ID B6H3D3_PENRW Unreviewed; 945 AA.
AC B6H3D3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN ORFNames=Pc13g06600 {ECO:0000313|EMBL:CAP91729.1}, PCH_Pc13g06600
GN {ECO:0000313|EMBL:CAP91729.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91729.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP91729.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920428; CAP91729.1; -; Genomic_DNA.
DR RefSeq; XP_002559093.1; XM_002559047.1.
DR AlphaFoldDB; B6H3D3; -.
DR STRING; 500485.B6H3D3; -.
DR GeneID; 8305532; -.
DR KEGG; pcs:Pc13g06600; -.
DR VEuPathDB; FungiDB:PCH_Pc13g06600; -.
DR eggNOG; KOG1077; Eukaryota.
DR HOGENOM; CLU_003824_1_0_1; -.
DR OMA; PVLMHRY; -.
DR OrthoDB; 123661at2759; -.
DR BioCyc; PCHR:PC13G06600-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c13.
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:UP000000724};
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 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; 106027 MW; 4E0702C0EAEBC4FB CRC64;
MSSMRGLVQF IADLRNARAR ELEEKRVNKE LANIRQKFKS GNLNGYQKKK YVCKLLYVYI
QGYDVDFGHL EAVNLISSSK YSEKQIGYLA VTLFLHEEHE LLHLVVNSIR KDLLDHHELN
NCLALHAVAN VGGRELGEAL 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 TTIVHGTRTG SGNAPASPAS
ASNAASASGD LAGLDLSGPS APAPNMASAA HLTPEWDIGY NRLFFSREGV LFEDAQIQVG
LRSEYRGPMG VLKLYISNKS TYAIGSLTTT VDNPASPQLK IDTKNLPEPT IPAAGQTQQT
LFCTAHGPFT DAPTIRISYL AGALQAYTLQ LPVLMHRYME SSSLSAEEFF KRWRQIGGGP
LECQKTFGLL GKNKTINERF TRKIVEGFSF KILDGVDPNA QNIVGCAVYQ FEGGKTGCLL
RLEPNYEKKM YRVTIRATQE EVPQALARQM ELKLAQGMRA DEAFD
//
