ID A0A158NWA4_ATTCE Unreviewed; 940 AA.
AC A0A158NWA4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN Name=105625076 {ECO:0000313|EnsemblMetazoa:XP_012061812.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012061812.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012061812.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- FUNCTION: Adaptins are components of the adapter complexes which link
CC clathrin to receptors in coated vesicles.
CC {ECO:0000256|PIRNR:PIRNR037091}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type and beta-type subunits), a medium
CC adaptin (mu-type subunit) and a small adaptin (sigma-type subunit).
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; ADTU01002959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012061812.1; XM_012206422.1.
DR AlphaFoldDB; A0A158NWA4; -.
DR STRING; 12957.A0A158NWA4; -.
DR EnsemblMetazoa; XM_012206422.1; XP_012061812.1; LOC105625076.
DR GeneID; 105625076; -.
DR KEGG; acep:105625076; -.
DR eggNOG; KOG1077; Eukaryota.
DR InParanoid; A0A158NWA4; -.
DR OrthoDB; 25313at2759; -.
DR Proteomes; UP000005205; 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:UP000005205};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT DOMAIN 707..820
FT /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT Ig-like subdomain"
FT /evidence="ECO:0000259|SMART:SM00809"
FT REGION 623..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..11
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 42
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 52
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 56..60
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 940 AA; 105367 MW; FFE8E30CE26B444E CRC64;
MPAVRGDGMR GLAVFISDIR NCKSKEAEIK RINKELANIR SKFKGDKTLD GYQKKKYVCK
LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIKL IIQSIKNDLA
SRNPIHVNLA LQCIANIGSK EMAEAFGNEI PKLLVSGDTM DVVKQSAALC LLRLLRTAPD
VVPGGEWTSR IVHLLNDQHL GVVTAAASLI DALVKRNPDE YKGCVSLAVS RLSRIVTSSY
TDLQDYTYYF VPAPWLSVKL LRLLQNYTPP AEDPGVRGRL NECLETILNK AQEPPKSKKV
QHSNAKNAVL FEAISLIIHN DSEPNLLVRA CNQLGQFLSN RETNLRYLAL ESMCHLATSE
FSHEAVKKHQ EVVILSMKME KDVSVRQQAV DLLYAMCDKS NAEEIVQEML NYLETADYSI
REEMVLKVAI LAEKYATDYT WYVDVILNLI RIAGDYVSEE VWYRVIQIVI NRDDVQGYAA
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDQRSSPA VQFQLLHSKY HLCSPMTRAL
LLSTYIKFVN LFPEIRSQIQ DVFRQHSNLR SADAELQQRA SEYLQLSIIA STDVLATVLE
EMPAFPERES SILAVLKKKK PGRVPENEIR ESKSPAPNTN HHTEPPPTAA TTVTVNNSSA
DLLGLSTPPS SQPSSNTGVL LDVLGDIYNM PNKLGTTNGT QNTYNPKKFV CKNNGVLFEN
DLIQIGVKSE FRQNLGRVGL FYGNKTQYAL HSFQPQLSWT DENQAKLAVQ VKPVDPILEA
GAQIQQMINA ECIDDYNDSP SMIISFIYNN VPQKITMKLP LTINKFFEPT EMNGESFFAR
WKNLGGANQQ RSQKIFKAQQ PMDLTQVRTK LQGFGMQLLD GIDPNPDNFV CAGIVHMRAQ
QVGCLLRLEP NKQAQMFRLT VRSSKESMSV EICDLLVDQF
//
