MCP2_YEAST
ID MCP2_YEAST Reviewed; 569 AA.
AC Q06567; D6VYQ0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ABC1 family protein MCP2 {ECO:0000305|PubMed:23781023};
DE AltName: Full=MDM10-complementing protein 2 {ECO:0000303|PubMed:23781023};
DE AltName: Full=MIOREX complex component 13 {ECO:0000305|PubMed:25683707};
DE AltName: Full=Mitochondrial organization of gene expression protein 13 {ECO:0000303|PubMed:25683707};
DE Flags: Precursor;
GN Name=MCP2 {ECO:0000303|PubMed:23781023};
GN Synonyms=MRX13 {ECO:0000303|PubMed:25683707};
GN OrderedLocusNames=YLR253W {ECO:0000312|SGD:S000004243}; ORFNames=L9672.2;
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 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 [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 [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=23781023; DOI=10.1242/jcs.121244;
RA Tan T., Ozbalci C., Brugger B., Rapaport D., Dimmer K.S.;
RT "Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid
RT homeostasis.";
RL J. Cell Sci. 126:3563-3574(2013).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25683707; DOI=10.1016/j.celrep.2015.01.012;
RA Kehrein K., Schilling R., Moller-Hergt B.V., Wurm C.A., Jakobs S.,
RA Lamkemeyer T., Langer T., Ott M.;
RT "Organization of mitochondrial gene expression in two distinct ribosome-
RT containing assemblies.";
RL Cell Rep. 10:843-853(2015).
CC -!- FUNCTION: Component of MIOREX complexes, large expressome-like
CC assemblies of ribosomes with factors involved in all the steps of post-
CC transcriptional gene expression (PubMed:25683707). Involved in
CC mitochondrial lipid homeostasis (PubMed:23781023).
CC {ECO:0000269|PubMed:23781023, ECO:0000269|PubMed:25683707}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:23781023}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; U20865; AAB67388.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09566.1; -; Genomic_DNA.
DR PIR; S59398; S59398.
DR RefSeq; NP_013354.1; NM_001182140.1.
DR AlphaFoldDB; Q06567; -.
DR SMR; Q06567; -.
DR BioGRID; 31520; 62.
DR DIP; DIP-4782N; -.
DR IntAct; Q06567; 2.
DR MINT; Q06567; -.
DR STRING; 4932.YLR253W; -.
DR MaxQB; Q06567; -.
DR PaxDb; Q06567; -.
DR PRIDE; Q06567; -.
DR DNASU; 850955; -.
DR EnsemblFungi; YLR253W_mRNA; YLR253W; YLR253W.
DR GeneID; 850955; -.
DR KEGG; sce:YLR253W; -.
DR SGD; S000004243; MCP2.
DR VEuPathDB; FungiDB:YLR253W; -.
DR eggNOG; KOG1235; Eukaryota.
DR GeneTree; ENSGT00940000158221; -.
DR HOGENOM; CLU_006533_2_5_1; -.
DR InParanoid; Q06567; -.
DR OMA; PYVKGNS; -.
DR BioCyc; YEAST:G3O-32357-MON; -.
DR PRO; PR:Q06567; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06567; protein.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0055088; P:lipid homeostasis; IGI:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR CDD; cd13969; ADCK1-like; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR045307; ADCK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..569
FT /note="ABC1 family protein MCP2"
FT /id="PRO_0000200737"
FT TOPO_DOM 19..34
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:23781023"
FT TRANSMEM 35..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..569
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:23781023"
SQ SEQUENCE 569 AA; 65917 MW; 7DC8EE15C09C26E5 CRC64;
MMTKAFFNKL PFEVFRRYVR TGKSIPQRSP RTRKSLLVGG TIASAVVLYN FNDTFHDSVK
HTALTTKRIA VVTQATTRCF YHYKRALNKS YENKKEREVA LNKCHKMCAL ITLHALRSNG
GIYIKLGQHI GAMTYLLPKE WTDTMIPLQD HCPESTYEEI DELFKEDLGT SIEDMFLEFN
KTPIGVASLA QVHVAKLKNS DGKGSSVAVK CQHPSLKEFI PLDVMLTRTV FELLDVFFPD
YPLTWLGDEL QSSIYVELNF TKEAENAEKT RHYFSKFKKQ TALKIPKVIE SHKRILIMEY
VGGKRLDDLE YIDSHGISRS EVSSCLSHIF NNMIFTPNVG IHCDPHGGNL AIRSVKPAKD
NGYHNFEIVL FDHGLYRYPS TRTRRLYAKF WLSLLFDKDQ TKMKKYAKGF ANITDEQFPL
LAAAITGRSI DAALNYDIST SRTQEEMDVM ANGILEGTLL SDLMSILSRI PRVVLLILKT
NDLTRHLDEC LQNPLGPERT FLIMTQYCAK TVYDEKVERI NSEYARWSIK WMWENLTNWI
VYERRINQLY FYDFVLWWKK FIPKTWLSS
