Entry euk:AP2A2_DICDI

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   10-MAY-2017, entry version 97.
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; Mycetozoa; Dictyosteliida; 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.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
CC       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       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer
CC       composed of two large adaptins (alpha-type and beta-type
CC       subunits), a medium adaptin (mu-type subunit AP50) and a small
CC       adaptin (sigma-type subunit AP17).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Note=Component of the coat
CC       surrounding the cytoplasmic face of coated vesicles in the plasma
CC       membrane. {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
CC       and AX4. These strains contain a duplication of a segment of 750
CC       kb of chromosome 2 compared to the corresponding sequence in
CC       strain AX2. {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   ProteinModelPortal; Q86KI1; -.
DR   SMR; Q86KI1; -.
DR   STRING; 44689.DDB0234235; -.
DR   PaxDb; Q86KI1; -.
DR   PRIDE; 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   eggNOG; ENOG410XNQE; LUCA.
DR   InParanoid; Q86KI1; -.
DR   KO; K11824; -.
DR   OMA; RYGGAFQ; -.
DR   PhylomeDB; Q86KI1; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   PRO; PR:Q86KI1; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0009992; P:cellular water homeostasis; IMP:dictyBase.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 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; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR013041; Coatomer/clathrin_app_Ig-like.
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; Complete proteome; Endocytosis;
KW   Lipid-binding; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN         1    989       AP-2 complex subunit alpha-2.
FT                                /FTId=PRO_0000328675.
FT   REPEAT      112    149       HEAT 1.
FT   REPEAT      188    225       HEAT 2.
FT   REPEAT      368    402       HEAT 3.
FT   REPEAT      403    440       HEAT 4.
FT   COMPBIAS    645    651       Poly-Gln.
FT   COMPBIAS    654    662       Poly-Gln.
FT   COMPBIAS    682    688       Poly-Gln.
FT   COMPBIAS    698    702       Poly-Gln.
FT   COMPBIAS    719    725       Poly-Gln.
FT   CONFLICT    614    614       T -> S (in Ref. 1; EAL70705).
FT                                {ECO:0000305}.
FT   CONFLICT    617    618       NT -> GS (in Ref. 1; EAL70705).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       764    859       ipfam:Alpha_adaptinC2 [T]
FT   MYHIT        34    590       ipfam:Adaptin_N [T]
FT   MYHIT       872    982       ipfam:Alpha_adaptin_C [T]
FT   MYHIT       757    866       ismart:Alpha_adaptinC2 [T]
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
//