp=4; IntAct=EBI-297693, EBI-432924;
CC P84092; Q60838: Dvl2; Xeno; NbExp=4; IntAct=EBI-297693, EBI-641940;
CC P84092; P17301: ITGA2; Xeno; NbExp=2; IntAct=EBI-297693, EBI-702960;
CC P84092; P13612: ITGA4; Xeno; NbExp=2; IntAct=EBI-297693, EBI-703044;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96CW1}.
CC Membrane, coated pit {ECO:0000250|UniProtKB:Q96CW1}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q96CW1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96CW1}. Note=AP-2 appears to be excluded from
CC internalizing CCVs and to disengage from sites of endocytosis seconds
CC before internalization of the nascent CCV.
CC {ECO:0000250|UniProtKB:P84091}.
CC -!- TISSUE SPECIFICITY: Detected in brain.
CC -!- PTM: Phosphorylation at Thr-156 increases the affinity of the AP-2
CC complex for cargo membrane proteins during the initial stages of
CC endocytosis. {ECO:0000250|UniProtKB:Q96CW1}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; M23674; AAA72731.1; -; mRNA.
DR EMBL; BC087724; AAH87724.1; -; mRNA.
DR PIR; A31596; A31596.
DR RefSeq; NP_446289.1; NM_053837.1.
DR PDB; 1BW8; X-ray; 2.65 A; A=122-435.
DR PDB; 1BXX; X-ray; 2.70 A; A=158-435.
DR PDB; 1HES; X-ray; 3.00 A; A=158-435.
DR PDB; 1I31; X-ray; 2.50 A; A=122-435.
DR PDB; 2BP5; X-ray; 2.80 A; M=1-435.
DR PDB; 2JKR; X-ray; 2.98 A; M/U=1-435.
DR PDB; 2JKT; X-ray; 3.40 A; M/U=1-435.
DR PDB; 2PR9; X-ray; 2.51 A; A=158-435.
DR PDB; 2VGL; X-ray; 2.59 A; M=1-435.
DR PDB; 2XA7; X-ray; 3.10 A; M=1-435.
DR PDB; 3H85; X-ray; 2.60 A; A=158-435.
DR PDB; 3ML6; X-ray; 3.50 A; A/B/C/D/E/F=170-435.
DR PDB; 4UQI; X-ray; 2.79 A; M=1-435.
DR PDB; 5C7Z; X-ray; 2.77 A; A=159-435.
DR PDB; 5FPI; X-ray; 2.77 A; A=1-435.
DR PDB; 5WRK; X-ray; 2.62 A; A=158-435.
DR PDB; 5WRL; X-ray; 3.10 A; A=158-435.
DR PDB; 5WRM; X-ray; 2.60 A; A=158-435.
DR PDB; 6QH5; X-ray; 2.56 A; M/N=1-435.
DR PDB; 6QH6; X-ray; 5.00 A; N=1-435.
DR PDB; 6RH6; NMR; -; B=149-163.
DR PDB; 6YAE; EM; 3.90 A; M=1-435.
DR PDB; 6YAF; EM; 9.10 A; M=1-435.
DR PDB; 6YAH; EM; 10.20 A; M=1-435.
DR PDBsum; 1BW8; -.
DR PDBsum; 1BXX; -.
DR PDBsum; 1HES; -.
DR PDBsum; 1I31; -.
DR PDBsum; 2BP5; -.
DR PDBsum; 2JKR; -.
DR PDBsum; 2JKT; -.
DR PDBsum; 2PR9; -.
DR PDBsum; 2VGL; -.
DR PDBsum; 2XA7; -.
DR PDBsum; 3H85; -.
DR PDBsum; 3ML6; -.
DR PDBsum; 4UQI; -.
DR PDBsum; 5C7Z; -.
DR PDBsum; 5FPI; -.
DR PDBsum; 5WRK; -.
DR PDBsum; 5WRL; -.
DR PDBsum; 5WRM; -.
DR PDBsum; 6QH5; -.
DR PDBsum; 6QH6; -.
DR PDBsum; 6RH6; -.
DR PDBsum; 6YAE; -.
DR PDBsum; 6YAF; -.
DR PDBsum; 6YAH; -.
DR AlphaFoldDB; P84092; -.
DR SMR; P84092; -.
DR BioGRID; 250498; 11.
DR CORUM; P84092; -.
DR DIP; DIP-29761N; -.
DR IntAct; P84092; 23.
DR MINT; P84092; -.
DR STRING; 10116.ENSRNOP00000054900; -.
DR iPTMnet; P84092; -.
DR PhosphoSitePlus; P84092; -.
DR SwissPalm; P84092; -.
DR jPOST; P84092; -.
DR PaxDb; P84092; -.
DR PRIDE; P84092; -.
DR Ensembl; ENSRNOT00000088821; ENSRNOP00000070202; ENSRNOG00000001709.
DR GeneID; 116563; -.
DR KEGG; rno:116563; -.
DR CTD; 1173; -.
DR RGD; 620135; Ap2m1.
DR eggNOG; KOG0938; Eukaryota.
DR GeneTree; ENSGT00940000159223; -.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; P84092; -.
DR OMA; VWKIPRI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; P84092; -.
DR TreeFam; TF300722; -.
DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-RNO-8964038; LDL clearance.
DR EvolutionaryTrace; P84092; -.
DR PRO; PR:P84092; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001709; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P84092; baseline and differential.
DR Genevisible; P84092; RN.
DR GO; GO:0030122; C:AP-2 adaptor complex; IDA:CAFA.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
DR GO; GO:0005048; F:signal sequence binding; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:RGD.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0097494; P:regulation of vesicle size; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR DisProt; DP00455; -.
DR IDEAL; IID50122; -.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coated pit; Endocytosis; Lipid-binding;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..435
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000193776"
FT DOMAIN 170..434
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT BINDING 341
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT BINDING 345
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT BINDING 354
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CW1"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96CW1"
FT MUTAGEN 156
FT /note="T->A: Inhibits endocytosis by AP-2; no effect on
FT membrane association of AP-2."
FT /evidence="ECO:0000269|PubMed:11516654"
FT MUTAGEN 176
FT /note="D->A: Abolishes interaction with TTGN1 and EGFR."
FT /evidence="ECO:0000269|PubMed:10228163"
FT MUTAGEN 421
FT /note="W->A: Abolishes interaction with TTGN1 and EGFR."
FT /evidence="ECO:0000269|PubMed:10228163"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4UQI"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:2XA7"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2XA7"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 191..205
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2VGL"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5WRK"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2JKR"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1I31"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:5WRM"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:1I31"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:1I31"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 350..361
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:1I31"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2XA7"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:1I31"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:1I31"
FT STRAND 419..433
FT /evidence="ECO:0007829|PDB:1I31"
SQ SEQUENCE 435 AA; 49655 MW; 82803219BA279954 CRC64;
MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
WVRYIGRSGI YETRC
