MMR1_YEAST
ID MMR1_YEAST Reviewed; 491 AA.
AC Q06324; D6VYJ3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Mitochondrial MYO2 receptor-related protein 1;
GN Name=MMR1; OrderedLocusNames=YLR190W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP PHOSPHORYLATION, AND INTERACTION WITH PCL7.
RX PubMed=12006994;
RA Shi X.Z., Ao S.Z.;
RT "Phosphorylation of YLR190w by PAP1 PHO85 kinase complex.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:187-192(2002).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=13679573; DOI=10.1073/pnas.2033246100;
RA Shepard K.A., Gerber A.P., Jambhekar A., Takizawa P.A., Brown P.O.,
RA Herschlag D., DeRisi J.L., Vale R.D.;
RT "Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-
RT localized transcripts using DNA microarray analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11429-11434(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYO2.
RX PubMed=15201867; DOI=10.1038/sj.emboj.7600271;
RA Itoh T., Toh-e A., Matsui Y.;
RT "Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of
RT mitochondria in the budding yeast.";
RL EMBO J. 23:2520-2530(2004).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12; SER-16 AND SER-37, 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 -!- FUNCTION: Involved in the guiding of mitochondrial tubules to the bud
CC tip during cell division. {ECO:0000269|PubMed:15201867}.
CC -!- SUBUNIT: Interacts with MYO2 and PCL7. {ECO:0000269|PubMed:12006994,
CC ECO:0000269|PubMed:15201867}.
CC -!- INTERACTION:
CC Q06324; Q04477: SPC24; NbExp=3; IntAct=EBI-37386, EBI-27228;
CC -!- SUBCELLULAR LOCATION: Bud tip. Bud neck. Mitochondrion outer membrane;
CC Peripheral membrane protein.
CC -!- PTM: Phosphorylated by the cyclin-CDK PCL7-PHO85.
CC {ECO:0000269|PubMed:12006994}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U17246; AAB67454.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09509.1; -; Genomic_DNA.
DR PIR; S51435; S51435.
DR RefSeq; NP_013291.1; NM_001182077.1.
DR PDB; 6IXP; X-ray; 2.73 A; B/C/E/F=398-430.
DR PDBsum; 6IXP; -.
DR AlphaFoldDB; Q06324; -.
DR SMR; Q06324; -.
DR BioGRID; 31460; 396.
DR DIP; DIP-1498N; -.
DR IntAct; Q06324; 3.
DR MINT; Q06324; -.
DR STRING; 4932.YLR190W; -.
DR iPTMnet; Q06324; -.
DR MaxQB; Q06324; -.
DR PaxDb; Q06324; -.
DR PRIDE; Q06324; -.
DR EnsemblFungi; YLR190W_mRNA; YLR190W; YLR190W.
DR GeneID; 850887; -.
DR KEGG; sce:YLR190W; -.
DR SGD; S000004180; MMR1.
DR VEuPathDB; FungiDB:YLR190W; -.
DR eggNOG; ENOG502RXGA; Eukaryota.
DR HOGENOM; CLU_029804_0_0_1; -.
DR InParanoid; Q06324; -.
DR OMA; HISMQMA; -.
DR BioCyc; YEAST:G3O-32312-MON; -.
DR PRO; PR:Q06324; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06324; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR InterPro; IPR013712; MMR1.
DR Pfam; PF08505; MMR1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..491
FT /note="Mitochondrial MYO2 receptor-related protein 1"
FT /id="PRO_0000245841"
FT REGION 300..439
FT /note="Interaction with MYO2"
FT /evidence="ECO:0000269|PubMed:15201867"
FT REGION 419..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 295..384
FT /evidence="ECO:0000255"
FT COMPBIAS 445..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:6IXP"
SQ SEQUENCE 491 AA; 54817 MW; 31D8A7AFBF455A8E CRC64;
MNSPTMKSEQ LTPKLSPMSF CLDDQRNAGS FQNLLNSPTK LKLDTGPIGN SLLYPTSLSK
LSELSRGGRS KQRRGSDTMR SVSPIRFQFL NNTPKMLKPE YLSQTTSNLP LLSALLKNSK
KTTSEGQNSN PDPLNIEKNI IKQSIKDKLE QLRSSESVAQ VQKKERNPPS FEAKVCAEEP
ILRKNAEGLL PSYVPVPATP LEDPENHGVR KVEDKGLRVV SGGSTQCLST EVNELPKDLN
LDNLPTDNNG FVQYGLKGNN NNNRYSFISS TSTDYEPEWC DGQQHISMQM ASMANAEEAN
SREKSNLDIK IKQLELEITE LKLQNEKLVH SMTTNRYIEE RFMLEVMKDP SIQAQRSQRD
IERKVKQLEK KFFNCKKVLK KLTESSAVVA TSTSKTEGNS ARIPCPKTRL ARVSVLDLKK
IEEQPDSSSG TSSEEDHLTN DDTDANTSED LNVAFEEEPT SAISTTASVQ SGESKRGFQL
NLPVQVEKKE K
