AP2A2_ARATH
ID AP2A2_ARATH Reviewed; 1013 AA.
AC Q8LPK4; Q9FGT0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=AP-2 complex subunit alpha-2;
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 2;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE Short=At-aC-Ad;
DE Short=At-alphaC-Ad;
GN Name=ALPHAC-AD; OrderedLocusNames=At5g22780; ORFNames=K5A21.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND REVIEW.
RX PubMed=11598180; DOI=10.1091/mbc.12.10.2907;
RA Boehm M., Bonifacino J.S.;
RT "Adaptins: the final recount.";
RL Mol. Biol. Cell 12:2907-2920(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH AP180.
RX PubMed=15054111; DOI=10.1242/jcs.01062;
RA Barth M., Holstein S.E.;
RT "Identification and functional characterization of Arabidopsis AP180, a
RT binding partner of plant alphaC-adaptin.";
RL J. Cell Sci. 117:2051-2062(2004).
CC -!- FUNCTION: Subunit of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The complex binds
CC polyphosphoinositides. {ECO:0000269|PubMed:15054111}.
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) (By
CC similarity). Interacts with AP180. {ECO:0000250,
CC ECO:0000269|PubMed:15054111}.
CC -!- INTERACTION:
CC Q8LPK4; Q9ZVN6: AP180; NbExp=2; IntAct=EBI-2366827, EBI-2366853;
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles in the plasma membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10137.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024030; BAB10137.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB025618; BAB10137.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED93075.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68365.1; -; Genomic_DNA.
DR EMBL; AY099646; AAM20497.1; -; mRNA.
DR RefSeq; NP_001330127.1; NM_001343765.1.
DR RefSeq; NP_197670.1; NM_122184.4.
DR AlphaFoldDB; Q8LPK4; -.
DR SMR; Q8LPK4; -.
DR BioGRID; 17616; 9.
DR IntAct; Q8LPK4; 1.
DR STRING; 3702.AT5G22780.1; -.
DR PaxDb; Q8LPK4; -.
DR PRIDE; Q8LPK4; -.
DR ProteomicsDB; 240323; -.
DR EnsemblPlants; AT5G22780.1; AT5G22780.1; AT5G22780.
DR EnsemblPlants; AT5G22780.2; AT5G22780.2; AT5G22780.
DR GeneID; 832341; -.
DR Gramene; AT5G22780.1; AT5G22780.1; AT5G22780.
DR Gramene; AT5G22780.2; AT5G22780.2; AT5G22780.
DR KEGG; ath:AT5G22780; -.
DR Araport; AT5G22780; -.
DR TAIR; locus:2157510; AT5G22780.
DR eggNOG; KOG1077; Eukaryota.
DR HOGENOM; CLU_003824_1_0_1; -.
DR InParanoid; Q8LPK4; -.
DR OMA; PINILRY; -.
DR OrthoDB; 751651at2759; -.
DR PhylomeDB; Q8LPK4; -.
DR PRO; PR:Q8LPK4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPK4; baseline and differential.
DR Genevisible; Q8LPK4; AT.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Coated pit; Endocytosis; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..1013
FT /note="AP-2 complex subunit alpha-2"
FT /id="PRO_0000397847"
FT REPEAT 254..289
FT /note="HEAT 1"
FT REPEAT 354..391
FT /note="HEAT 2"
FT REPEAT 393..430
FT /note="HEAT 3"
FT REPEAT 521..565
FT /note="HEAT 4"
FT DOMAIN 742..841
FT /note="GAE"
FT REGION 652..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..1013
FT /note="Required for AP180 binding"
FT COMPBIAS 654..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 112299 MW; 91A317D5EDD77C25 CRC64;
MTGMRGLSVF ISDVRNCQNK EAERLRVDKE LGNIRTCFKN EKVLTPYKKK KYVWKMLYIH
MLGYDVDFGH MEAVSLISAP KYPEKQVGYI VTSCLLNENH DFLKLAINTV RNDIIGRNET
FQCLALTLVG NIGGRDFAES LAPDVQKLLI SSSCRPLVRK KAALCLLRLF RKNPDAVNVD
GWADRMAQLL DERDLGVLTS STSLLVALVS NNHEAYSSCL PKCVKILERL ARNQDVPQEY
TYYGIPSPWL QVKAMRALQY FPTIEDPSTR KALFEVLQRI LMGTDVVKNV NKNNASHAVL
FEALSLVMHL DAEKEMMSQC VALLGKFISV REPNIRYLGL ENMTRMLMVT DVQDIIKKHQ
SQIITSLKDP DISIRRRALD LLYGMCDVSN AKDIVEELLQ YLSTAEFSMR EELSLKAAIL
AEKFAPDLSW YVDVILQLID KAGDFVSDDI WFRVVQFVTN NEDLQPYAAS KAREYMDKIA
IHETMVKVSA YILGEYGHLL ARQPGCSASE LFSILHEKLP TVSTPTIPIL LSTYAKLLMH
AQPPDPELQK KVWAVFKKYE SCIDVEIQQR AVEYFELSKK GPAFMDVLAE MPKFPERQSS
LIKKAENVED TADQSAIKLR AQQQPSNAIV LADPQPVNGA PPPLKVPILS GSTDPESVAR
SLSHPNGTLS NIDPQTPSPD LLSDLLGPLA IEAPPGAVSY EQHGPVGAEG VPDEIDGSAI
VPVEEQTNTV ELIGNIAERF HALCLKDSGV LYEDPHIQIG IKAEWRGHHG RLVLFMGNKN
TSPLTSVQAL ILPPAHLRLD LSPVPDTIPP RAQVQSPLEV MNIRPSRDVA VLDFSYKFGT
NVVSAKLRIP ATLNKFLQPL QLTSEEFFPQ WRAISGPPLK LQEVVRGVRP LALPEMANLF
NSFHVTICPG LDPNPNNLVA STTFYSETTG AMLCLARIET DPADRTQLRL TVGSGDPTLT
FELKEFIKEQ LITIPMGSRA LVPAAGPAPS PAVQPPSPAA LADDPGAMLA GLL
