AIM3_YEAST
ID AIM3_YEAST Reviewed; 947 AA.
AC P38266; D6VQA7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Altered inheritance of mitochondria protein 3;
GN Name=AIM3; OrderedLocusNames=YBR108W; ORFNames=YBR0901;
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=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(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 515.
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 FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP INTERACTION WITH RVS167, AND SUBCELLULAR LOCATION.
RX PubMed=15561700; DOI=10.1074/jbc.m412454200;
RA Germann M., Swain E., Bergman L., Nickels J.T. Jr.;
RT "Characterizing the sphingolipid signaling pathway that remediates defects
RT associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and
RT Rvs167p.";
RL J. Biol. Chem. 280:4270-4278(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-729, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; THR-729 AND THR-861, AND
RP IDENTIFICATION BY 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 [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-58 AND SER-64, AND
RP IDENTIFICATION BY 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).
CC -!- SUBUNIT: Interacts with RVS167. {ECO:0000269|PubMed:15561700}.
CC -!- INTERACTION:
CC P38266; P38822: BZZ1; NbExp=2; IntAct=EBI-21584, EBI-3889;
CC P38266; P53281: LSB1; NbExp=3; IntAct=EBI-21584, EBI-23329;
CC P38266; P43603: LSB3; NbExp=4; IntAct=EBI-21584, EBI-22980;
CC P38266; P39743: RVS167; NbExp=6; IntAct=EBI-21584, EBI-14500;
CC P38266; P32793: YSC84; NbExp=5; IntAct=EBI-21584, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:15561700};
CC Peripheral membrane protein {ECO:0000269|PubMed:15561700}.
CC Note=Localize within detergent-insoluble glycolipid-enriched membranes.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- SIMILARITY: Belongs to the AIM3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55611.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85063.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X78993; CAA55611.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35977; CAA85063.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07227.2; -; Genomic_DNA.
DR PIR; S48273; S48273.
DR RefSeq; NP_009666.3; NM_001178456.2.
DR AlphaFoldDB; P38266; -.
DR SMR; P38266; -.
DR BioGRID; 32812; 202.
DR DIP; DIP-1602N; -.
DR IntAct; P38266; 16.
DR MINT; P38266; -.
DR STRING; 4932.YBR108W; -.
DR iPTMnet; P38266; -.
DR MaxQB; P38266; -.
DR PaxDb; P38266; -.
DR PRIDE; P38266; -.
DR EnsemblFungi; YBR108W_mRNA; YBR108W; YBR108W.
DR GeneID; 852405; -.
DR KEGG; sce:YBR108W; -.
DR SGD; S000000312; AIM3.
DR VEuPathDB; FungiDB:YBR108W; -.
DR eggNOG; ENOG502S02E; Eukaryota.
DR HOGENOM; CLU_324433_0_0_1; -.
DR InParanoid; P38266; -.
DR OMA; DNPFRRY; -.
DR BioCyc; YEAST:G3O-29070-MON; -.
DR PRO; PR:P38266; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38266; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0000147; P:actin cortical patch assembly; IGI:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IMP:SGD.
DR InterPro; IPR031370; Aim3.
DR Pfam; PF17096; AIM3; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..947
FT /note="Altered inheritance of mitochondria protein 3"
FT /id="PRO_0000202486"
FT REGION 1..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 515
FT /note="V -> A (in Ref. 1; CAA55611 and 2; CAA85063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 103863 MW; CD624428B29DA272 CRC64;
MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER KSGKKNSSDE
EYDSEDEMEY ERKPTDIRSL KDPKSFPPPP LKPGQKTYTG QQQQQMPNGQ ASYAFQGAYQ
GQPGAGSTEQ SQYAQPQYNQ YPQQQLQQGV MPQQQQLQQG VVPQQPPIYG EQVPPYGSNS
NATSYQSLPQ QNQPQNAIPS QVSLNSASQQ STGFVSQNLQ YGTQSSNPAP SPSFQNGLQC
HQQPQYVSHG STNLGQSQFP SGQQQQPTTQ FGQQVLPSPA QPQQQQQGQP LPPPRGQVIL
PAPGEPLSNG FGQQQQQQQQ QQQPLNQNNA LLPQMNVEGV SGMAAVQPVY GQAMSSTTNM
QDSNPSYGAS PMQGQPPVGG QPPVPVRMQP QPPQPMQQGN IYPIEPSLDS TGSTPHFEVT
PFDPDAPAPK PKIDIPTVDV SSLPPPPTHR DRGAVVHQEP APSGKIQPNT TSSAASLPAK
HSRTTTADNE RNSGNKENDE STSKSSILGH YDVDVNIMPP PKPFRHGLDS VPSEHTTKNA
PERAVPILPP RNNVEPPPPP SRGNFERTES VLSTNAANVQ EDPISNFLPP PKPFRHTETK
QNQNSKASPV EMKGEVLPGH PSEEDRNVEP SLVPQSKPQS QSQFRRAHME TQPIQNFQPP
PKPFRRSQSS NSSDSSYTID GPEANHGRGR GRIAKHHDGD EYNPKSENST ENGRLGDAPN
SFIRKRAPTP PAPSRSEKLH EGTITSEVDS SKDANKYEKS IPPVTSSIQA QQSTKKAPPP
VVKPKPRNFS LKANEYPKEL TREATGQDEV LNSITNELSH IKLRKTNVNL EKLGGSKKVK
DSSPVPSDLD EKYVSASGSI TPPRPPPSRS SPKKVPPVVP KKNDNLKKKP PVVPKKKPLL
KSLEPRPIEM ERAYSGDISA ADDNLNPFER YKRNVVPQED DRLHKLK
