AP2M_ARATH
ID AP2M_ARATH Reviewed; 438 AA.
AC O23140; B9DI54;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=AP-2 complex subunit mu;
DE AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE AltName: Full=Adaptor protein-2 mu-adaptin;
DE AltName: Full=Adaptor-related protein complex 2 subunit mu;
DE AltName: Full=At-muA-Ad;
DE AltName: Full=Clathrin assembly protein complex 2 mu medium chain;
DE AltName: Full=Mu2-adaptin;
DE AltName: Full=Protein AP47/50;
DE Short=AtAP47/50;
GN Name=AP2M; Synonyms=AP47/50; OrderedLocusNames=At5g46630; ORFNames=MZA15.2;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Happel N., Robinson D.G., Holstein S.H.;
RT "An Arabidopsis thaliana cDNA clone is homologous to the micro-adaptins of
RT clathrin-coated vesicle adaptor complexes.";
RL (er) Plant Gene Register PGR97-168(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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] OF 306-438.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
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 [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 GENE FAMILY, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14871308; DOI=10.1111/j.1365-313x.2003.01995.x;
RA Happel N., Hoening S., Neuhaus J.M., Paris N., Robinson D.G.,
RA Holstein S.E.;
RT "Arabidopsis muA-adaptin interacts with the tyrosine motif of the vacuolar
RT sorting receptor VSR-PS1.";
RL Plant J. 37:678-693(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. AP-2 recognizes Y-X-X-Phi
CC endocytosis signal motif within the cytosolic tails of transmembrane
CC cargo molecules. The complex binds polyphosphoinositides.
CC {ECO:0000269|PubMed:14871308}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14871308}.
CC Membrane, coated pit {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network membrane {ECO:0000269|PubMed:14871308}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14871308}; Cytoplasmic side
CC {ECO:0000269|PubMed:14871308}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles in the plasma membrane (By
CC similarity). Detected in the trans-Golgi membrane but not in the
CC plasmamembrane (PubMed:14871308). {ECO:0000250,
CC ECO:0000269|PubMed:14871308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23140-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AF009631; AAB88283.1; -; mRNA.
DR EMBL; AB016882; BAB08907.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95407.1; -; Genomic_DNA.
DR EMBL; AK317765; BAH20421.1; -; mRNA.
DR RefSeq; NP_199475.1; NM_124033.4. [O23140-1]
DR AlphaFoldDB; O23140; -.
DR SMR; O23140; -.
DR BioGRID; 19954; 171.
DR STRING; 3702.AT5G46630.2; -.
DR PaxDb; O23140; -.
DR PRIDE; O23140; -.
DR ProteomicsDB; 246775; -. [O23140-1]
DR EnsemblPlants; AT5G46630.1; AT5G46630.1; AT5G46630. [O23140-1]
DR GeneID; 834706; -.
DR Gramene; AT5G46630.1; AT5G46630.1; AT5G46630. [O23140-1]
DR KEGG; ath:AT5G46630; -.
DR Araport; AT5G46630; -.
DR eggNOG; KOG0938; Eukaryota.
DR HOGENOM; CLU_026996_5_1_1; -.
DR OMA; VEFQVPM; -.
DR PhylomeDB; O23140; -.
DR PRO; PR:O23140; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O23140; baseline and differential.
DR Genevisible; O23140; AT.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd09251; AP-2_Mu2_Cterm; 1.
DR CDD; cd14836; AP2_Mu_N; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR043532; AP2_Mu_N.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR043512; Mu2_C.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Endocytosis;
KW Golgi apparatus; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..438
FT /note="AP-2 complex subunit mu"
FT /id="PRO_0000424262"
FT DOMAIN 177..437
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ SEQUENCE 438 AA; 49322 MW; BF08ED27109CBFF9 CRC64;
MPVAASAIYF LNLRGDVLIN RTYRDDVGGN MVDAFRTHIM QTKELGNCPV RQIGGCSFVY
MRISNVYIVI VVSSNANVAC GFKFVVEAVA LFKSYFGGAF DEDAIRNNFV LIYELLDEIM
DFGYPQNLSP EILKLYITQE GVRSPFSSKP KDKPVPNATL QVTGAVGWRR EGLAYKKNEV
FLDIVESVNL LMSSKGNVLR CDVTGKVLMK CFLSGMPDLK LGLNDKIGLE KESEMKSRPA
KSGKTIELDD VTFHQCVNLT RFNSEKTVSF VPPDGEFELM KYRITEGVNL PFRVLPTIKE
LGRTRMEVNV KVKSVFGAKM FALGVVVKIP VPKQTAKTNF QVTTGRAKYN PSIDCLVWKI
RKFPGQTEST LSAEIELIST MGEKKSWTRP PIQMEFQVPM FTASGLRVRF LKVWEKSGYN
TVEWVRYITK AGSYEIRC
