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AP-2 complex subunit mu (AP-2 mu chain) (Adaptor protein complex AP-2 subunit mu) (Adaptor-related protein complex 2 subunit mu) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (Mu2-adaptin) (Plasma membrane adaptor AP-2 50 kDa protein)

 AP2M1_RAT               Reviewed;         435 AA.
P84092; P20172; P53679;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
05-JUL-2017, entry version 125.
RecName: Full=AP-2 complex subunit mu;
AltName: Full=AP-2 mu chain;
AltName: Full=Adaptor protein complex AP-2 subunit mu;
AltName: Full=Adaptor-related protein complex 2 subunit mu;
AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
AltName: Full=Clathrin coat assembly protein AP50;
AltName: Full=Clathrin coat-associated protein AP50;
AltName: Full=Mu2-adaptin;
AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
Name=Ap2m1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3148444; DOI=10.1089/dna.1988.7.663;
Thurieau C., Brosius J., Burne C., Jolles P., Keen J.H.,
Mattaliano R.J., Chow E.P., Ramachandran K.L., Kirchhausen T.;
"Molecular cloning and complete amino acid sequence of AP50, an
assembly protein associated with clathrin-coated vesicles.";
DNA 7:663-669(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH EGFR AND TTGN1, AND MUTAGENESIS OF ASP-176 AND
TRP-421.
PubMed=10228163; DOI=10.1093/emboj/18.9.2489;
Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.;
"Inhibition of the receptor-binding function of clathrin adaptor
protein AP-2 by dominant-negative mutant mu2 subunit and its effects
on endocytosis.";
EMBO J. 18:2489-2499(1999).
[4]
FUNCTION OF THE AP-2 COMPLEX, AND MUTAGENESIS OF THR-156.
PubMed=11516654; DOI=10.1016/S0960-9822(01)00240-8;
Olusanya O., Andrews P.D., Swedlow J.R., Smythe E.;
"Phosphorylation of threonine 156 of the mu2 subunit of the AP2
complex is essential for endocytosis in vitro and in vivo.";
Curr. Biol. 11:896-900(2001).
[5]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=14745134; DOI=10.1247/csf.28.419;
Nakatsu F., Ohno H.;
"Adaptor protein complexes as the key regulators of protein sorting in
the post-Golgi network.";
Cell Struct. Funct. 28:419-429(2003).
[6]
FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
Owen D.J., Collins B.M., Evans P.R.;
"Adaptors for clathrin coats: structure and function.";
Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 159-435 IN COMPLEX WITH EGFR
INTERNALIZATION SIGNAL.
PubMed=9812899; DOI=10.1126/science.282.5392.1327;
Owen D.J., Evans P.R.;
"A structural explanation for the recognition of tyrosine-based
endocytotic signals.";
Science 282:1327-1332(1998).
[8]
X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) OF 158-435 IN COMPLEX WITH SELP
INTERNALIZATION SIGNAL.
PubMed=11247301; DOI=10.1034/j.1600-0854.2001.020205.x;
Owen D.J., Setiadi H., Evans P.R., McEver R.P., Green S.A.;
"A third specificity-determining site in mu 2 adaptin for sequences
upstream of Yxx phi sorting motifs.";
Traffic 2:105-110(2001).
[9]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH AP2B1; AP2A2;
AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
PubMed=12086608; DOI=10.1016/S0092-8674(02)00735-3;
Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
"Molecular architecture and functional model of the endocytic AP2
complex.";
Cell 109:523-535(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 260-435 IN COMPLEX WITH EGFR
INTERNALIZATION SIGNAL.
PubMed=12121421; DOI=10.1034/j.1600-0854.2002.30808.x;
Boll W., Rapoport I., Brunner C., Modis Y., Prehn S., Kirchhausen T.;
"The mu2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and YppO
sorting signals at distinct sites.";
Traffic 3:590-600(2002).
[11]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-435 IN COMPLEX WITH AP2A2;
AP2B1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
PubMed=19140243; DOI=10.1038/nature07422;
Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R.,
Hoening S., Owen D.J.;
"A structural explanation for the binding of endocytic dileucine
motifs by the AP2 complex.";
Nature 456:976-979(2008).
[12]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 170-435 IN COMPLEX WITH DVL2,
FUNCTION, AND INTERACTION WITH DVL2.
PubMed=20947020; DOI=10.1016/j.str.2010.07.010;
Yu A., Xing Y., Harrison S.C., Kirchhausen T.;
"Structural analysis of the interaction between Dishevelled2 and
clathrin AP-2 adaptor, a critical step in noncanonical Wnt
signaling.";
Structure 18:1311-1320(2010).
-!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
Adaptor protein complexes function in protein transport via
transport vesicles in different membrane traffic pathways. Adaptor
protein complexes are vesicle coat components and appear to be
involved in cargo selection and vesicle formation. AP-2 is
involved in clathrin-dependent endocytosis in which cargo proteins
are incorporated into vesicles surrounded by clathrin (clathrin-
coated vesicles, CCVs) which are destined for fusion with the
early endosome. The clathrin lattice serves as a mechanical
scaffold but is itself unable to bind directly to membrane
components. Clathrin-associated adaptor protein (AP) complexes
which can bind directly to both the clathrin lattice and to the
lipid and protein components of membranes are considered to be the
major clathrin adaptors contributing the CCV formation. AP-2 also
serves as a cargo receptor to selectively sort the membrane
proteins involved in receptor-mediated endocytosis. AP-2 seems to
play a role in the recycling of synaptic vesicle membranes from
the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
cytosolic tails of transmembrane cargo molecules. AP-2 may also
play a role in maintaining normal post-endocytic trafficking
through the ARF6-regulated, non-clathrin pathway. The AP-2 mu
subunit binds to transmembrane cargo proteins; it recognizes the
Y-X-X-Phi motifs. The surface region interacting with to the Y-X-
X-Phi motif is inaccessible in cytosolic AP-2, but becomes
accessible through a conformational change following
phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-
associated AP-2. The membrane-specific phosphorylation event
appears to involve assembled clathrin which activates the AP-2 mu
kinase AAK1 (By similarity). Plays a role in endocytosis of
frizzled family members upon Wnt signaling. {ECO:0000250,
ECO:0000269|PubMed:11516654, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:20947020}.
-!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
with ATP6V1H and MEGF10. Interacts with EGFR and TTGN1. Interacts
with F2R. Interacts with PIP5K1C isoform 1; tyrosine
phosphorylation of PIP5K1C weakens the interaction (By
similarity). Interacts with KIAA0319; required for clathrin-
mediated endocytosis of KIAA0319 (By similarity). Interacts with
DVL2 (via DEP domain). Interacts with KCNQ1; mediates estrogen-
induced internalization via clathrin-coated vesicles (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96CW1,
ECO:0000269|PubMed:10228163, ECO:0000269|PubMed:11247301,
ECO:0000269|PubMed:12086608, ECO:0000269|PubMed:12121421,
ECO:0000269|PubMed:19140243, ECO:0000269|PubMed:20947020,
ECO:0000269|PubMed:9812899}.
-!- INTERACTION:
P63010:AP2B1 (xeno); NbExp=2; IntAct=EBI-297693, EBI-432924;
P19814:Ttgn1; NbExp=4; IntAct=EBI-297693, EBI-541446;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane,
coated pit {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears
to be excluded from internalizing CCVs and to disengage from sites
of endocytosis seconds before internalization of the nascent CCV.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in brain.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. {ECO:0000305}.
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EMBL; M23674; AAA72731.1; -; mRNA.
EMBL; BC087724; AAH87724.1; -; mRNA.
PIR; A31596; A31596.
RefSeq; NP_446289.1; NM_053837.1.
UniGene; Rn.3172; -.
PDB; 1BW8; X-ray; 2.65 A; A=122-435.
PDB; 1BXX; X-ray; 2.70 A; A=158-435.
PDB; 1HES; X-ray; 3.00 A; A=158-435.
PDB; 1I31; X-ray; 2.50 A; A=122-435.
PDB; 2BP5; X-ray; 2.80 A; M=1-435.
PDB; 2JKR; X-ray; 2.98 A; M/U=1-435.
PDB; 2JKT; X-ray; 3.40 A; M/U=1-435.
PDB; 2PR9; X-ray; 2.51 A; A=158-435.
PDB; 2VGL; X-ray; 2.59 A; M=1-435.
PDB; 2XA7; X-ray; 3.10 A; M=1-435.
PDB; 3H85; X-ray; 2.60 A; A=158-435.
PDB; 3ML6; X-ray; 3.50 A; A/B/C/D/E/F=170-435.
PDB; 4UQI; X-ray; 2.79 A; M=1-435.
PDB; 5C7Z; X-ray; 2.77 A; A=159-435.
PDB; 5FPI; X-ray; 2.77 A; A=1-435.
PDBsum; 1BW8; -.
PDBsum; 1BXX; -.
PDBsum; 1HES; -.
PDBsum; 1I31; -.
PDBsum; 2BP5; -.
PDBsum; 2JKR; -.
PDBsum; 2JKT; -.
PDBsum; 2PR9; -.
PDBsum; 2VGL; -.
PDBsum; 2XA7; -.
PDBsum; 3H85; -.
PDBsum; 3ML6; -.
PDBsum; 4UQI; -.
PDBsum; 5C7Z; -.
PDBsum; 5FPI; -.
DisProt; DP00455; -.
ProteinModelPortal; P84092; -.
SMR; P84092; -.
BioGrid; 250498; 6.
DIP; DIP-29761N; -.
IntAct; P84092; 9.
MINT; MINT-122557; -.
STRING; 10116.ENSRNOP00000054900; -.
SwissPalm; P84092; -.
PaxDb; P84092; -.
PRIDE; P84092; -.
Ensembl; ENSRNOT00000088821; ENSRNOP00000070202; ENSRNOG00000001709.
GeneID; 116563; -.
KEGG; rno:116563; -.
CTD; 1173; -.
RGD; 620135; Ap2m1.
eggNOG; KOG0938; Eukaryota.
eggNOG; ENOG410XPFS; LUCA.
GeneTree; ENSGT00530000062779; -.
HOGENOM; HOG000173246; -.
HOVERGEN; HBG050516; -.
InParanoid; P84092; -.
KO; K11826; -.
OMA; SWRKADV; -.
PhylomeDB; P84092; -.
TreeFam; TF300722; -.
Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
Reactome; R-RNO-190873; Gap junction degradation.
Reactome; R-RNO-196025; Formation of annular gap junctions.
Reactome; R-RNO-2132295; MHC class II antigen presentation.
Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
Reactome; R-RNO-8964038; LDL clearance.
EvolutionaryTrace; P84092; -.
PRO; PR:P84092; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001709; -.
ExpressionAtlas; P84092; baseline and differential.
Genevisible; P84092; RN.
GO; GO:0030122; C:AP-2 adaptor complex; IDA:CAFA.
GO; GO:0030125; C:clathrin vesicle coat; TAS:RGD.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0030133; C:transport vesicle; TAS:RGD.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
GO; GO:0005048; F:signal sequence binding; IDA:BHF-UCL.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IMP:SynGO.
GO; GO:0016192; P:vesicle-mediated transport; TAS:RGD.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR001392; Clathrin_mu.
InterPro; IPR018240; Clathrin_mu_CS.
InterPro; IPR011012; Longin-like_dom.
InterPro; IPR028565; MHD.
Pfam; PF00928; Adap_comp_sub; 1.
Pfam; PF01217; Clat_adaptor_s; 1.
PIRSF; PIRSF005992; Clathrin_mu; 1.
PRINTS; PR00314; CLATHRINADPT.
SUPFAM; SSF49447; SSF49447; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
PROSITE; PS51072; MHD; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Coated pit; Complete proteome;
Endocytosis; Lipid-binding; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Transport.
CHAIN 1 435 AP-2 complex subunit mu.
/FTId=PRO_0000193776.
DOMAIN 170 434 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
BINDING 341 341 Phosphatidylinositol lipid headgroup.
BINDING 343 343 Phosphatidylinositol lipid headgroup.
BINDING 345 345 Phosphatidylinositol lipid headgroup.
BINDING 354 354 Phosphatidylinositol lipid headgroup.
BINDING 356 356 Phosphatidylinositol lipid headgroup.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:Q96CW1}.
MOD_RES 156 156 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96CW1}.
MUTAGEN 156 156 T->A: Inhibits endocytosis by AP-2; no
effect on membrane association of AP-2.
{ECO:0000269|PubMed:11516654}.
MUTAGEN 176 176 D->A: Abolishes interaction with TTGN1
and EGFR. {ECO:0000269|PubMed:10228163}.
MUTAGEN 421 421 W->A: Abolishes interaction with TTGN1
and EGFR. {ECO:0000269|PubMed:10228163}.
STRAND 4 8 {ECO:0000244|PDB:2VGL}.
STRAND 14 19 {ECO:0000244|PDB:2VGL}.
STRAND 21 23 {ECO:0000244|PDB:2VGL}.
HELIX 26 35 {ECO:0000244|PDB:2VGL}.
TURN 36 38 {ECO:0000244|PDB:2VGL}.
STRAND 40 42 {ECO:0000244|PDB:4UQI}.
STRAND 46 50 {ECO:0000244|PDB:2VGL}.
STRAND 53 60 {ECO:0000244|PDB:2VGL}.
STRAND 63 71 {ECO:0000244|PDB:2VGL}.
HELIX 75 93 {ECO:0000244|PDB:2VGL}.
HELIX 98 103 {ECO:0000244|PDB:2VGL}.
HELIX 105 115 {ECO:0000244|PDB:2VGL}.
HELIX 126 129 {ECO:0000244|PDB:2VGL}.
HELIX 130 132 {ECO:0000244|PDB:2VGL}.
HELIX 145 156 {ECO:0000244|PDB:2XA7}.
TURN 160 162 {ECO:0000244|PDB:2XA7}.
STRAND 172 185 {ECO:0000244|PDB:1I31}.
STRAND 191 205 {ECO:0000244|PDB:1I31}.
STRAND 207 209 {ECO:0000244|PDB:1I31}.
STRAND 211 217 {ECO:0000244|PDB:1I31}.
STRAND 218 220 {ECO:0000244|PDB:2VGL}.
STRAND 238 240 {ECO:0000244|PDB:2JKR}.
STRAND 244 248 {ECO:0000244|PDB:1I31}.
STRAND 252 254 {ECO:0000244|PDB:2VGL}.
TURN 255 258 {ECO:0000244|PDB:2JKR}.
STRAND 263 265 {ECO:0000244|PDB:1I31}.
STRAND 269 279 {ECO:0000244|PDB:1I31}.
STRAND 287 296 {ECO:0000244|PDB:1I31}.
TURN 297 299 {ECO:0000244|PDB:1I31}.
STRAND 300 309 {ECO:0000244|PDB:1I31}.
STRAND 316 325 {ECO:0000244|PDB:1I31}.
STRAND 330 336 {ECO:0000244|PDB:1I31}.
STRAND 338 345 {ECO:0000244|PDB:1I31}.
HELIX 346 348 {ECO:0000244|PDB:1I31}.
STRAND 350 361 {ECO:0000244|PDB:1I31}.
STRAND 363 372 {ECO:0000244|PDB:1I31}.
STRAND 377 379 {ECO:0000244|PDB:1I31}.
STRAND 386 394 {ECO:0000244|PDB:1I31}.
TURN 396 398 {ECO:0000244|PDB:2XA7}.
STRAND 401 407 {ECO:0000244|PDB:1I31}.
STRAND 409 412 {ECO:0000244|PDB:1I31}.
HELIX 415 417 {ECO:0000244|PDB:1I31}.
STRAND 419 433 {ECO:0000244|PDB:1I31}.
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


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