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Database: UniProt
Entry: A0A3D8QZF6_9EURO
LinkDB: A0A3D8QZF6_9EURO
Original site: A0A3D8QZF6_9EURO 
ID   A0A3D8QZF6_9EURO        Unreviewed;       957 AA.
AC   A0A3D8QZF6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN   ORFNames=DSM5745_09001 {ECO:0000313|EMBL:RDW67135.1};
OS   Aspergillus mulundensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW67135.1, ECO:0000313|Proteomes:UP000256690};
RN   [1] {ECO:0000313|EMBL:RDW67135.1, ECO:0000313|Proteomes:UP000256690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW67135.1,
RC   ECO:0000313|Proteomes:UP000256690};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDW67135.1}.
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DR   EMBL; PVWQ01000012; RDW67135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8QZF6; -.
DR   STRING; 1810919.A0A3D8QZF6; -.
DR   OrthoDB; 123661at2759; -.
DR   Proteomes; UP000256690; 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; 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   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:UP000256690};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT   DOMAIN          696..807
FT                   /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT                   Ig-like subdomain"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   BINDING         5..6
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         37
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         46
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         50..54
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   957 AA;  107170 MW;  B3135AECB60C1B61 CRC64;
     MSSMRGLVQF IADLRNARAR ELEEKRVNKE LANIRQKFKS GSLDGYQKKK YVCKLLYVYI
     QGYDVDFGHL EAVNLISSNK YSEKQIGYLA VTLFLHEEHE LLHLVVNSIR KDLLDQHELN
     NCLALHAVAN VGSREMGEAL STDVHRLLIS PTSKAFVKKK AALTLLRLYR KYPSIVQNQW
     AERIISLMDD PDMGVTLSVT SLVMALAQDR PDEYRGSYVK AAQRLKRIVV DNDIAPDYLY
     YRVPCPWLQV KLLRLLQYYP PSADSHVRDI IRESLQQIMQ IAMDTPKNVQ QNNAQNAVLF
     EAINLLIHLD TEHTLMMQIS SRLGKYIQSR ETNVRYLGLE AMTHFAARAE TLDPIKKHQS
     IILGSLRDRD ISVRRKGLDL VYSMCDITNA APIVNELMRY LQSADYAIRE EMVLKVAILT
     EKYATDAQWY IDVTLKLLSL AGDHVNDEVW QRVIQIVTNN EELQAYAAQT LLTYLKSDCH
     ESLVKIGCYV LGEFGHLVAD NQGSSPIEQF LALQAKMMTS TDNTRAMILS SFVKFVNLFP
     EIKPQLLHIF RLYSHSPDPE LQQRAFEYLS LATLPTDDLL RTVCDEMPPF SERASILLSR
     LHQKTAGTTD KKTWVVGGKD ANTDGAEILM AQNTGLKRSF TTIVNGTPTG ANGATASSSA
     SGDLAGLDLS ASTPPPAPTN MASAANLSPD WDIGYNKLYF SDEGVLFEDL QIQVGLRSEF
     RGHLGVLKLY ISNKSSFPIG SLTTTVDNPS APHLRIDSKS LPEPSVPAAG QTQQTLFFEA
     KGPFSSAPTI RISYLAGALQ AYTLQLPILM HRYLEPSSLT AEDFFKRWRQ IGGGPLEAQN
     TFGLAPKAGS VSEGFTKRLV EQFGWKLLSG VDPIPTNIVG CAVYHSAQGK IGCLLRLEPN
     YERKMYRVTI RATQEGIPQA LARQMEERLS HGTLSDRSYV REKPRGIDVG DDFTSGY
//
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