ID Q6FUD2_CANGA Unreviewed; 1006 AA.
AC Q6FUD2;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN OrderedLocusNames=CAGL0F04389g {ECO:0000313|CGD:CAL0129691,
GN ECO:0000313|EMBL:CAG59086.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59086.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59086.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR380952; CAG59086.1; -; Genomic_DNA.
DR RefSeq; XP_446162.1; XM_446162.1.
DR AlphaFoldDB; Q6FUD2; -.
DR STRING; 284593.Q6FUD2; -.
DR EnsemblFungi; CAGL0F04389g-T; CAGL0F04389g-T-p1; CAGL0F04389g.
DR GeneID; 2887669; -.
DR KEGG; cgr:CAGL0F04389g; -.
DR CGD; CAL0129691; CAGL0F04389g.
DR VEuPathDB; FungiDB:CAGL0F04389g; -.
DR eggNOG; KOG1077; Eukaryota.
DR HOGENOM; CLU_003824_1_0_1; -.
DR InParanoid; Q6FUD2; -.
DR OMA; PVLMHRY; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0030122; C:AP-2 adaptor complex; IEA:EnsemblFungi.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
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; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 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 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:UP000002428};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 746..848
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 696..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
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 73..77
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 1006 AA; 113626 MW; 717387E8274A3551 CRC64;
MDRKKTFVGT SNNGSSSIKG LQLFIADLRS APHLQDQERR IQSEITKIKQ NFDTQHQKQS
KGQDKQGGYQ RKKYIAKLAY IYITSNTSKL NDIIFGLDQT MELIQSSVYS EKFIAYMTIE
LLYEHKTVMD KINDALQYQI LLDLRSNDEN FVSLALNCVG IVGSLSKTLS NDEDIVAEVF
QILRSPTSSM NLKKKSSLAF LTLLKKNNAI LTNEPQRKQI WIQRILSLLD NRDNYRLTLA
SLPLIEYIAV HVDPAACTRL VPQLTQTLYS CLMNESSSNI DNPQLDFRFA NMPNPWIITK
TVSLLNMLII SSNEKSSAQN DHLLHTSTMN KEILNTLRTC ISQAIQLGER SFSDPMERIV
QNTILFSLIN FAPKLDPSDD AITDSVTALC KLLSSSQINI RYLALDSLIK LCSVLGTSAM
NAVRLQNLDM ISQLLYDERD ASIIRKLADL LYIFTDSSNV KKTVDDLLQY ITSSKQLADP
NLKSDIAVKI AVLSEKYATD SNWFVTVSLK LLSFTSLTSI NDDEIWQRLC QIVVNNPALQ
RTACEQLLYY FKNSQTSEPL IKTGAFLFGE FIDQITDLIS VADLFNIFTT KYFTVTNFTK
AMILTTVMKL YRCSDSIYTG AVKIYQMELS SLDIELQSRS YEYLNILRIA RMENNPNLIN
ILFHPIPPFN SSTNPLLKRL GLLQTSDNDL TIEALTSNPS SKDSSNPFTQ PTSTDTSVTE
NGKNMVTQEE LYNSQILAAS WRDGFSRMLS FKRGILFSSS LLKILYRLDY PSPEEPYQQK
ISLTFINESE WDMTNFSTNI IPFRTDSNPE YVVQEISLLS ALDIAPRRRT EQTLDIIIRR
QFNAEYSPII SIFFKCGAST NTINLKLGVG LNSTLRTTEA PKQQLTLAQF FSRWKALGDA
LGTEGECIIT KLRLKSIKNI SHSQEESILQ VSLILKRMGF DIVEQSNLPN SLFFAGIIHT
KTDGNYGCLI RVSCEDEEYF TLTCRATIGS GLATNIASCI KLAAFA
//
