ID A0A0D1WRQ8_9EURO Unreviewed; 943 AA.
AC A0A0D1WRQ8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=PV11_09542 {ECO:0000313|EMBL:KIV77761.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77761.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77761.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77761.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846954; KIV77761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1WRQ8; -.
DR STRING; 1016849.A0A0D1WRQ8; -.
DR HOGENOM; CLU_003824_1_0_1; -.
DR OrthoDB; 123661at2759; -.
DR Proteomes; UP000053599; 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:UP000053599};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 706..817
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 943 AA; 105918 MW; E6F365C5371EE417 CRC64;
MSSMRGLVQF IADLRNARAR ELEEKRINKE LANIRQKFKS EKLDGYQKKK YVCKLLYIYI
QGYNVDFGHL EAVNLISATK YSEKQIGYLA VTLFLHEQHE LLHLVVNSIR KDLTDHNELN
NCLALHAVAN VGGREMGEAL SGDVHRLLIS PTSKSFVKKK AALTLLRLYR KYPGIHQAEW
AERIISLMDD PDMGVVLSVT SLIMALTQDH PEAYKGSYVK AAQRLRKIVI ENDVSPDYFY
YKVPCPWIQV KFLKLLQYYP PSEDSHVRDI IRESLQAIVQ AASETPKNVQ QNNAQNAVLF
DAINLLIHLD SEHQLMIQIS SKLGRFIQSR ETNVRYLGLD AMAHFAARSD TLDPIKRHQS
IIIGSLRDRD ISVRRKGLDL LYSMCDTTNA QSIVNELLKY LQSADYSIRE EMTLKIAILT
EKYATDAQWY IDISLRLLAM AGDHVSDEVW QRVVQIVTNN EEIQPYAAQH IFEYLKAEGC
HDTLVKIGGY ILGEFGHLIA DHKGCSPIEQ LMVLQTKMIS APDTSRALLL STFVKFVNLF
PEIKPQLLQM FQFYSHSPDS ELQQRACEYL AIATLPTDDL LRTICDEMPP FSERASILLQ
RLHKKSVGTS ERRTWLVGGK DANADKQEVL LAQQTGLKRT FTTIVNGGAQ TNGNGTVSKN
ATGAQNAAGG ASKDLEGLDM NGHTDDAKSN LASAAHLSPD WELGYEQMYF TDEGVLYEDP
QIQVGLRAEY RGHLGVVKLY FANKASFPIG SFTTTLENKS APKLKMDTKS LPDSSVGPDS
QVQQTIICTS VAPFAEPPTI RISYLAGALQ GYTLKLPILP HRFMDPSELS AEDFFKRWRQ
IGGGPLEAQS TFGLKNQGSE LSDKHTRDVV SGFKWRILDN VDPNPQNIVG CAVLQLEKGK
TGCLLRLEPN HQQKMFRLTI RATQDTVPGI LLGMMQERLA KGS
//
