APM2_YEAST
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 03-AUG-2022, entry version 161.
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=6; 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; 41.
DR ComplexPortal; CPX-533; Adaptor complex AP-1R.
DR DIP; DIP-1200N; -.
DR IntAct; P38700; 10.
DR MINT; P38700; -.
DR STRING; 4932.YHL019C; -.
DR MaxQB; P38700; -.
DR PaxDb; P38700; -.
DR PRIDE; P38700; -.
DR TopDownProteomics; P38700; -.
DR EnsemblFungi; YHL019C_mRNA; YHL019C; YHL019C.
DR GeneID; 856367; -.
DR KEGG; sce:YHL019C; -.
DR SGD; S000001011; APM2.
DR VEuPathDB; FungiDB:YHL019C; -.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_0_2_1; -.
DR InParanoid; P38700; -.
DR OMA; WVRYKTI; -.
DR BioCyc; YEAST:G3O-31039-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
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:0030122; C:AP-2 adaptor complex; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:SGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IMP:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR027200; Apm2.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR PANTHER; PTHR10529:SF271; PTHR10529:SF271; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
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..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 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
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
