ID   AP1M1_ARATH             Reviewed;         428 AA.
AC   Q9SAC9; Q9SGX7;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=AP-1 complex subunit mu-1;
DE   AltName: Full=Adaptor protein complex AP-1 subunit mu-1;
DE   AltName: Full=Adaptor protein-1 mu-adaptin 1;
DE   AltName: Full=Adaptor-related protein complex 1 subunit mu-1;
DE   AltName: Full=At-muB1-Ad;
DE   AltName: Full=Clathrin assembly protein complex 1 mu-1 medium chain;
DE   AltName: Full=Mu1-adaptin 1;
GN   Name=AP1M1; OrderedLocusNames=At1g10730; ORFNames=F20B24.16, T16B5.13;
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   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   [4]
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   [5]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND COMPONENT OF THE AP-1 COMPLEX.
RX   PubMed=23733933; DOI=10.1073/pnas.1300460110;
RA   Park M., Song K., Reichardt I., Kim H., Mayer U., Stierhof Y.D., Hwang I.,
RA   Juergens G.;
RT   "Arabidopsis mu-adaptin subunit AP1M of adaptor protein complex 1 mediates
RT   late secretory and vacuolar traffic and is required for growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:10318-10323(2013).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC       plays a role in protein sorting at the trans-Golgi network and early
CC       endosomes (TGN/EE). The AP complexes mediate the recruitment of
CC       clathrin to membranes and the recognition of sorting signals within the
CC       cytosolic tails of transmembrane cargo molecules. Functions redundantly
CC       with AP1M2 in multiple post-Golgi trafficking pathways leading from the
CC       TGN to the vacuole, the plasma membrane, and the cell-division plane.
CC       {ECO:0000269|PubMed:23733933}.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit and beta-type subunit), a
CC       medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC       subunit).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic
CC       vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Growth retardation phenotype.
CC       {ECO:0000269|PubMed:23733933}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF17661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007354; AAD31340.1; -; Genomic_DNA.
DR   EMBL; AC009398; AAF17661.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28635.1; -; Genomic_DNA.
DR   PIR; G86240; G86240.
DR   RefSeq; NP_172543.1; NM_100949.2.
DR   AlphaFoldDB; Q9SAC9; -.
DR   SMR; Q9SAC9; -.
DR   BioGRID; 22856; 16.
DR   STRING; 3702.AT1G10730.1; -.
DR   PaxDb; Q9SAC9; -.
DR   PRIDE; Q9SAC9; -.
DR   ProteomicsDB; 244473; -.
DR   EnsemblPlants; AT1G10730.1; AT1G10730.1; AT1G10730.
DR   GeneID; 837616; -.
DR   Gramene; AT1G10730.1; AT1G10730.1; AT1G10730.
DR   KEGG; ath:AT1G10730; -.
DR   Araport; AT1G10730; -.
DR   TAIR; locus:2019913; AT1G10730.
DR   eggNOG; KOG0937; Eukaryota.
DR   HOGENOM; CLU_026996_0_0_1; -.
DR   InParanoid; Q9SAC9; -.
DR   OrthoDB; 725236at2759; -.
DR   PhylomeDB; Q9SAC9; -.
DR   PRO; PR:Q9SAC9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAC9; baseline and differential.
DR   Genevisible; Q9SAC9; AT.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; IPR022775; AP_mu_sigma_su.
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   Pfam; PF01217; Clat_adaptor_s; 1.
DR   PIRSF; PIRSF005992; Clathrin_mu; 1.
DR   PRINTS; PR00314; CLATHRINADPT.
DR   SUPFAM; SSF49447; SSF49447; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..428
FT                   /note="AP-1 complex subunit mu-1"
FT                   /id="PRO_0000424261"
FT   DOMAIN          170..426
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   428 AA;  49224 MW;  4187FAF1D86F7DEC CRC64;
     MAGAASALFL LDIKGRVLVW RDYRGDVTAA QAERFFTKLI ETEGDSQSND PVAYDNGVTY
     MFVQHSNIYL MIASRQNCNA ASLLFFLHRV VDVFKHYFEE LEEESLRDNF VVVYELLDEM
     MDFGYPQFTE ARILSEFIKT DAYRMEVTQR PPMAVTNSVS WRSEGLKFKK NEVFLDVIES
     VNILVNSNGQ IVRSDVVGAL KMRTYLSGMP ECKLGLNDRI LLEAQGRAIK GKAIDLEDIK
     FHQCVRLARF ENDRTISFIP PDGSFDLMTY RLSTQVKPLI WVEAHIERHS RSRVEMLVKA
     RSQFKDRSYA TSVEIELPVP TDAYNPDVRT SLGSAAYAPE KDALVWKIQY FYGNKEHTLK
     ADFHLPSIAA EEATPERKAP IRVKFEIPKF IVSGIQVRYL KIIEKSGYQA HPWVRYITMA
     GEYELRLM