ID F7CVC4_HORSE Unreviewed; 862 AA.
AC F7CVC4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=AP2A2 {ECO:0000313|Ensembl:ENSECAP00000012998.4,
GN ECO:0000313|VGNC:VGNC:15378};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000012998.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000012998.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012998.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000012998.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012998.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the 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 proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-
CC containing lipids, positioning AP-2 on the membrane. The AP-2 alpha
CC subunit acts via its C-terminal appendage domain as a scaffolding
CC platform for endocytic accessory proteins. The AP-2 alpha and AP-2
CC sigma subunits are thought to contribute to the recognition of the
CC [ED]-X-X-X-L-[LI] motif. {ECO:0000256|PIRNR:PIRNR037091}.
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). {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004277}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR037091}.
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DR AlphaFoldDB; F7CVC4; -.
DR STRING; 9796.ENSECAP00000012998; -.
DR PaxDb; 9796-ENSECAP00000012998; -.
DR Ensembl; ENSECAT00000016112.4; ENSECAP00000012998.4; ENSECAG00000014550.4.
DR VGNC; VGNC:15378; AP2A2.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_1_1_1; -.
DR InParanoid; F7CVC4; -.
DR OMA; PVLMHRY; -.
DR OrthoDB; 25313at2759; -.
DR TreeFam; TF300308; -.
DR Proteomes; UP000002281; Chromosome 12.
DR Bgee; ENSECAG00000014550; Expressed in prefrontal cortex and 23 other cell types or tissues.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.1230; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.310.10; TATA-Binding Protein; 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; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1.
DR PANTHER; PTHR22780:SF30; AP-2 COMPLEX SUBUNIT ALPHA-2; 1.
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; ARM repeat; 1.
DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE 1: Evidence at protein level;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR037091};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583, ECO:0000256|PIRNR:PIRNR037091};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037091};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR037091};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F7CVC4};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 630..743
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 537..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 95419 MW; 9FB670A138A2197F CRC64;
MEAVNLLSSN RYTEKQIGYL FISVLVNSNS ELIRLINNAI KNDLASRNPT FMGLALHCIA
NVGSREMAEA FAGEIPKILV AGDTMDSVKQ SAALCLLRLY RTSPDLVPMG DWTSRVVHLL
NDQHLGVVTA ATSLITTLAQ KNPEEFKTSV SLAVSRLSRI VTSASTDLQD YTYYFVPAPW
LSVKLLRLLQ CYPPPEDPAV RGRLTECLET ILNKAQEPPK SKKVQHSNAK NAVLFEAISL
IIHHDSEPNL LVRACNQLGQ FLQHRETNLR YLALESMCTL ASSEFSHEAV KTHIETVTNA
LKTERDVSVR QRAVDLLYAM CDRSNAQQIV AEMLSYLETA DYSIREEIVL KVAILAEKYA
VDYTWYVDTI LNLIRIAGDY VSEEVWYRVI QIVINRDDVQ GYAAKTVFEA LQAPACHENL
VKVGGYILGE FGNLIAGDPR SSPLIQFNLL HSKFHLCSVP TRALLLSTYI KFVNLFPEVK
TTIQDVLRSD SQLKNADVEL QQRAVEYLRL STVASTDILA TVLEEMPPFP ERESSILAKL
KKKKGPSTVT DLEEAKRERS ADINGGPEPA PASASATSTP SPSADLLGLG AAPPAPVGPP
PSSGGLLVDV FSDSPSAVAP LAPGSEDNFA RFVCKNNGVL FENQLLQIGL KSEFRQNLGR
MFIFYGNKTS TQFLSFTPTL ICSDDLRANL SLQTKPVDPT VDGGAQVQQV VNIECVSDFT
EAPVLNIQFR YGGTFQNVSV KLPITLNKFF QPTEMASQDF FQRWKQLSNP QQEVQNIFKA
KHPMDTEITK AKIIGFGSAL LEEVDPNPAN FVGAGIIHTK TTQIGCLLRL EPNLQAQMYR
LTLRTSKETV SQRLCELLSE QF
//
