AIM3_YEAS7
ID AIM3_YEAS7 Reviewed; 944 AA.
AC A6ZL53;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Altered inheritance of mitochondria protein 3;
GN Name=AIM3; ORFNames=SCY_0323;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000011; EDN64722.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZL53; -.
DR EnsemblFungi; EDN64722; EDN64722; SCY_0323.
DR HOGENOM; CLU_324433_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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..944
FT /note="Altered inheritance of mitochondria protein 3"
FT /id="PRO_0000399606"
FT REGION 1..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..944
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 96..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..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..944
FT /note="Basic and acidic 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 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 858
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
SQ SEQUENCE 944 AA; 103860 MW; 527928FFDA347BCA CRC64;
MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER KSGKKNSSDE
EYESEDEMEY ERKPTDIRSL KDPKSFPPPP LKPGQKTYAG QQQQQMPNGQ ASYAFQGAYQ
GQPGAGSMEQ SQYAQPQYNQ YPQQQLQQGV VPQQPPIYGE QVPPYGSNSN ATSYQSLPQQ
NQPQYAIPSQ VSLNSASQQS TGFVSQNLQY GTQSSNPAPS PSFQNGLQCH QQPQYVSHGS
TNLGQSQFPS GQQQQPTTQF GQQVLPSPAQ PHPQPQQQQQ GQPLPPPRGQ VILPAPGEPL
SNGFEQQQQQ QQQQQQQQPL NQNNALLPQM NVEGVSGMAA VQPVYGQAMS STTNMQDSNP
SYGASPMQGQ PPVGGQPPVP VRMQPQPPQP MQQGNIYPIE PSLDSTSSTP HFEVTPFDPD
APAPKPKIDI PTVDVSSLPP PPTHRDRGAV LHQEPAPSGK IQPNTTSSAA SLPAKHSRTT
TADNERNSGN KENDESTSKS SILGHYDVDV NIMPPPKPFR HGLDSVPSEH TRKNALERAV
PILPPRNNVE PPPPPSRGNF ERTELVLSTN AANVQEDPIS NFLPPPKPFR HTETKQNQNS
KASPVEIKDE VLPGHPSEED RNVEPSLLPQ SKPQSKSQSQ FRRAHMETQP IQNFQPPPKP
FRRSQSSNSS DSSYTIDGPE ANHGRGRGRI AKHHDGDEYN PKSENSTENG RLGDAPNSFI
RKRAPTPPAP SRSEKLHEGA ITSEFDSSKD ANKYEKSIPP VTSSIQAQQS TKKAPPPVVK
PKPRNFSLKA NEYPKELTRE ATGQDEVLNS ITNELSHIKL RKTNVNLEKL GGAKKVKDSS
PVPSDLDEKY VSASGSITPP RPPPSRSSPK KVPPVVPKKN DNLKKKPPVV PKKKPLLKSL
EPRPIEMERA YSGDISAADD NLNPFERYKR NVVPQEDDRL HKLK
