ID W6PRJ7_PENRF Unreviewed; 945 AA.
AC W6PRJ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 03-MAY-2023, entry version 40.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=alpha-Adaptin {ECO:0000313|EMBL:CDM26808.1};
GN ORFNames=PROQFM164_S01g000617 {ECO:0000313|EMBL:CDM26808.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM26808.1};
RN [1] {ECO:0000313|EMBL:CDM26808.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM26808.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792015; CDM26808.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PRJ7; -.
DR STRING; 1365484.W6PRJ7; -.
DR OMA; PVLMHRY; -.
DR OrthoDB; 123661at2759; -.
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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 701..812
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 644..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 945 AA; 105978 MW; 033FBBF146F9127E CRC64;
MSSMRGLVQF IADLRNARAR ELEEKRVNKE LANIRQKFKS GNLNGYQKKK YVCKLLYVYI
QGYDVDFGHL EAVNLITSPK YSEKQIGYLA VTLFLHEEHE LLHLVVNSIR KDLLDHNELN
NCLALHAVAN VGGKELGEAL GSEVHRLLIS PTSKSFVKKK AALTLLRLYR KYPGIVRNEW
AERIISIMDD PDMGVTLSVT SLVMALAQDL PEEYKGCYVK AAQRLKRIVV DNDIAPDYLY
YRVPCPWIQV KFLRLLQYYP PSEDSHVREI IRESLSQMMQ AAMETPKNVQ QNNAQNAILF
EAINLLIHLD SEHNLMMQIS TRLGKYIQSR ETNVRYLGLD ALTHFAARAE TLDPIKKHQN
IILGSLRDRD ISVRRKGLDL LYSMCDTSNA GPIVNELLRY LQTADYAIRE EMVLKVAILT
EKYAADAQWY IDMTLKLLSL AGEHVNDEVW QRVIQIVTNN EELQAYAAHT LLGYLKSDCH
ESLVKIGCYV LGEYGHLIAE NAGSSPIEQF LALQAKMFSS SDNARAMILS SFVKFVNLFP
EIKPQLLQIF RLYSHSPDSE LQQRAFEYLS LATLPTDDLL RTVCDEMPPF SERTSILLSR
LHQKTAGASE KKTWVIGGKD ANADKQEMLL AQNTGLKRTF TTIVNGTRTG SGNTPASPAS
ASNAASSSGD LAGLDLSGPT APAPNMASAA HLTPEWDIGY NRLYFSREGV LFEDAQIQVG
LRSEYRGPMG VVKLYISNKS TYPIGSLTTT VDNPASPQLK IDTRNLPEPT VAAAGQTQQT
LFCTAHGPFA DAPTIRISYL AGALQAYTLQ LPVLMHRYME SSSLSAEEFF KRWRQIGGGP
LESQKTFALL GKNKTTNERF TRRIVEGFAF KILDGVDPNS QNIVGCAVYQ FEGGKTGCLL
RLEPNYEKKM YRVTVRATQE EVPGPLVKQM ELKLAQGMRA DEAFD
//
