ID   AP2A2_DICDI             Reviewed;         989 AA.
AC   Q86KI1; Q557K4; Q557L6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=AP-2 complex subunit alpha-2;
DE   AltName: Full=100 kDa coated vesicle protein C;
DE   AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE   AltName: Full=Adaptor-related protein complex 2 subunit alpha-2;
DE   AltName: Full=Alpha-adaptin C;
DE   AltName: Full=Alpha2-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE   AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN   Name=ap2a1-1; ORFNames=DDB_G0273439;
GN   and
GN   Name=ap2a1-2; ORFNames=DDB_G0273501;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Component of the adaptor complexes which link clathrin to
CC       receptors in coated vesicles. Clathrin-associated protein complexes are
CC       believed to interact with the cytoplasmic tails of membrane proteins,
CC       leading to their selection and concentration (By similarity).
CC       {ECO:0000250}.
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 AP50) and a small adaptin (sigma-type subunit
CC       AP17).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles in the plasma membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000010; EAL70705.2; -; Genomic_DNA.
DR   EMBL; AAFI02000010; EAL70674.1; -; Genomic_DNA.
DR   RefSeq; XP_644619.1; XM_639527.1.
DR   RefSeq; XP_644631.2; XM_639539.2.
DR   AlphaFoldDB; Q86KI1; -.
DR   SMR; Q86KI1; -.
DR   STRING; 44689.DDB0234235; -.
DR   PaxDb; Q86KI1; -.
DR   EnsemblProtists; EAL70674; EAL70674; DDB_G0273439.
DR   EnsemblProtists; EAL70705; EAL70705; DDB_G0273501.
DR   GeneID; 8618983; -.
DR   GeneID; 8618994; -.
DR   KEGG; ddi:DDB_G0273439; -.
DR   KEGG; ddi:DDB_G0273501; -.
DR   dictyBase; DDB_G0273439; ap2a1-1.
DR   dictyBase; DDB_G0273501; ap2a1-2.
DR   eggNOG; KOG1077; Eukaryota.
DR   HOGENOM; CLU_003824_1_0_1; -.
DR   InParanoid; Q86KI1; -.
DR   OMA; SPIEQFM; -.
DR   PhylomeDB; Q86KI1; -.
DR   Reactome; R-DDI-437239; Recycling pathway of L1.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-DDI-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-DDI-8964038; LDL clearance.
DR   PRO; PR:Q86KI1; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IDA:dictyBase.
DR   GO; GO:0030132; C:clathrin coat of coated pit; IDA:dictyBase.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:dictyBase.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR   GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0009992; P:cellular water homeostasis; IMP:dictyBase.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR   GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.30.310.10; -; 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   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; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Coated pit; Endocytosis; Lipid-binding; Membrane;
KW   Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..989
FT                   /note="AP-2 complex subunit alpha-2"
FT                   /id="PRO_0000328675"
FT   REPEAT          112..149
FT                   /note="HEAT 1"
FT   REPEAT          188..225
FT                   /note="HEAT 2"
FT   REPEAT          368..402
FT                   /note="HEAT 3"
FT   REPEAT          403..440
FT                   /note="HEAT 4"
FT   REGION          610..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        614
FT                   /note="T -> S (in Ref. 1; EAL70705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        617..618
FT                   /note="NT -> GS (in Ref. 1; EAL70705)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   989 AA;  110700 MW;  45942B42F8DB1017 CRC64;
     MSMNVTNPNI AKTSMRGLTN FISDLRNSPS KENEEKRVTK EMAHIRKEFK ENKNIDGYQR
     RKYVCKLVYM YMLGYELDFG HMEAVTLLSS TKFSEKQIGY IALGILLNEQ HEMLPLIINS
     FKEDLLARSD YFQSLALAAI CNIGGKEVAE FLSPLIQKLL IANTSSPMVK KRCALAILRM
     NRKHIGLVTP DSWVERLVSV LDEPDFGVLT SLMSLLIELA SENPIGWEPA IPKVIHLLKK
     IIINKEFPKE YVYYHVTCPW LQVKLLKFLR YFPAPDDSQG GKVLGEILTA VFAQSESAKA
     GTVNHKNSLN AVLFEAINLI IHLDNDPVLL KQTSLLLGRF ITVKETNIRY LGLEAMSHFA
     SLSNETSIMI KKYQDTVLLS LKDSDISIRR RALDLLYGMC DKNTCKHIVA ELLSYLQTAD
     YAIREELVIK IANLAEKFAS NYSWYVDVIL QLITTAGDFV SDDIWFRVVK IVTNHEDIQA
     YAASTVFNAL QSRNCHETLI KVGGYILGEF GHLIADNPQS SPLVQFNILH SKFNTCGAPT
     KALLLSTYAK FVNLFPELTQ QTQEVFKQHQ SYIDAEIQQR ACEYLNLTSL NEDLMQTVLD
     VIPAFIDAKD NSNTTSNTAN NSNMINSQDS KISSGGFNQS PQPSQQQQQQ QPPQQQQAQL
     QQNVSSNGLD LLDPFGLGLG NQQQQQQQPV QQAQPVYQQQ QQAESFSPVQ SDTVSSFGQQ
     QQQQQGGFSS PTIQASSSPI SSGGSDPMQI KILASYKRLC LVSEGVLYED SMLQVGLKSE
     YQSGQGRLML YYGNSSAFPL TNFNVTLNSI AGLTLQPQSI APVIQPKAQL QQPVTFSCTS
     EFTESPVITI NFLTPGKPIT ITLRLPIVIS KFFEPLRLSS GDFFARWKTI SGKPLEIQEI
     FKSTKPIDIQ SYNRVIQEGL NITVLKQVDP NPNNIVASCL FPFGSNGQPI NSYIRIETNP
     QANMCRLTIR SQSATLTNTI KNLLISHLQ