AP3M_ARATH
ID AP3M_ARATH Reviewed; 415 AA.
AC F4I562; Q9FXB1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=AP-3 complex subunit mu;
DE AltName: Full=Adaptor protein complex AP-3 subunit mu;
DE AltName: Full=Adaptor protein-3 mu-adaptin;
DE AltName: Full=Adaptor-related protein complex 3 subunit mu;
DE AltName: Full=At-muD-Ad;
DE AltName: Full=Mu3-adaptin;
DE AltName: Full=Protein ZIG SUPPRESSOR 4;
GN Name=AP3M; Synonyms=ZIP4; OrderedLocusNames=At1g56590; ORFNames=F25P12.96;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-415.
RA Wrobel R.L., Kimball T.L., Riters M.A., Steffen E., Thao S., Aceti D.J.,
RA Blommel P.G., Newman C.S., Zhao Q., Fox B.G., Phillips G.N. Jr.,
RA Markley J.L.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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.
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).
RN [7]
RP DISRUPTION PHENOTYPE, AND MUTANT ZIP4.
RX PubMed=19884248; DOI=10.1093/pcp/pcp137;
RA Niihama M., Takemoto N., Hashiguchi Y., Tasaka M., Morita M.T.;
RT "ZIP genes encode proteins involved in membrane trafficking of the TGN-
RT PVC/vacuoles.";
RL Plant Cell Physiol. 50:2057-2068(2009).
RN [8]
RP MUTAGENESIS OF 398-LEU--LEU-415, FUNCTION, AND COMPONENT OF THE AP-3
RP COMPLEX.
RX PubMed=21670741; DOI=10.1038/cr.2011.99;
RA Zwiewka M., Feraru E., Moeller B., Hwang I., Feraru M.I., Kleine-Vehn J.,
RA Weijers D., Friml J.;
RT "The AP-3 adaptor complex is required for vacuolar function in
RT Arabidopsis.";
RL Cell Res. 21:1711-1722(2011).
RN [9]
RP REVIEW.
RX PubMed=22253225; DOI=10.1105/tpc.111.090415;
RA Wolfenstetter S., Wirsching P., Dotzauer D., Schneider S., Sauer N.;
RT "Routes to the tonoplast: the sorting of tonoplast transporters in
RT Arabidopsis mesophyll protoplasts.";
RL Plant Cell 24:215-232(2012).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which
CC seems to be clathrin-associated. The complex is associated with the
CC Golgi region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to the vacuole. It also functions in
CC maintaining the identity of lytic vacuoles and in regulating the
CC transition between storage and lytic vacuoles.
CC {ECO:0000269|PubMed:21670741}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit).
CC -!- INTERACTION:
CC F4I562; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25519891, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus.
CC Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the
CC coat surrounding the cytoplasmic face of coated vesicles located at the
CC Golgi complex. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced gravitropic response.
CC {ECO:0000269|PubMed:19884248}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09104.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009323; AAG09104.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33412.1; -; Genomic_DNA.
DR EMBL; BX814222; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT015502; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F96607; F96607.
DR RefSeq; NP_176052.3; NM_104536.5.
DR AlphaFoldDB; F4I562; -.
DR SMR; F4I562; -.
DR BioGRID; 27338; 4.
DR IntAct; F4I562; 1.
DR STRING; 3702.AT1G56590.1; -.
DR PaxDb; F4I562; -.
DR PRIDE; F4I562; -.
DR ProteomicsDB; 244407; -.
DR DNASU; 842113; -.
DR EnsemblPlants; AT1G56590.1; AT1G56590.1; AT1G56590.
DR GeneID; 842113; -.
DR Gramene; AT1G56590.1; AT1G56590.1; AT1G56590.
DR KEGG; ath:AT1G56590; -.
DR Araport; AT1G56590; -.
DR TAIR; locus:2027564; AT1G56590.
DR eggNOG; KOG2740; Eukaryota.
DR HOGENOM; CLU_026996_6_2_1; -.
DR OMA; WDIGRID; -.
DR OrthoDB; 928391at2759; -.
DR PRO; PR:F4I562; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I562; baseline and differential.
DR Genevisible; F4I562; AT.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
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 Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..415
FT /note="AP-3 complex subunit mu"
FT /id="PRO_0000424263"
FT DOMAIN 178..414
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT MUTAGEN 398..415
FT /note="Missing: Affects vacuolar morphology; defective
FT lytic vacuoles with altered morphology and accumulation of
FT proteins."
FT /evidence="ECO:0000269|PubMed:21670741"
SQ SEQUENCE 415 AA; 46313 MW; 764A3AC60970D21A CRC64;
MLQCIFLISD SGEVMLEKQL TGHRVDRSIC AWFWDQYISQ GDSFKALPVI ASPTHYLFQI
VRDGITFLAC SQVEMPPLMA IEFLCRVADV LSEYLGGLNE DLIKDNFIIV YELLDEMIDN
GFPLTTEPSI LKEMIAPPNL VSKMLSVVTG NASNVSDTLP SGAGSCVPWR PTDPKYSSNE
VYVDLVEEMD AIVNRDGELV KCEIYGEVQM NSQLTGFPDL TLSFANPSIL EDMRFHPCVR
YRPWESHQVL SFVPPDGEFK LMSYRVKKLK NTPVYVKPQI TSDSGTCRIS VLVGIRSDPG
KTIESITLSF QLPHCVSSAD LSSNHGTVTI LSNKTCTWTI GRIPKDKTPC LSGTLALEPG
LERLHVFPTF KLGFKIMGIA LSGLRIEKLD LQTIPPRLYK GFRAQTRAGE FDVRL
