IML1_ASHGO
ID IML1_ASHGO Reviewed; 1534 AA.
AC Q75DV2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Vacuolar membrane-associated protein IML1;
GN Name=IML1; OrderedLocusNames=ABL079C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 1026.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IML1 family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50692.2; -; Genomic_DNA.
DR RefSeq; NP_982868.2; NM_208221.2.
DR AlphaFoldDB; Q75DV2; -.
DR STRING; 33169.AAS50692; -.
DR PRIDE; Q75DV2; -.
DR EnsemblFungi; AAS50692; AAS50692; AGOS_ABL079C.
DR GeneID; 4618949; -.
DR KEGG; ago:AGOS_ABL079C; -.
DR eggNOG; KOG3572; Eukaryota.
DR HOGENOM; CLU_000935_1_1_1; -.
DR InParanoid; Q75DV2; -.
DR OMA; REMWHFE; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IBA:GO_Central.
DR GO; GO:1990130; C:GATOR1 complex; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IEA:EnsemblFungi.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:EnsemblFungi.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR045838; DEPDC5_CTD.
DR InterPro; IPR027244; IML1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13179; PTHR13179; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF19418; DEPDC5_CTD; 1.
DR Pfam; PF12257; IML1; 1.
DR SMART; SM00049; DEP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50186; DEP; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Vacuole.
FT CHAIN 1..1534
FT /note="Vacuolar membrane-associated protein IML1"
FT /id="PRO_0000301761"
FT DOMAIN 1149..1224
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 19..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 175141 MW; AA8DF905DFEA6C4E CRC64;
MQSNLLQFSN LRTGNLRLAS TNRGSANGGG SSTMESGTSG AGSSSNKQVN MVIENNTLTI
GGTEGKRAFG RRLQMDTSGL KVKSKVDQEE LESAMKTPIS GIPFFNQSSR RSYQFELSFH
NTPVSDDCHV LIDVSQLPGA REGDLAELRT YHRSPGTRDK KVYFKIKSLD VEARRRSATT
GLSILTGQLR YLLDLPSRSP VWVKLKSKNE HQADLVELHV KDCHVNRGDM WCISSTLLDT
CVFTGQRVTY INALRLIVKA IYRNGKKVIS GYVGNNTKVI FASESARIIF LIQITEEMWH
FEQNGEKTFH KVVNSLFPRI LKRWKDIGTY HTITIVFCAS VDESGQSFRN IPPGVRLKNT
KDYFRIVVDR VNILYWDEIM KTLRKEFMQI IGDLRNTQTD DGGGPIRWSF TPVIKSNILE
TINFATTLLA DQFRVPDLKH TVTHVIIISP GTGLYDVNYD LLKVTCRKLL SLEIAVDLIC
LSRAPLHIVP LFRYIDYQGE LCHSAPTWLS ISFWDDNKKS QEWHPRCKIY DVQMMGVTER
RDSEEVTLNY MNSALHTTSV TDFMDQYDKE VFDADKCYPL SNENRESTPL EDTSNIESTV
LPKSGHEVQS IVWKPPRSSK PLVEPTTVQS VIVSLHQPGT INNSSEDDLT DTSSSNSSPE
ANESLALASL KNMTQISRGL TKRIVSKLIP DIKSKRSRHS IMATGNEHPR NDTYEDIEDI
RKVDCHSTGT NITFLKPTFR SMDAEHYNPP DTVSSHGSAG TDSRRESLMF EKKSVLLDDF
AKKKSNVNKY IKEKSLVDSL IHLDNPSVCF SGEVATMLIP DRWKDVYPKY VAKKYTKWRS
FTTPAELPIT TVHFPSLSDF ESNFIFRNHS VSLNIDREVY GQTTFDLLRD MIYIRLLAGF
QICTSELLKK VEATGSNEIH EQEIAKVLSK DNYMVAIYYM IIDNEVHRIK CGYNGTIDVQ
RFLRKNENKM MDTIAKYTPL VRTRYEHSYR PCKMDPLRIS RTSLRWNQVD QILAGYYDSM
MDSSKIGFRS KFVILPADIP PNTFSSTVNG RKETLSAEEI RLEGLRKLIS SISKSRLRTN
PEKATKASRK EEILPEVHFY TGSLFEYLAD HHDNLEHVDS PAKDAQSADL SKFNRDAELS
RLAYELQHGE KPIKLTNRKW HFKNHSSCFV GLEMVNWLIE NFSDIDTRDE AVIYGQQLLT
DGLFHHVDRR HGFLDGHYFY RISDPFVDIK IEKGSAESPL NSDPITINRR VSASTIISSK
QNSSGMIQSK NGDSELLDRQ SVNDEGKTIV ISTAIDIDLD PAGNSHKLET CTVHYDQVHN
PDHCFHIRIE WLTATPKLLD DLVTNWGRLC ERYGLRLVEI PWHELCTIPS FDPTHSFIEA
TLAINPWTDP EFMDAEIFAS QKYFYHVHLL ESFGFLLDNR ASRILQNERV SFNVVYSWGK
PSFKYAQFIH NTGAYMAEIR ENGDLFLAPN NLYLSRNGIG NSSGSLHLGP KSAIYSEKVM
LDFKHVCEDY KKLRSVFWEA RDKWQQTRNT LEEY
