Entry euk:AP2A2_BOVIN

ID   AP2A2_BOVIN             Reviewed;         938 AA.
AC   Q0VCK5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   10-MAY-2017, entry version 78.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-17.
RX   PubMed=2564002; DOI=10.1083/jcb.108.3.833;
RA   Robinson M.S.;
RT   "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins
RT   (alpha-adaptins).";
RL   J. Cell Biol. 108:833-842(1989).
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}.
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 (By similarity).
CC       Interacts with ATAT1; this interaction is required for efficient
CC       alpha-tubulin acetylation by ATAT1 (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; BC120121; AAI20122.1; -; mRNA.
DR   RefSeq; NP_001069170.1; NM_001075702.1.
DR   UniGene; Bt.2041; -.
DR   ProteinModelPortal; Q0VCK5; -.
DR   SMR; Q0VCK5; -.
DR   STRING; 9913.ENSBTAP00000048343; -.
DR   PaxDb; Q0VCK5; -.
DR   PRIDE; Q0VCK5; -.
DR   GeneID; 515216; -.
DR   KEGG; bta:515216; -.
DR   CTD; 161; -.
DR   eggNOG; KOG1077; Eukaryota.
DR   eggNOG; ENOG410XNQE; LUCA.
DR   HOGENOM; HOG000170596; -.
DR   HOVERGEN; HBG050518; -.
DR   InParanoid; Q0VCK5; -.
DR   KO; K11824; -.
DR   Proteomes; UP000009136; Unplaced.
DR   Bgee; ENSBTAG00000009915; -.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IDA:BHF-UCL.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0048268; P:clathrin coat assembly; IC:BHF-UCL.
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   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:0000250|UniProtKB:P18484}.
FT   CHAIN         2    938       AP-2 complex subunit alpha-2.
FT                                /FTId=PRO_0000283799.
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}.
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    588       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;  103769 MW;  853700BF86A7A916 CRC64;
     MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
     KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
     ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLHRASP
     DLVPVGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
     STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDPAVRGRL TECLEAILNK AQEPPKSKKV
     QHSNAKNAVL FEAISLVTHH DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
     FSHEAVKTHI ETVINALKTE RDVSVRQRAV DLLYAMCDRS NAQQIVAEML SYLETADYSI
     REEIVLKVAI LAEKYAVDYT WYVDTILNLI RIAGDYVSEE VWYRVIQIVI NRDDVQGYAA
     KTVFEALQAP ACHENLVKVG GYILGEFGNL IAGDPRSSPL TQFHLLHSKF HLCSVPTRAL
     LLSTYIKFVN LFPEVKGTIQ DVLRSDSQLK NADVELQQRA VEYLRLSTVA STDILATVLE
     EMPPFPERES SILAKLKKKK GPSTVTDLEE AKRERSADVN GGPEPALAST SAVSTPSPSA
     DLLGLGAAPP VPAGPPPSSG GLLVDVFSDS PSAAAPLAPG SEDNFARFVC KNNGVLFENQ
     LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICSD DLQANLSLQT KPVDPTVDGG
     AQVQQAVNIE CVSDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW
     KQLSNPQQEV QSIFKAKHPM DTEVTKAKII GFGSALLEEV DPNPANFVGA GIIHTRTAQI
     GCLLRLEPNL QAQMYRLTLR TSRETVSQRL CELLSEQF
//