ID   APM2_YEAST              Reviewed;         605 AA.
AC   P38700; D3DKR4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 177.
DE   RecName: Full=Adaptin medium chain homolog APM2;
DE   AltName: Full=Adaptin-mu1-II;
GN   Name=APM2; OrderedLocusNames=YHL019C;
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=S288c / REE526;
RX   PubMed=7749194; DOI=10.1091/mbc.6.1.41;
RA   Stepp J.D., Pellicena-Palle A., Hamilton S., Kirchhausen T., Lemmon S.K.;
RT   "A late Golgi sorting function for Saccharomyces cerevisiae Apm1p, but not
RT   for Apm2p, a second yeast clathrin AP medium chain-related protein.";
RL   Mol. Biol. Cell 6:41-58(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
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   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).
RN   [5]
RP   INTERACTION WITH APL2.
RX   PubMed=10564262; DOI=10.1091/mbc.10.11.3643;
RA   Yeung B.G., Phan H.L., Payne G.S.;
RT   "Adaptor complex-independent clathrin function in yeast.";
RL   Mol. Biol. Cell 10:3643-3659(1999).
RN   [6]
RP   FUNCTION, SUBUNIT, INTERACTION WITH MIL1, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF PHE-273 AND ASP-275.
RX   PubMed=26658609; DOI=10.1091/mbc.e15-09-0621;
RA   Whitfield S.T., Burston H.E., Bean B.D., Raghuram N., Maldonado-Baez L.,
RA   Davey M., Wendland B., Conibear E.;
RT   "The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory
RT   protein and confers differential cargo sorting.";
RL   Mol. Biol. Cell 27:588-598(2016).
CC   -!- FUNCTION: Component of the AP-1-related (AP-1R) complex, an adapter
CC       protein complex that mediates of cargo protein sorting in clathrin-
CC       coated vesicles (PubMed:26658609). AP-1R has a specific role in SNARE
CC       SNC1 sorting (PubMed:26658609). In contrast to the APM1-containing AP-1
CC       complex, AP-1R is incapable of sorting CHS3 (PubMed:26658609).
CC       {ECO:0000269|PubMed:26658609}.
CC   -!- SUBUNIT: Component of the AP-1R complex composed of at least APM2, APL4
CC       and APS1 (PubMed:26658609). Interacts with MIL1 (PubMed:26658609).
CC       Interacts with APL2 (PubMed:10564262). {ECO:0000269|PubMed:10564262,
CC       ECO:0000269|PubMed:26658609}.
CC   -!- INTERACTION:
CC       P38700; P36000: APL2; NbExp=7; IntAct=EBI-2705, EBI-2206;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:26658609}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:26658609}. Early endosome membrane
CC       {ECO:0000269|PubMed:26658609}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:26658609}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle membrane {ECO:0000269|PubMed:26658609}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:26658609}.
CC   -!- DISRUPTION PHENOTYPE: Leads to sensitivity to cationic amphiphilic
CC       drugs (CADs) such as sertraline. {ECO:0000269|PubMed:26658609}.
CC   -!- MISCELLANEOUS: Present with 2890 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; U09841; AAA83415.1; -; Genomic_DNA.
DR   EMBL; U11582; AAB65072.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06666.1; -; Genomic_DNA.
DR   PIR; S46833; S46833.
DR   RefSeq; NP_011844.1; NM_001179099.1.
DR   AlphaFoldDB; P38700; -.
DR   SMR; P38700; -.
DR   BioGRID; 36404; 43.
DR   ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR   DIP; DIP-1200N; -.
DR   FunCoup; P38700; 84.
DR   IntAct; P38700; 10.
DR   STRING; 4932.YHL019C; -.
DR   GlyGen; P38700; 1 site.
DR   iPTMnet; P38700; -.
DR   PaxDb; 4932-YHL019C; -.
DR   PeptideAtlas; P38700; -.
DR   TopDownProteomics; P38700; -.
DR   EnsemblFungi; YHL019C_mRNA; YHL019C; YHL019C.
DR   GeneID; 856367; -.
DR   KEGG; sce:YHL019C; -.
DR   AGR; SGD:S000001011; -.
DR   SGD; S000001011; APM2.
DR   VEuPathDB; FungiDB:YHL019C; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   HOGENOM; CLU_026996_0_2_1; -.
DR   InParanoid; P38700; -.
DR   OMA; AAIHYMD; -.
DR   OrthoDB; 10259133at2759; -.
DR   BioCyc; YEAST:G3O-31039-MONOMER; -.
DR   Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR   BioGRID-ORCS; 856367; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38700; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38700; protein.
DR   GO; GO:0030121; C:AP-1 adaptor complex; EXP:ComplexPortal.
DR   GO; GO:0005769; C:early endosome; IDA:SGD.
DR   GO; GO:0031901; C:early endosome membrane; EXP:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR   GO; GO:0035615; F:clathrin-cargo adaptor activity; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd09250; AP-1_Mu1_Cterm; 1.
DR   CDD; cd14828; AP_Mu_N; 1.
DR   FunFam; 3.30.450.60:FF:000030; APM2p protein; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR   InterPro; IPR050431; Adaptor_comp_med_subunit.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR027200; Apm2_N.
DR   InterPro; IPR018240; Clathrin_mu_CS.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR028565; MHD.
DR   PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR   SUPFAM; SSF64356; SNARE-like; 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..605
FT                   /note="Adaptin medium chain homolog APM2"
FT                   /id="PRO_0000193793"
FT   DOMAIN          269..604
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   REGION          150..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..171
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..196
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         273
FT                   /note="F->A: Leads to sensitivity to sertraline, when
FT                   associated with S-275."
FT                   /evidence="ECO:0000269|PubMed:26658609"
FT   MUTAGEN         275
FT                   /note="D->S: Leads to sensitivity to sertraline, when
FT                   associated with A-273."
FT                   /evidence="ECO:0000269|PubMed:26658609"
SQ   SEQUENCE   605 AA;  69990 MW;  7E216B11325EEE3C CRC64;
     MSSSLFILDE NLEPLVSKNI RALPNLSSVL SSFKQCYHDG SPPILSQNDW FFIHLKRDFL
     HFVSVIHTTD KPNIDLMTIL AFLEQFYHLL QKYFEIEVLT KNVILDNILL VLELIDECID
     FGIVQVTDPS IIKDYIRVKV NVPRVTVDNE EWSPGEESSS SSGSDSDSEY SNTNKRKDKK
     KKRKKKKGTK GKSVGKSKLK SIMVNNKENR GINVVETVKE TLRNKNDTGK EAANDELPND
     GNDLYINGDI AKTIIMPISW RTKGIHYAKN EFFLDVIERV QYLMDFEKGV IRKNLIHGEI
     VCRCYLSGMP KLKISINKIL NRDPQFMSNS SFHQCVSLDS INTIEKDEEK NSDDDAGLQA
     ATDAREIEFI PPDGEFVLCQ YELKRHVKDA PMVRLKDFEI KPKLKKFKIQ IVTKIQTNFK
     PTNSTSKLNV RIPLTKVFQE YKIDLSKQIR FKANIGKVVF NLSDDFLLWE IQTMKGHREH
     STNKSSQYNS DEDDPNTCAS MVAEFPLFNQ EEYDRLQEEM KTSMNPPPLR TGPRLEELYR
     QVHDQQTSHV TPRDKLVNID FEIPYCTCSG LKVEYLKVEE PQLQYQSFPW VRYKTVSDEE
     YAYIV
//