AP1M2_ARATH
ID AP1M2_ARATH Reviewed; 428 AA.
AC O22715;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=AP-1 complex subunit mu-2;
DE AltName: Full=Adaptor protein complex AP-1 subunit mu-2;
DE AltName: Full=Adaptor protein-1 mu-adaptin 2;
DE AltName: Full=Adaptor-related protein complex 1 subunit mu-2;
DE AltName: Full=At-muB2-Ad;
DE AltName: Full=Clathrin assembly protein complex 1 mu-2 medium chain;
DE AltName: Full=Mu1-adaptin 2;
DE AltName: Full=Protein HAPLESS 13;
GN Name=AP1M2; Synonyms=HAP13; OrderedLocusNames=At1g60780; ORFNames=F8A5.29;
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=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 [4]
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15514068; DOI=10.1534/genetics.104.029447;
RA Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D.,
RA Levin J.Z., Preuss D.;
RT "Arabidopsis hapless mutations define essential gametophytic functions.";
RL Genetics 168:971-982(2004).
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE AP-1 COMPLEX.
RX PubMed=23543752; DOI=10.1093/pcp/pct048;
RA Teh O.K., Shimono Y., Shirakawa M., Fukao Y., Tamura K., Shimada T.,
RA Hara-Nishimura I.;
RT "The AP-1 mu adaptin is required for KNOLLE localization at the cell plate
RT to mediate cytokinesis in Arabidopsis.";
RL Plant Cell Physiol. 54:838-847(2013).
RN [8]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION,
RP AND COMPONENT OF THE AP-1 COMPLEX.
RX PubMed=23766365; DOI=10.1104/pp.113.221051;
RA Wang J.G., Li S., Zhao X.Y., Zhou L.Z., Huang G.Q., Feng C., Zhang Y.;
RT "HAPLESS13, the Arabidopsis mu1 adaptin, is essential for protein sorting
RT at the trans-Golgi network/early endosome.";
RL Plant Physiol. 162:1897-1910(2013).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, COMPONENT OF THE AP-1 COMPLEX, AND
RP SUBCELLULAR LOCATION.
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. Required for KNOLLE
CC localization at the cell plate to mediate cytokinesis. Functions
CC redundantly with AP1M1 in multiple post-Golgi trafficking pathways
CC leading from the TGN to the vacuole, the plasma membrane, and the cell-
CC division plane. {ECO:0000269|PubMed:23543752,
CC ECO:0000269|PubMed:23733933, ECO:0000269|PubMed:23766365}.
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, trans-Golgi network membrane
CC {ECO:0000269|PubMed:23543752, ECO:0000269|PubMed:23733933,
CC ECO:0000269|PubMed:23766365}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11598180}; Cytoplasmic side
CC {ECO:0000305|PubMed:11598180}. Early endosome membrane
CC {ECO:0000269|PubMed:23766365}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11598180}; Cytoplasmic side
CC {ECO:0000305|PubMed:11598180}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000305|PubMed:23733933}; Peripheral membrane
CC protein {ECO:0000305|PubMed:11598180}; Cytoplasmic side
CC {ECO:0000305|PubMed:11598180}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:23543752,
CC ECO:0000269|PubMed:23766365}.
CC -!- DISRUPTION PHENOTYPE: Short pollen tube growth and failure to exit the
CC style (PubMed:15514068). Compromised cytokinesis due to the
CC mislocalization of the KNOLLE syntaxin (PubMed:23543752,
CC PubMed:23733933). Full spectrum of growth defects, suggestive of
CC compromised auxin signaling and of defective RLK signaling. Cell
CC morphogenesis was also disturbed (PubMed:23766365). Impaired pollen
CC function and growth retardation phenotype (PubMed:23733933).
CC {ECO:0000269|PubMed:15514068, ECO:0000269|PubMed:23543752,
CC ECO:0000269|PubMed:23733933, ECO:0000269|PubMed:23766365}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AC002292; AAB71967.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33731.1; -; Genomic_DNA.
DR EMBL; AY099652; AAM20503.1; -; mRNA.
DR EMBL; BT002144; AAN72155.1; -; mRNA.
DR PIR; C96633; C96633.
DR RefSeq; NP_176277.1; NM_104761.4.
DR AlphaFoldDB; O22715; -.
DR SMR; O22715; -.
DR BioGRID; 27596; 18.
DR STRING; 3702.AT1G60780.1; -.
DR iPTMnet; O22715; -.
DR PaxDb; O22715; -.
DR PRIDE; O22715; -.
DR ProMEX; O22715; -.
DR ProteomicsDB; 240598; -.
DR EnsemblPlants; AT1G60780.1; AT1G60780.1; AT1G60780.
DR GeneID; 842372; -.
DR Gramene; AT1G60780.1; AT1G60780.1; AT1G60780.
DR KEGG; ath:AT1G60780; -.
DR Araport; AT1G60780; -.
DR TAIR; locus:2036606; AT1G60780.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_0_0_1; -.
DR InParanoid; O22715; -.
DR OMA; CRAKAQI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; O22715; -.
DR PRO; PR:O22715; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22715; baseline and differential.
DR Genevisible; O22715; AT.
DR GO; GO:0030121; C:AP-1 adaptor complex; IPI:TAIR.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; IMP:TAIR.
DR GO; GO:0035653; P:clathrin-coated vesicle cargo loading, AP-1-mediated; IPI:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IMP:TAIR.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:TAIR.
DR GO; GO:0007034; P:vacuolar transport; IMP:TAIR.
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; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..428
FT /note="AP-1 complex subunit mu-2"
FT /id="PRO_0000424260"
FT DOMAIN 170..426
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ SEQUENCE 428 AA; 49032 MW; 1C3C18CF06919C4F CRC64;
MAGAASALFL LDIKGRVLVW RDYRGDVSAA QAERFFTKLI EKEGDSQSND PVAYDNGVTY
MFVQHSNVYL MIASRQNCNA ASLLFFLHRV VDVFKHYFEE LEEESLRDNF VVVYELLDEM
MDFGYPQYTE ARILSEFIKT DAYRMEVTQR PPMAVTNAVS WRSEGIQYKK NEVFLDVIEN
VNILVNSNGQ IVRSDVVGAL KMRTYLTGMP ECKLGLNDRV LLEAQGRATK GKAIDLEDIK
FHQCVRLARF ENDRTISFIP PDGAFDLMTY RLSTQVKPLI WVEAQIESHS RSRVEMLIKA
RSQFKERSTA TNVEIELPVP TDASNPTVRT SLGSASYAPE KDALVWKIKS FPGNKEYMLR
AEFHLPSITA EEATPERKAP IRVKFEIPYF TVSGIQVRYL KIIEKSGYQA LPWVRYITMA
GEYELRLV
