ID A0A238FFD1_9BASI Unreviewed; 992 AA.
AC A0A238FFD1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=BQ2448_4047 {ECO:0000313|EMBL:SCV72510.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV72510.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration.
CC {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|PIRNR:PIRNR037091}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMSP01000009; SCV72510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FFD1; -.
DR STRING; 269621.A0A238FFD1; -.
DR OrthoDB; 123661at2759; -.
DR Proteomes; UP000198372; Unassembled WGS sequence.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:InterPro.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
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:SF4; AP-2 COMPLEX SUBUNIT ALPHA; 1.
DR Pfam; PF01602; Adaptin_N; 2.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 2.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 771..882
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT BINDING 13..14
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT BINDING 45
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
FT BINDING 58..62
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000256|PIRSR:PIRSR037091-1"
SQ SEQUENCE 992 AA; 110948 MW; 4F65906D563CAF57 CRC64;
MLRVPNMNKD EMRGLTQYIA DLRACRVREL EEKRINKEMA HIRHKFKDGN LDGRQKKKYI
SKIIFTSILG YPVDVGHMEA VNLISSTKYS EKQIVSQHHT LPRAALDYPR SPLAQPLRRQ
GYLALTLLMH ENSDLVRLIV NSIRKDLDAL DETVNCLALH AIANIGGAEM AEALASDVHR
LLISPTSRSF VKKKAALTLL RLYRKHPEVI PAAEWASRIV SIMDDQDLGV ALAVASLVLT
LAQDNLVAYA VAYQKAVDRL AKIVLENEYP SDYLYYKVPI PWLQVKLLRL LQYYPPSEDA
NLRLTLHKVL ERILKNSQDM PKNPQHNNAL NAVLFEAINL AIHLDTESTI VHSAALLLGR
FISAKETNVR YLGLDTMTHL AARSDSLDAI KVHQTVIIQS LRDKDISVRR RGLDLLYSMC
DTSNSKVIVS ELLKYLPIAD YTLREEMVLK IAILTEKFAV EYEWYVDTIL KLMSIAGDHV
GDEVWYRIVQ IVTNTEELQE YAAQKVFDHL SLPNCHENIL KVGAYILGEY GHLIADEEGR
SPIEQFQLVN SRANLASAST KALLLTTYFK WLNLFPEIYE QIVNVFERYS RVLDAELQQR
ACEYLVIAKQ PDDELLQVVA DEMPPYPERE SALLSRLLKK HGDTGDKRTW HIGGKDINRG
QDAERYKGFG RRKMNATSDA TRAAPIDTTT AARSVAIPEV DTNDVMSSLA GLDLSSSTVE
RHDNSSALLP PAPAAGEASV PLLGAASTAT TPTTPRKMSL SLTHGSEKWL ARLLYNSDGV
LYEDTQLQVG VKTEFHGHQG RIAIFFGNKL SVALESLTAT FDVEDEDALE VKLPSIVPSH
LSAAAQVQQL ALVESKSTFS TPPLLRISYL AGSHQELVLR LPVFLTKFIE PVQLSSDAFF
ERWKQIGGAP REQQKIFPIV ILDGNRVDVA KQRKVVGGIR LGILEGVDPN PNNLVAAGVL
HMSSVGKVGC LVRVEPNPDR KEYERASIDR DA
//
