AIM3_YEAS8
ID AIM3_YEAS8 Reviewed; 946 AA.
AC D3UEK1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Altered inheritance of mitochondria protein 3;
GN Name=AIM3; ORFNames=EC1118_1B15_2542g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- SUBUNIT: Interacts with RVS167. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Localizes within detergent-insoluble
CC glycolipid-enriched membranes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AIM3 family. {ECO:0000305}.
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DR EMBL; FN393060; CBK39181.1; -; Genomic_DNA.
DR AlphaFoldDB; D3UEK1; -.
DR EnsemblFungi; CBK39181; CBK39181; EC1118_1B15_2542g.
DR HOGENOM; CLU_324433_0_0_1; -.
DR Proteomes; UP000000286; Chromosome II, Scaffold EC1118_1B15.
DR GO; GO:0030479; C:actin cortical patch; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR InterPro; IPR031370; Aim3.
DR Pfam; PF17096; AIM3; 1.
PE 3: Inferred from homology;
KW Membrane; Phosphoprotein.
FT CHAIN 1..946
FT /note="Altered inheritance of mitochondria protein 3"
FT /id="PRO_0000399604"
FT REGION 1..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..903
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 52..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
SQ SEQUENCE 946 AA; 103954 MW; 9F883BF0D1BAD225 CRC64;
MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER KSGKKNSSDE
EYESEDEMEH ERKPTDIRSL KDPKSFPPPP LKPGQKTYTG QQQQQMPNGQ ASYAFQGAYQ
GQPGAGSMEQ SQYAQPQYNQ YPQQQLQQGV VPQQPPIYGE QVPPYGSNSN ATSYQSLSQQ
NQPQYAIPSQ VSLNSASQQS TGFVSQNLQY GTQSSNPAPS PSFQNGLQCH QQPQYVSHGS
TNLGQSQFPS GQQQQPTTQF GQQVLPSPAQ PHPQPQQQQQ GQPLPPPRGQ VILPAPGEPL
SNGFGQQQQQ QQQQQQQQQQ PLNQNNALLP QMNVEGVSGM AAVQPVYGQA MSSTTNMQDS
NPSYGASPMQ GQPPVGGQPP VPVRMQPQPP QPMQQGNIYP IEPSLDSTSS TPHFEVTPFD
PDAPAPKPKI DIPTVDVSSL PPPPTHRDRG AVLHQEPAPS GKIQPNTTSS AASLPAKHSR
TTTADNERNS GNKENDESTS KSSILGHYDV DVNIMPPPKP FRHGLDSVPS EHTRKNASER
AVPILPPRNN VEPPPPPSRG NFERTESVLS TNAANVQEDP ISNFLPPPKP FRHTETKQNQ
NSKASPVEIK DEVLPGHPSE EDRNVEPSLL PQSKPQSQSQ SQFRRAHMET QPIQNFQPPP
KPFRRSQSSN SSDSSYTIDG PEANHGRGRG RIAKHHDGDE YNPKSENSTE NGRLGDAPNS
FIRKRAPTPP APSRSEKLHE GAITSEVDSS KDANKYEKSI PPVTSSIQAQ QSTKKAPPPV
VKPKPRNFSL KANEYPKELT REATGQDEVL NSITNELSHI KLRKTNVNLE KLGGSKKVKD
SSPVPSDLDE KYVSASGSIT PPRPPPSRSS PKKVPPVVPK KNDNLKKKPP VVPKKKPLLK
SLEPRPIEME RAYSGDISAA DDNLNPFERY KRNVVPQEDD RLHKLK
