AP2A1_ARATH
ID AP2A1_ARATH Reviewed; 1012 AA.
AC Q8LPL6; C0Z243; C0Z347; Q9FNI4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=AP-2 complex subunit alpha-1;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
DE AltName: Full=Adaptor-related protein complex 2 subunit alpha-1;
DE AltName: Full=Alpha-adaptin 1;
DE AltName: Full=Clathrin assembly protein complex 2 alpha large chain 1;
DE Short=At-a-Ad;
DE Short=At-alpha-Ad;
GN Name=ALPHA-ADR; OrderedLocusNames=At5g22770; ORFNames=MDJ22.19;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
RP INTERACTION WITH EPSIN2.
RX PubMed=17277094; DOI=10.1104/pp.106.095349;
RA Lee G.-J., Kim H., Kang H., Jang M., Lee D.W., Lee S., Hwang I.;
RT "EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and
RT phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in
RT protein trafficking in plant cells.";
RL Plant Physiol. 143:1561-1575(2007).
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 (By similarity). {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) and a small adaptin (sigma-type subunit) (By
CC similarity). Binds to EPSIN2. {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8LPL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LPL6-2; Sequence=VSP_039697;
CC Name=3;
CC IsoId=Q8LPL6-3; Sequence=VSP_039697, VSP_039698, VSP_039699;
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11683.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB006699; BAB11683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB024030; BAB11683.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED93072.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93073.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93074.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69277.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69278.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69279.1; -; Genomic_DNA.
DR EMBL; AY099568; AAM20420.1; -; mRNA.
DR EMBL; AK318657; BAH56772.1; -; mRNA.
DR EMBL; AK319011; BAH57126.1; -; mRNA.
DR RefSeq; NP_001330969.1; NM_001343764.1. [Q8LPL6-1]
DR RefSeq; NP_001330970.1; NM_001343762.1. [Q8LPL6-1]
DR RefSeq; NP_001330971.1; NM_001343763.1. [Q8LPL6-1]
DR RefSeq; NP_197669.1; NM_122183.3. [Q8LPL6-1]
DR RefSeq; NP_851057.1; NM_180726.2. [Q8LPL6-1]
DR RefSeq; NP_851058.1; NM_180727.2. [Q8LPL6-1]
DR AlphaFoldDB; Q8LPL6; -.
DR SMR; Q8LPL6; -.
DR BioGRID; 17615; 13.
DR IntAct; Q8LPL6; 3.
DR STRING; 3702.AT5G22770.1; -.
DR PaxDb; Q8LPL6; -.
DR PRIDE; Q8LPL6; -.
DR ProteomicsDB; 244991; -. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.1; AT5G22770.1; AT5G22770. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.2; AT5G22770.2; AT5G22770. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.3; AT5G22770.3; AT5G22770. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.4; AT5G22770.4; AT5G22770. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.5; AT5G22770.5; AT5G22770. [Q8LPL6-1]
DR EnsemblPlants; AT5G22770.6; AT5G22770.6; AT5G22770. [Q8LPL6-1]
DR GeneID; 832340; -.
DR Gramene; AT5G22770.1; AT5G22770.1; AT5G22770. [Q8LPL6-1]
DR Gramene; AT5G22770.2; AT5G22770.2; AT5G22770. [Q8LPL6-1]
DR Gramene; AT5G22770.3; AT5G22770.3; AT5G22770. [Q8LPL6-1]
DR Gramene; AT5G22770.4; AT5G22770.4; AT5G22770. [Q8LPL6-1]
DR Gramene; AT5G22770.5; AT5G22770.5; AT5G22770. [Q8LPL6-1]
DR Gramene; AT5G22770.6; AT5G22770.6; AT5G22770. [Q8LPL6-1]
DR KEGG; ath:AT5G22770; -.
DR Araport; AT5G22770; -.
DR TAIR; locus:2162419; AT5G22770.
DR eggNOG; KOG1077; Eukaryota.
DR HOGENOM; CLU_003824_1_0_1; -.
DR InParanoid; Q8LPL6; -.
DR OMA; SPIEQFM; -.
DR OrthoDB; 751651at2759; -.
DR PhylomeDB; Q8LPL6; -.
DR PRO; PR:Q8LPL6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LPL6; baseline and differential.
DR Genevisible; Q8LPL6; AT.
DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
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 Alternative splicing; Coated pit; Endocytosis; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1012
FT /note="AP-2 complex subunit alpha-1"
FT /id="PRO_0000397846"
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 525..565
FT /note="HEAT 4"
FT DOMAIN 742..841
FT /note="GAE"
FT REGION 652..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 653
FT /note="T -> TQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039697"
FT VAR_SEQ 912..931
FT /note="DPNPNNLVASTTFYSESTGA -> VSICLRSHSSCLLHTCILQT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039698"
FT VAR_SEQ 932..1012
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039699"
FT CONFLICT 609
FT /note="E -> G (in Ref. 5; BAH56772)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="P -> L (in Ref. 5; BAH57126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 112150 MW; 01E16E8A1DB0280D 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 KAREYLDKIA
IHETMVKVSA YILGEYGHLL ARQPGCSASE LFSILHEKLP TISTPTIPIL LSTYAKLLMH
AQPPDPELQK KVWAVFKKYE SCIDVEIQQR AVEYFELSKK GPAFMDVLAE MPKFPERQSS
LIKKAENVED TADQSAIKLR AQQQPSNAMV LADQQPVNGA PPPLKVPILS GSTDPESVAR
SLSHPNGTLS NIDPQTPSPD LLSDLLGPLA IEAPPGAVSN EQHGPVGAEG VPDEVDGSAI
VPVEEQTNTV ELIGNIAERF HALCLKDSGV LYEDPHIQIG IKAEWRGHHG RLVLFMGNKN
TSPLTSVQAL ILPPAHLRLD LSPVPDTIPP RAQVQSPLEV MNIRPSRDVA VLDFSYKFGA
NVVSAKLRIP ATLNKFLQPL QLTSEEFFPQ WRAISGPPLK LQEVVRGVRP LALPEMANLF
NSFHVTICPG LDPNPNNLVA STTFYSESTG AILCLARIET DPADRTQLRM TVGTGDPTLT
FELKEFIKEQ LITVPMGSRA LVPAAGPAPP VAQPPSPAAL ADDPGAMLAG LL
