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Database: UniProt
Entry: A0A0J7KSA5_LASNI
LinkDB: A0A0J7KSA5_LASNI
Original site: A0A0J7KSA5_LASNI 
ID   A0A0J7KSA5_LASNI        Unreviewed;       945 AA.
AC   A0A0J7KSA5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   RecName: Full=AP-2 complex subunit alpha {ECO:0000256|PIRNR:PIRNR037091};
GN   ORFNames=RF55_6671 {ECO:0000313|EMBL:KMQ93233.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ93233.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ93233.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ93233.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KMQ93233.1}.
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DR   EMBL; LBMM01003688; KMQ93233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7KSA5; -.
DR   STRING; 67767.A0A0J7KSA5; -.
DR   PaxDb; 67767-A0A0J7KSA5; -.
DR   OrthoDB; 25313at2759; -.
DR   Proteomes; UP000036403; 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:UP000036403};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037091}.
FT   DOMAIN          706..819
FT                   /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT                   Ig-like subdomain"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   REGION          623..642
FT                   /note="Disordered"
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   945 AA;  105743 MW;  24ADF4ECA2A44539 CRC64;
     MPAVRGDGMR GLAVFISDIR NCKSKEAEIK RINKELANIR SKFKGDKTLD GYQKKKYVCK
     LLFIFLLGHD IDFGHMEAVN LLSSNKYSEK QIGYLFISVL VNTNSDLIKL IIQSIKNDLG
     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 ENKSPAPNAN HHAEAPTTVT VAAVNNSSAD
     LLGLSTPPSS QPSSNTGVLL DVLGDIYNMP NRVGATNGTQ NTYNPKKFVC KNNGVLFESD
     LIQIGVKSEF RQNLGRIGLF YGNKTQYALH SFQPQLSWTD ENQAKLAVQV KPVDPILEAG
     AQIQQMINAE CIDDYNDAPN MIISFIYNNV PQKITMKLPL TINKFFEPTE MNGESFFARW
     KNLGGANQQR SQKIFKAQQP MDLAQVRTKL QGFGMQLLDG IDPNPDNFVC AGIVHMRAQQ
     VGCLLRLEPN KQAQVTGQIP MFRLTVRSSK ESMSVEICDL LVDQF
//
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