AIM3_YEAS1
ID AIM3_YEAS1 Reviewed; 936 AA.
AC B3LN45;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Altered inheritance of mitochondria protein 3;
GN Name=AIM3; ORFNames=SCRG_02858;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408048; EDV11998.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LN45; -.
DR EnsemblFungi; EDV11998; EDV11998; SCRG_02858.
DR HOGENOM; CLU_324433_0_0_1; -.
DR Proteomes; UP000008335; 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..936
FT /note="Altered inheritance of mitochondria protein 3"
FT /id="PRO_0000399605"
FT REGION 1..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..936
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..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..936
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 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 718
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
FT MOD_RES 850
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38266"
SQ SEQUENCE 936 AA; 102618 MW; ADDA06936DAA906D CRC64;
MGFWENNKDS ITSGLKSAGK YGYQGTKYVA KTGYKASKKH YNNSKARRER KSGKKNSSDE
EYESEDEMEH ERKPTDIRSL KDPKSFPPPP LKPGQKTYTG QQQQQMPNGQ ASYAFQGAYQ
GQPGAGSMEQ SQYAQPQYNQ YPQQQLQQGV MPQQPPIYGE QVPPYGSNSN ATSYQSLPQQ
NQPQYAIPSQ VSLNSASQQS TGFVSQNLQY GTQSSNPAPS PSFQNGLQCH QQPQYVSHGS
TNLGQSQFPS GQQQQPTTQF GQQVLPSPAQ PHPQPQQQQQ GQPLPPPRGQ VILPAPGEPL
SNGFGQQQQQ 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 PQSKSQSQSQ SQFRRAHMET QPIQNFQPPP KPFRRSQSSN
SSDSSYTIDG PEANHGRGRG RIAKHHDGDE YNPKSENSTE NGRLGDAPNS FIRKRAPTPP
APSGSEKLHE GAITSEVDSS KDANKYEKSI PPVTSSIQAQ QSTKKAPPPV VKPKPRNFSL
KANEYPKELT REATGQDEVL NSITNELSHI KLRKINVNLE KLGGSKKVKD SSPVPSDLDE
KYVSASGSIT PPRPPPSRSS PKKVPPVVPK KNDNLKKKPP VVPKKKPLLK SLEPRPIEME
RAYSGDISAA DDNLNPFERY KRNVVPQEDD RLHKLK
