MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | 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; |
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| MyHits synonyms | AP2A2_RAT , P18484 , 406428A9BFFB1E53 |
 Legends: 1, INIT_MET Removed. {ECO:0000269|PubMed:1325787, ECO:0000269|PubMed:2495531}; 2, BINDING Phosphatidylinositol lipid headgroup. {ECO:0000250}; 3, REGION Lipid-binding; 4, ipfam:Alpha_adaptinC2 [T]; 5, ismart:Alpha_adaptinC2 [T]; 6, ipfam:Alpha_adaptin_C [T]; 7, HELIX {ECO:0000244|PDB:2VGL}; 8, STRAND {ECO:0000244|PDB:2VGL}; 9, HELIX {ECO:0000244|PDB:4UQI}; 10, TURN {ECO:0000244|PDB:2VGL}.
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ID AP2A2_RAT Reviewed; 938 AA.
AC P18484;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 10-MAY-2017, entry version 149.
DE RecName: Full=AP-2 complex subunit alpha-2;
DE AltName: Full=100 kDa coated vesicle protein C;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE AltName: Full=Adaptor-related protein complex 2 subunit alpha-2;
DE AltName: Full=Alpha-adaptin C;
DE AltName: Full=Alpha2-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN Name=Ap2a2; Synonyms=Adtab;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2402467; DOI=10.1093/nar/18.17.5306;
RA Tucker K.L., Nathanson K., Kirchhausen T.;
RT "Sequence of the rat alpha c large chain of the clathrin associated
RT protein complex AP-2.";
RL Nucleic Acids Res. 18:5306-5306(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-18.
RC TISSUE=Brain;
RX PubMed=2495531; DOI=10.1073/pnas.86.8.2612;
RA Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P.,
RA Burne C., Keen J.H., Davis A.E.;
RT "Structural and functional division into two domains of the large
RT (100- to 115-kDa) chains of the clathrin-associated protein complex
RT AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=1325787; DOI=10.1016/S0006-291X(05)81473-1;
RA Voglmaier S.M., Keen J.H., Murphy J.E., Ferris C.D., Prestwich G.D.,
RA Snyder S.H., Theibert A.B.;
RT "Inositol hexakisphosphate receptor identified as the clathrin
RT assembly protein AP-2.";
RL Biochem. Biophys. Res. Commun. 187:158-163(1992).
RN [4]
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
RT the post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [5]
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).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC Adaptor protein complexes function in protein transport via
CC transport vesicles in different membrane traffic pathways. Adaptor
CC protein complexes are vesicle coat components and appear to be
CC involved in cargo selection and vesicle formation. AP-2 is
CC involved in clathrin-dependent endocytosis in which cargo proteins
CC are incorporated into vesicles surrounded by clathrin (clathrin-
CC coated vesicles, CCVs) which are destined for fusion with the
CC early endosome. The clathrin lattice serves as a mechanical
CC scaffold but is itself unable to bind directly to membrane
CC components. Clathrin-associated adaptor protein (AP) complexes
CC which can bind directly to both the clathrin lattice and to the
CC lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane
CC proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC play a role in the recycling of synaptic vesicle membranes from
CC the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC play a role in maintaining normal post-endocytic trafficking
CC through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC subunit binds polyphosphoinositide-containing lipids, positioning
CC AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC terminal appendage domain as a scaffolding platform for endocytic
CC accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134,
CC ECO:0000269|PubMed:15473838}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1,
CC EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1. Interacts with
CC DGKD isoform 2 (By similarity). Interacts with DENND1A, DENND1B
CC and DENND1C (By similarity). Interacts with FCHO1 and DAB2 (By
CC similarity). Interacts with ATAT1; this interaction is required
CC for efficient alpha-tubulin acetylation by ATAT1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P21707:Syt1; NbExp=5; IntAct=EBI-539360, EBI-458098;
CC -!- SUBCELLULAR LOCATION: Cell membrane
CC {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P17427}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P17427}. Note=AP-2 appears to be excluded
CC from internalizing CCVs and to disengage from sites of endocytosis
CC seconds before internalization of the nascent CCV.
CC {ECO:0000250|UniProtKB:P17427}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; X53773; CAA37791.1; -; mRNA.
DR PIR; S11276; S11276.
DR UniGene; Rn.34928; -.
DR PDB; 2VGL; X-ray; 2.59 A; A=1-620.
DR PDB; 2XA7; X-ray; 3.10 A; A=1-621.
DR PDB; 4NEE; X-ray; 2.88 A; A/B/G/J=1-395.
DR PDB; 4UQI; X-ray; 2.79 A; A=1-620.
DR PDBsum; 2VGL; -.
DR PDBsum; 2XA7; -.
DR PDBsum; 4NEE; -.
DR PDBsum; 4UQI; -.
DR ProteinModelPortal; P18484; -.
DR SMR; P18484; -.
DR DIP; DIP-29765N; -.
DR IntAct; P18484; 6.
DR MINT; MINT-93156; -.
DR STRING; 10116.ENSRNOP00000060992; -.
DR PaxDb; P18484; -.
DR PeptideAtlas; P18484; -.
DR PRIDE; P18484; -.
DR UCSC; RGD:71015; rat.
DR RGD; 71015; Ap2a2.
DR eggNOG; KOG1077; Eukaryota.
DR eggNOG; ENOG410XNQE; LUCA.
DR HOVERGEN; HBG050518; -.
DR InParanoid; P18484; -.
DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR EvolutionaryTrace; P18484; -.
DR PRO; PR:P18484; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030122; C:AP-2 adaptor complex; IMP:CAFA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:CAFA.
DR GO; GO:0032403; F:protein complex binding; IPI:RGD.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coated pit; Complete proteome;
KW Direct protein sequencing; Endocytosis; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1325787,
FT ECO:0000269|PubMed:2495531}.
FT CHAIN 2 938 AP-2 complex subunit alpha-2.
FT /FTId=PRO_0000193734.
FT REGION 5 80 Lipid-binding.
FT BINDING 43 43 Phosphatidylinositol lipid headgroup.
FT {ECO:0000250}.
FT BINDING 53 53 Phosphatidylinositol lipid headgroup.
FT {ECO:0000250}.
FT BINDING 57 57 Phosphatidylinositol lipid headgroup.
FT {ECO:0000250}.
FT BINDING 58 58 Phosphatidylinositol lipid headgroup.
FT {ECO:0000250}.
FT BINDING 61 61 Phosphatidylinositol lipid headgroup.
FT {ECO:0000250}.
FT HELIX 11 22 {ECO:0000244|PDB:2VGL}.
FT HELIX 26 45 {ECO:0000244|PDB:2VGL}.
FT STRAND 46 48 {ECO:0000244|PDB:2VGL}.
FT HELIX 52 68 {ECO:0000244|PDB:2VGL}.
FT HELIX 76 81 {ECO:0000244|PDB:2VGL}.
FT HELIX 82 84 {ECO:0000244|PDB:2VGL}.
FT HELIX 88 100 {ECO:0000244|PDB:2VGL}.
FT HELIX 106 121 {ECO:0000244|PDB:2VGL}.
FT HELIX 125 138 {ECO:0000244|PDB:2VGL}.
FT HELIX 141 147 {ECO:0000244|PDB:2VGL}.
FT HELIX 150 156 {ECO:0000244|PDB:2VGL}.
FT STRAND 158 160 {ECO:0000244|PDB:2VGL}.
FT HELIX 162 178 {ECO:0000244|PDB:2VGL}.
FT HELIX 180 182 {ECO:0000244|PDB:2VGL}.
FT HELIX 189 195 {ECO:0000244|PDB:2VGL}.
FT HELIX 201 217 {ECO:0000244|PDB:2VGL}.
FT HELIX 219 222 {ECO:0000244|PDB:2VGL}.
FT HELIX 225 238 {ECO:0000244|PDB:2VGL}.
FT STRAND 241 243 {ECO:0000244|PDB:2VGL}.
FT HELIX 245 247 {ECO:0000244|PDB:4UQI}.
FT STRAND 252 254 {ECO:0000244|PDB:2VGL}.
FT HELIX 255 264 {ECO:0000244|PDB:2VGL}.
FT HELIX 265 267 {ECO:0000244|PDB:2VGL}.
FT STRAND 268 270 {ECO:0000244|PDB:2VGL}.
FT HELIX 273 291 {ECO:0000244|PDB:2VGL}.
FT HELIX 299 319 {ECO:0000244|PDB:2VGL}.
FT HELIX 323 336 {ECO:0000244|PDB:2VGL}.
FT HELIX 342 355 {ECO:0000244|PDB:2VGL}.
FT TURN 359 361 {ECO:0000244|PDB:2VGL}.
FT HELIX 362 366 {ECO:0000244|PDB:2VGL}.
FT HELIX 369 376 {ECO:0000244|PDB:2VGL}.
FT HELIX 382 395 {ECO:0000244|PDB:2VGL}.
FT HELIX 398 414 {ECO:0000244|PDB:2VGL}.
FT HELIX 417 434 {ECO:0000244|PDB:2VGL}.
FT HELIX 439 452 {ECO:0000244|PDB:2VGL}.
FT HELIX 453 455 {ECO:0000244|PDB:2VGL}.
FT HELIX 459 468 {ECO:0000244|PDB:2VGL}.
FT HELIX 469 471 {ECO:0000244|PDB:2VGL}.
FT HELIX 472 474 {ECO:0000244|PDB:4UQI}.
FT HELIX 475 486 {ECO:0000244|PDB:2VGL}.
FT STRAND 488 490 {ECO:0000244|PDB:2VGL}.
FT HELIX 493 506 {ECO:0000244|PDB:2VGL}.
FT HELIX 508 511 {ECO:0000244|PDB:2VGL}.
FT HELIX 518 529 {ECO:0000244|PDB:2VGL}.
FT HELIX 534 550 {ECO:0000244|PDB:2VGL}.
FT HELIX 552 554 {ECO:0000244|PDB:2VGL}.
FT HELIX 555 562 {ECO:0000244|PDB:2VGL}.
FT HELIX 565 568 {ECO:0000244|PDB:2VGL}.
FT HELIX 573 587 {ECO:0000244|PDB:2VGL}.
FT TURN 592 597 {ECO:0000244|PDB:2VGL}.
FT STRAND 598 600 {ECO:0000244|PDB:2VGL}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 712 816 ipfam:Alpha_adaptinC2 [T]
FT MYHIT 31 587 ipfam:Adaptin_N [T]
FT MYHIT 706 819 ismart:Alpha_adaptinC2 [T]
FT MYHIT 825 933 ipfam:Alpha_adaptin_C [T]
SQ 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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