AP3M_YEAST
ID AP3M_YEAST Reviewed; 483 AA.
AC P38153; D6VQT3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=AP-3 complex subunit mu;
DE AltName: Full=AP-3 adaptor complex mu3A subunit;
DE AltName: Full=Adaptor-related protein complex 3 subunit mu;
DE AltName: Full=Mu-adaptin 3A;
DE AltName: Full=Mu3-adaptin;
GN Name=APM3; Synonyms=YKS6; OrderedLocusNames=YBR288C; ORFNames=YBR2035;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 35-36.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION OF THE AP-3 COMPLEX, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=9335339; DOI=10.1016/s0092-8674(01)80013-1;
RA Cowles C.R., Odorizzi G., Payne G.S., Emr S.D.;
RT "The AP-3 adaptor complex is essential for cargo-selective transport to the
RT yeast vacuole.";
RL Cell 91:109-118(1997).
RN [5]
RP IDENTIFICATION OF THE AP-3 COMPLEX, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=9250663; DOI=10.1093/emboj/16.14.4194;
RA Panek H.R., Stepp J.D., Engle H.M., Marks K.M., Tan P.K., Lemmon S.K.,
RA Robinson L.C.;
RT "Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the
RT four subunits of a novel clathrin AP-like complex.";
RL EMBO J. 16:4194-4204(1997).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE AP-3 COMPLEX.
RX PubMed=10559961; DOI=10.1038/14037;
RA Rehling P., Darsow T., Katzmann D.J., Emr S.D.;
RT "Formation of AP-3 transport intermediates requires Vps41 function.";
RL Nat. Cell Biol. 1:346-353(1999).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is
CC not clathrin-associated. The complex is associated with the Golgi
CC 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. Required for the transport via
CC the ALP pathway, which directs the transport of the cargo proteins PHO8
CC and VAM3 to the vacuole. {ECO:0000269|PubMed:10559961,
CC ECO:0000269|PubMed:9250663, ECO:0000269|PubMed:9335339}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of 2 large adaptins (APL5 and APL6), a medium adaptin (APM3) and a
CC small adaptin (APS3).
CC -!- INTERACTION:
CC P38153; Q08951: APL5; NbExp=4; IntAct=EBI-2710, EBI-29702;
CC P38153; P46682: APL6; NbExp=5; IntAct=EBI-2710, EBI-2213;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10559961,
CC ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10559961, ECO:0000305}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10559961, ECO:0000305}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095, ECO:0000305}. Note=Component of the coat
CC surrounding the cytoplasmic face of coated vesicles located at the
CC Golgi complex. {ECO:0000269|PubMed:10559961, ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; X76053; CAA53651.1; -; Genomic_DNA.
DR EMBL; Z36157; CAA85253.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07403.2; -; Genomic_DNA.
DR PIR; S44550; S44550.
DR RefSeq; NP_009847.4; NM_001178636.4.
DR PDB; 7P3X; EM; 9.10 A; M=1-483.
DR PDB; 7P3Y; EM; 10.10 A; M=1-483.
DR PDB; 7P3Z; EM; 10.50 A; M=1-483.
DR PDBsum; 7P3X; -.
DR PDBsum; 7P3Y; -.
DR PDBsum; 7P3Z; -.
DR AlphaFoldDB; P38153; -.
DR SMR; P38153; -.
DR BioGRID; 32982; 226.
DR ComplexPortal; CPX-535; Adapter complex AP-3.
DR DIP; DIP-4965N; -.
DR IntAct; P38153; 30.
DR MINT; P38153; -.
DR STRING; 4932.YBR288C; -.
DR iPTMnet; P38153; -.
DR MaxQB; P38153; -.
DR PaxDb; P38153; -.
DR PRIDE; P38153; -.
DR EnsemblFungi; YBR288C_mRNA; YBR288C; YBR288C.
DR GeneID; 852591; -.
DR KEGG; sce:YBR288C; -.
DR SGD; S000000492; APM3.
DR VEuPathDB; FungiDB:YBR288C; -.
DR eggNOG; KOG2740; Eukaryota.
DR HOGENOM; CLU_026449_0_0_1; -.
DR InParanoid; P38153; -.
DR OMA; TLNTNFP; -.
DR BioCyc; YEAST:G3O-29207-MON; -.
DR PRO; PR:P38153; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38153; protein.
DR GO; GO:0030123; C:AP-3 adaptor complex; IDA:SGD.
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:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
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; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR SUPFAM; SSF49447; SSF49447; 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 3D-structure; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..483
FT /note="AP-3 complex subunit mu"
FT /id="PRO_0000193794"
FT DOMAIN 211..482
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT CONFLICT 35..36
FT /note="QS -> RT (in Ref. 1; CAA53651 and 2; CAA85253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54837 MW; AAD5A7EA305C63CF CRC64;
MYLSFYITDT KNKLIFQYLL GATAPSFKHL WTRVQSTCPQ LLEDSSSDDY LDHSMVGRDL
EVYKYFSVIN KLNYWCLAST SKSKGPLDCF TFLETIDRIL LEYFDKDKLS IKKIVNNYDR
ISLIFNCCVE AGEPNVSDML YVNKIKEAVP ERSDLSKFIS STAHNLQQAV QLPQQRQQQL
QQNQISRGSN SLIENEEIVP WRTSRASKHE NNELYVDLLE TFHVVFEKKK SHLRLLTGSI
HGIVDVRSYL NDNPLVAVKL NTMGNDIGIP SLHDCVEIND GVFSPSNITF IPPDGKFRLL
EYSVDLSSQV KQSGVRMNSI GLMSLHFQNG LGKDSDEFEL SLNIENFKKV SQVDDLKIDL
QFNVENADPN EIAYKIKILR NTHGRFENSI IMGQGQWIFD KSTATGTVPV LRGCIEYENT
GPNFTKKVDL QTVSLEYSYI GQSASGIYVE AIDIVSGLTI GKNTKLYKGA KYKTQTGNFQ
VRL
