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AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)

 AP2A2_RAT               Reviewed;         938 AA.
P18484;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 160.
RecName: Full=AP-2 complex subunit alpha-2;
AltName: Full=100 kDa coated vesicle protein C;
AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
AltName: Full=Adaptor-related protein complex 2 subunit alpha-2;
AltName: Full=Alpha-adaptin C;
AltName: Full=Alpha2-adaptin;
AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
Name=Ap2a2; Synonyms=Adtab;
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].
PubMed=2402467; DOI=10.1093/nar/18.17.5306;
Tucker K.L., Nathanson K., Kirchhausen T.;
"Sequence of the rat alpha c large chain of the clathrin associated
protein complex AP-2.";
Nucleic Acids Res. 18:5306-5306(1990).
[2]
PROTEIN SEQUENCE OF 2-18.
TISSUE=Brain;
PubMed=2495531; DOI=10.1073/pnas.86.8.2612;
Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P.,
Burne C., Keen J.H., Davis A.E.;
"Structural and functional division into two domains of the large
(100- to 115-kDa) chains of the clathrin-associated protein complex
AP-2.";
Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989).
[3]
PROTEIN SEQUENCE OF 2-18.
PubMed=1325787; DOI=10.1016/S0006-291X(05)81473-1;
Voglmaier S.M., Keen J.H., Murphy J.E., Ferris C.D., Prestwich G.D.,
Snyder S.H., Theibert A.B.;
"Inositol hexakisphosphate receptor identified as the clathrin
assembly protein AP-2.";
Biochem. Biophys. Res. Commun. 187:158-163(1992).
[4]
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).
[5]
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).
-!- 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 alpha
subunit binds polyphosphoinositide-containing lipids, positioning
AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
terminal appendage domain as a scaffolding platform for endocytic
accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134,
ECO:0000269|PubMed:15473838}.
-!- 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). Binds EPN1,
EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1. Interacts with
DGKD isoform 2 (By similarity). Interacts with DENND1A, DENND1B
and DENND1C (By similarity). Interacts with FCHO1 and DAB2 (By
similarity). Interacts with ATAT1; this interaction is required
for efficient alpha-tubulin acetylation by ATAT1 (By similarity).
Interacts with KIAA1107 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:O94973}.
-!- INTERACTION:
P21707:Syt1; NbExp=5; IntAct=EBI-539360, EBI-458098;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P17427}; Cytoplasmic side
{ECO:0000250|UniProtKB:P17427}. Membrane, coated pit
{ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P17427}; Cytoplasmic side
{ECO:0000250|UniProtKB:P17427}. 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|UniProtKB:P17427}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X53773; CAA37791.1; -; mRNA.
PIR; S11276; S11276.
UniGene; Rn.34928; -.
PDB; 2VGL; X-ray; 2.59 A; A=1-620.
PDB; 2XA7; X-ray; 3.10 A; A=1-621.
PDB; 4NEE; X-ray; 2.88 A; A/B/G/J=1-395.
PDB; 4UQI; X-ray; 2.79 A; A=1-620.
PDBsum; 2VGL; -.
PDBsum; 2XA7; -.
PDBsum; 4NEE; -.
PDBsum; 4UQI; -.
ProteinModelPortal; P18484; -.
SMR; P18484; -.
CORUM; P18484; -.
DIP; DIP-29765N; -.
IntAct; P18484; 12.
MINT; P18484; -.
STRING; 10116.ENSRNOP00000060992; -.
CarbonylDB; P18484; -.
PaxDb; P18484; -.
PeptideAtlas; P18484; -.
PRIDE; P18484; -.
UCSC; RGD:71015; rat.
RGD; 71015; Ap2a2.
eggNOG; KOG1077; Eukaryota.
eggNOG; ENOG410XNQE; LUCA.
HOVERGEN; HBG050518; -.
InParanoid; P18484; -.
EvolutionaryTrace; P18484; -.
PRO; PR:P18484; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030122; C:AP-2 adaptor complex; IMP:CAFA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
GO; GO:0035091; F:phosphatidylinositol binding; IMP:CAFA.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.30.310.10; -; 1.
InterPro; IPR017104; AP2_complex_asu.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR012295; TBP_dom_sf.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02296; Alpha_adaptin_C; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
PIRSF; PIRSF037091; AP2_complex_alpha; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Coated pit; Complete proteome;
Direct protein sequencing; Endocytosis; Lipid-binding; Membrane;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1325787,
ECO:0000269|PubMed:2495531}.
CHAIN 2 938 AP-2 complex subunit alpha-2.
/FTId=PRO_0000193734.
REGION 5 80 Lipid-binding.
BINDING 43 43 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 53 53 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 57 57 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 58 58 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
BINDING 61 61 Phosphatidylinositol lipid headgroup.
{ECO:0000250}.
HELIX 11 22 {ECO:0000244|PDB:2VGL}.
HELIX 26 45 {ECO:0000244|PDB:2VGL}.
STRAND 46 48 {ECO:0000244|PDB:2VGL}.
HELIX 52 68 {ECO:0000244|PDB:2VGL}.
HELIX 76 81 {ECO:0000244|PDB:2VGL}.
HELIX 82 84 {ECO:0000244|PDB:2VGL}.
HELIX 88 100 {ECO:0000244|PDB:2VGL}.
HELIX 106 121 {ECO:0000244|PDB:2VGL}.
HELIX 125 138 {ECO:0000244|PDB:2VGL}.
HELIX 141 147 {ECO:0000244|PDB:2VGL}.
HELIX 150 156 {ECO:0000244|PDB:2VGL}.
STRAND 158 160 {ECO:0000244|PDB:2VGL}.
HELIX 162 178 {ECO:0000244|PDB:2VGL}.
HELIX 180 182 {ECO:0000244|PDB:2VGL}.
HELIX 189 195 {ECO:0000244|PDB:2VGL}.
HELIX 201 217 {ECO:0000244|PDB:2VGL}.
HELIX 219 222 {ECO:0000244|PDB:2VGL}.
HELIX 225 238 {ECO:0000244|PDB:2VGL}.
STRAND 241 243 {ECO:0000244|PDB:2VGL}.
HELIX 245 247 {ECO:0000244|PDB:4UQI}.
STRAND 252 254 {ECO:0000244|PDB:2VGL}.
HELIX 255 264 {ECO:0000244|PDB:2VGL}.
HELIX 265 267 {ECO:0000244|PDB:2VGL}.
STRAND 268 270 {ECO:0000244|PDB:2VGL}.
HELIX 273 291 {ECO:0000244|PDB:2VGL}.
HELIX 299 319 {ECO:0000244|PDB:2VGL}.
HELIX 323 336 {ECO:0000244|PDB:2VGL}.
HELIX 342 355 {ECO:0000244|PDB:2VGL}.
TURN 359 361 {ECO:0000244|PDB:2VGL}.
HELIX 362 366 {ECO:0000244|PDB:2VGL}.
HELIX 369 376 {ECO:0000244|PDB:2VGL}.
HELIX 382 395 {ECO:0000244|PDB:2VGL}.
HELIX 398 414 {ECO:0000244|PDB:2VGL}.
HELIX 417 434 {ECO:0000244|PDB:2VGL}.
HELIX 439 452 {ECO:0000244|PDB:2VGL}.
HELIX 453 455 {ECO:0000244|PDB:2VGL}.
HELIX 459 468 {ECO:0000244|PDB:2VGL}.
HELIX 469 471 {ECO:0000244|PDB:2VGL}.
HELIX 472 474 {ECO:0000244|PDB:4UQI}.
HELIX 475 486 {ECO:0000244|PDB:2VGL}.
STRAND 488 490 {ECO:0000244|PDB:2VGL}.
HELIX 493 506 {ECO:0000244|PDB:2VGL}.
HELIX 508 511 {ECO:0000244|PDB:2VGL}.
HELIX 518 529 {ECO:0000244|PDB:2VGL}.
HELIX 534 550 {ECO:0000244|PDB:2VGL}.
HELIX 552 554 {ECO:0000244|PDB:2VGL}.
HELIX 555 562 {ECO:0000244|PDB:2VGL}.
HELIX 565 568 {ECO:0000244|PDB:2VGL}.
HELIX 573 587 {ECO:0000244|PDB:2VGL}.
TURN 592 597 {ECO:0000244|PDB:2VGL}.
STRAND 598 600 {ECO:0000244|PDB:2VGL}.
SEQUENCE 938 AA; 104045 MW; 406428A9BFFB1E53 CRC64;
MPAVSKGEGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL
LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD
LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ
LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG
AQVQQVINIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW
KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF


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