MIL1_YEAST
ID MIL1_YEAST Reviewed; 1073 AA.
AC P43564; D6VTJ7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable lipase MIL1 {ECO:0000303|PubMed:26658609};
DE EC=3.1.1.- {ECO:0000305|PubMed:26658609};
DE AltName: Full=Medium adaptin-interacting ligand 1 {ECO:0000303|PubMed:26658609};
GN Name=MIL1 {ECO:0000303|PubMed:26658609}; OrderedLocusNames=YFL034W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 323.
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 [3]
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 [4]
RP INTERACTION WITH RPP0.
RX PubMed=15286401; DOI=10.1007/bf02702559;
RA Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A.,
RA Balachandara S.R., Sharma S.;
RT "Identification of a hypothetical membrane protein interactor of ribosomal
RT phosphoprotein P0.";
RL J. Biosci. 29:33-43(2004).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1037, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP FUNCTION, INTERACTION WITH APM2, DOMAIN, AND MUTAGENESIS OF
RP 143-TRP--PRO-147; SER-759; ASP-817 AND HIS-858.
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: Probable lipase that recruits the AP-1-related (AP-1R)
CC complex to membranes via interaction with APM2 (PubMed:26658609). The
CC AP-1R complex is an adapter protein complex that mediates of cargo
CC protein SNC1 sorting in clathrin-coated vesicles (PubMed:26658609).
CC {ECO:0000269|PubMed:26658609}.
CC -!- SUBUNIT: Interacts with RPP0 (PubMed:15286401). Interacts with APM2
CC (PubMed:26658609). {ECO:0000269|PubMed:15286401,
CC ECO:0000269|PubMed:26658609}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:26658609}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:26658609};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane {ECO:0000269|PubMed:26658609}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TMCO4 family. {ECO:0000305}.
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DR EMBL; D50617; BAA09205.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12407.2; -; Genomic_DNA.
DR PIR; S56220; S56220.
DR RefSeq; NP_116583.2; NM_001179932.2.
DR AlphaFoldDB; P43564; -.
DR BioGRID; 31113; 80.
DR DIP; DIP-6508N; -.
DR IntAct; P43564; 4.
DR MINT; P43564; -.
DR STRING; 4932.YFL034W; -.
DR ESTHER; yeast-yfd4; Duf_726.
DR iPTMnet; P43564; -.
DR MaxQB; P43564; -.
DR PaxDb; P43564; -.
DR PRIDE; P43564; -.
DR EnsemblFungi; YFL034W_mRNA; YFL034W; YFL034W.
DR GeneID; 850510; -.
DR KEGG; sce:YFL034W; -.
DR SGD; S000001860; MIL1.
DR VEuPathDB; FungiDB:YFL034W; -.
DR eggNOG; KOG2385; Eukaryota.
DR GeneTree; ENSGT00390000001400; -.
DR HOGENOM; CLU_001695_2_1_1; -.
DR InParanoid; P43564; -.
DR OMA; GWMNGKV; -.
DR BioCyc; YEAST:G3O-30428-MON; -.
DR PRO; PR:P43564; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43564; protein.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0035652; P:clathrin-coated vesicle cargo loading; IMP:SGD.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007941; DUF726.
DR PANTHER; PTHR17920; PTHR17920; 1.
DR Pfam; PF05277; DUF726; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1073
FT /note="Probable lipase MIL1"
FT /id="PRO_0000202674"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..147
FT /note="APM2-interacting WQEMP motif"
FT /evidence="ECO:0000269|PubMed:26658609"
FT COMPBIAS 9..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 850
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 143..147
FT /note="WQEMP->AAEAA: Impairs the interaction with APM2 and
FT its recruitment to membranes, and leads to sertraline
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:26658609"
FT MUTAGEN 759
FT /note="S->A: Increases sensitivity to sertraline."
FT /evidence="ECO:0000269|PubMed:26658609"
FT MUTAGEN 817
FT /note="D->A: Increases sensitivity to sertraline."
FT /evidence="ECO:0000269|PubMed:26658609"
FT MUTAGEN 858
FT /note="H->A: Increases sensitivity to sertraline."
FT /evidence="ECO:0000269|PubMed:26658609"
FT CONFLICT 323
FT /note="K -> N (in Ref. 1; BAA09205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1073 AA; 119510 MW; 2CB2CAB4F9E24DA2 CRC64;
MSDSEEDLGV QLKGLKIARH LKESGEHTDE ESNSSPEHDC GLSNQDDLTV MHTQAKEEVF
KRREEDGTRT EDALHEGEAG KEGTGFPSSQ SVCSPNEADS GIDRADKPIL LDPFKSVHDT
DPVPGTKSRS NSDSDSDSDD GGWQEMPAVS SFNIYNHRGE LELTSKVRNS EQASETSPTV
PPGKNCKSVN DSRFDYTKMA AEQQAQRSYR TNKKTDFLFD HKVLKKKINS SQTSVNLTSS
PSTTSLNNEK NNDDDDDDSY DEYEDDVEPV NDLNRDSQLN ITKNLLSDME KFAYVGAINI
LANQMCTNLA TLCLCIDIKS HKKLAHRLQF TQKDMAAWKT VVLSRLYDHL GISQEEIVMI
EKLSLHKIQL EDLCKCLKTT QSIDNPWEND RDHEEDGIEE TTERMSPNEQ NGSVQASTPD
PEQSATPETP KAKQSPLSSD VPGKVLDPEN VKSQDKLNID VAWTIICDLF LICLQSSTYD
SRSRTLLINF AKVLNMTSLE ICEFERRVTD SLDMEQSTED QVWDEQDHMR NRRRSKRRKK
MAYVALAMVG GSLVLGLSGG LLAPVIGGGI AAGLSTIGIT GATSFLTGVG GTTVVAVSST
AIGANIGARG MSKRMGSVRT FEFRPLHNNR RVNLILTVSG WMVGNEDDVR LPFSTVDPVE
GDLYSLYWEP EMLKSIGQTV SIVATEIFTT SLQQILGATV LTALISSIQW PMALSKLGYI
LDNPWNVSLD RAWSAGKILA DTLIARNLGA RPITLVGFSI GARVIFSCLI ELCKKKALGL
IENVYLFGTP AVMKKEQLVM ARSVVSGRFV NGYSDKDWFL AYLFRAAAGG FSAVMGISTI
ENVEGIENIN CTEFVDGHLN YRKSMPKLLK RIGIAVLSEE FVEIEEMMNP EEVKRKRKLI
NDVDAAQKKL SERKKHNSWV PKWLKPKKSK WKVMVEEAVE EGRDMQDLPE NDVNNNENEN
PDEHEGIARQ KRRDAALVDH GALMHELQLI KQAMHEDEIK NKACLPGEDK EVESSNDFLG
ESHYKPPSTP KINPPQSPNN FQLLSAGRTI LPEDDDFDPR GKKKVEFSFP DDI
