AIM44_YEAST
ID AIM44_YEAST Reviewed; 758 AA.
AC Q99299; D6W3L0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Altered inheritance of mitochondria protein 44;
GN Name=AIM44; OrderedLocusNames=YPL158C; ORFNames=P2570;
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 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 INDUCTION.
RX PubMed=11309124; DOI=10.1046/j.1365-2958.2001.02388.x;
RA Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.;
RT "Overlapping and distinct roles of the duplicated yeast transcription
RT factors Ace2p and Swi5p.";
RL Mol. Microbiol. 40:422-432(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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).
CC -!- INTERACTION:
CC Q99299; P19073: CDC42; NbExp=4; IntAct=EBI-29423, EBI-4274;
CC Q99299; P25293: NAP1; NbExp=5; IntAct=EBI-29423, EBI-11850;
CC Q99299; Q08229: NBA1; NbExp=5; IntAct=EBI-29423, EBI-36841;
CC Q99299; P53939: NIS1; NbExp=5; IntAct=EBI-29423, EBI-28760;
CC Q99299; P06780: RHO1; NbExp=3; IntAct=EBI-29423, EBI-15121;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is controlled by SWI5.
CC {ECO:0000269|PubMed:11309124}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AIM44 family. {ECO:0000305}.
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DR EMBL; X96770; CAA65563.1; -; Genomic_DNA.
DR EMBL; Z73514; CAA97863.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11276.1; -; Genomic_DNA.
DR PIR; S65169; S65169.
DR RefSeq; NP_015167.1; NM_001183972.1.
DR AlphaFoldDB; Q99299; -.
DR SMR; Q99299; -.
DR BioGRID; 36025; 502.
DR DIP; DIP-3992N; -.
DR IntAct; Q99299; 11.
DR MINT; Q99299; -.
DR STRING; 4932.YPL158C; -.
DR iPTMnet; Q99299; -.
DR PaxDb; Q99299; -.
DR PRIDE; Q99299; -.
DR EnsemblFungi; YPL158C_mRNA; YPL158C; YPL158C.
DR GeneID; 855945; -.
DR KEGG; sce:YPL158C; -.
DR SGD; S000006079; AIM44.
DR VEuPathDB; FungiDB:YPL158C; -.
DR eggNOG; ENOG502R02U; Eukaryota.
DR HOGENOM; CLU_385965_0_0_1; -.
DR InParanoid; Q99299; -.
DR OMA; MDFKFPS; -.
DR BioCyc; YEAST:G3O-34054-MON; -.
DR PRO; PR:Q99299; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q99299; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IMP:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0045185; P:maintenance of protein location; IMP:SGD.
DR GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0098841; P:protein localization to cell division site after cytokinesis; IMP:SGD.
DR GO; GO:1901900; P:regulation of protein localization to cell division site; IMP:SGD.
DR GO; GO:1990344; P:secondary cell septum biogenesis; IMP:SGD.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..758
FT /note="Altered inheritance of mitochondria protein 44"
FT /id="PRO_0000203491"
FT REGION 55..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 648..711
FT /evidence="ECO:0000255"
FT COMPBIAS 57..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..690
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 758 AA; 84846 MW; 3B4FA92B91C87F2B CRC64;
MIIRAPIRTK TKSFRGDQMD FKFPSNESLP RGTLEEYHLN NHHLLNDVFA AENGVSRDED
GNSQTLSDYT STSNTNTNSG YSSNGYYSFA NISDNTTSSP RIVINQNETA RLTSSDSNKS
DFFASHDFPG NDSLHYSSSN VVKNQLHSME AIPEGNITGS ISTAFQTIPT ADNVSYDIAP
SSASSLLPRK STSKSAILPS TQEAKPMTKL NMEKDIKTIE LNNSVVPKPK KKLNRVPTIR
RVESSRFSNS RYSSSVSSKS SSSRCSLKRS KAIRCKGGLL YYFTSLGIKI KKKLRKLRLV
LRRRLFSYNV QKVPSATNSK TTKSKANINN KSKKRGTNLV NKNSNSTPRQ KKSQRYVSNL
QRSISSKSLV PVLAPQKKTK PLTVDTKFKA NHPQSEDSKV GSNTPRSPLV SYTPSLRRTN
SSIRRAASIL TASATMTPAN NKNSFISVPD NVSHAVTRNS SMYSRSRLVR SKPSTALNAI
ARQPSIVVEN KVIPLSMNRY SIKEEDEYVI DTSSMRELSP VNSVCSSDYD RESSESYSNY
ADAMETTEVD NKDRVECNNE IQNVDANNEE TSNEESYNLM KHYLSTVIAQ RIMLRVQIAR
IQNYKSNVVY MNKSAETNST IYEDLVDSLL TEYEADGSSS QIFDGVTVRA DEEEEEDEDD
EDDEEEEEEN DDEEDEEDEE DDEDDEEEEE KRKEGEGRNL AKEVDELAEL SPMRKQSDLS
ITLRSPFAML NPAYSNSIIS LPTGVVKRSL TLPVGMKI
