MCP1_YEAST
ID MCP1_YEAST Reviewed; 302 AA.
AC Q12106; D6W2T2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mitochondrial adapter protein MCP1 {ECO:0000305};
DE AltName: Full=MDM10-complementing protein 1 {ECO:0000303|PubMed:23781023};
GN Name=MCP1 {ECO:0000303|PubMed:23781023};
GN OrderedLocusNames=YOR228C {ECO:0000312|SGD:S000005754}; ORFNames=YOR50-18;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH VPS13, TOPOLOGY, AND MUTAGENESIS OF HIS-187;
RP HIS-237 AND GLY-241.
RX PubMed=28864540; DOI=10.1083/jcb.201610055;
RA John Peter A.T., Herrmann B., Antunes D., Rapaport D., Dimmer K.S.,
RA Kornmann B.;
RT "Vps13-Mcp1 interact at vacuole-mitochondria interfaces and bypass ER-
RT mitochondria contact sites.";
RL J. Cell Biol. 216:3219-3229(2017).
RN [9]
RP FUNCTION, INTERACTION WITH VPS13, AND MUTAGENESIS OF 4-LEU--VAL-12 AND
RP 9-PRO--PRO-11.
RX PubMed=30018089; DOI=10.1083/jcb.201804111;
RA Bean B.D.M., Dziurdzik S.K., Kolehmainen K.L., Fowler C.M.S., Kwong W.K.,
RA Grad L.I., Davey M., Schluter C., Conibear E.;
RT "Competitive organelle-specific adaptors recruit Vps13 to membrane contact
RT sites.";
RL J. Cell Biol. 217:3593-3607(2018).
RN [10]
RP FUNCTION.
RX PubMed=34830155; DOI=10.3390/ijms222212274;
RA Kolakowski D., Rzepnikowska W., Kaniak-Golik A., Zoladek T., Kaminska J.;
RT "The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi
RT Apparatus.";
RL Int. J. Mol. Sci. 22:12274-12274(2021).
CC -!- FUNCTION: Recruits the lipid transfer protein Vps13 to mitochondria
CC thereby promoting vacuole-mitochondria contacts (PubMed:28864540,
CC PubMed:30018089, PubMed:34830155). Involved in mitochondrial lipid
CC homeostasis (PubMed:23781023, PubMed:28864540).
CC {ECO:0000269|PubMed:23781023, ECO:0000269|PubMed:28864540,
CC ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:34830155}.
CC -!- SUBUNIT: Interacts (via PxP motif) with VPS13 (via SHR-BD domain).
CC {ECO:0000269|PubMed:28864540, ECO:0000269|PubMed:30018089}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:23781023}; Multi-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; X92441; CAA63191.1; -; Genomic_DNA.
DR EMBL; Z75136; CAA99448.1; -; Genomic_DNA.
DR EMBL; AY558034; AAS56360.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10998.1; -; Genomic_DNA.
DR PIR; S60955; S60955.
DR RefSeq; NP_014871.3; NM_001183647.3.
DR AlphaFoldDB; Q12106; -.
DR BioGRID; 34621; 158.
DR STRING; 4932.YOR228C; -.
DR TCDB; 9.B.178.1.1; the mdmd complementing protein 1 (mcp1) family.
DR PaxDb; Q12106; -.
DR PRIDE; Q12106; -.
DR EnsemblFungi; YOR228C_mRNA; YOR228C; YOR228C.
DR GeneID; 854403; -.
DR KEGG; sce:YOR228C; -.
DR SGD; S000005754; MCP1.
DR VEuPathDB; FungiDB:YOR228C; -.
DR eggNOG; ENOG502RYUN; Eukaryota.
DR HOGENOM; CLU_066681_1_0_1; -.
DR InParanoid; Q12106; -.
DR OMA; HLLIMKW; -.
DR BioCyc; YEAST:G3O-33726-MON; -.
DR PRO; PR:Q12106; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12106; protein.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IGI:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IGI:SGD.
DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR039960; MCP1.
DR InterPro; IPR012472; MCP1_TM.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR38409; PTHR38409; 1.
DR Pfam; PF07950; DUF1691; 2.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Mitochondrial adapter protein MCP1"
FT /id="PRO_0000245281"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT TRANSMEM 62..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..100
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT TRANSMEM 101..121
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT TRANSMEM 174..194
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..219
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT TRANSMEM 220..240
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT TRANSMEM 259..276
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..302
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:23781023,
FT ECO:0000305|PubMed:28864540"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..12
FT /note="PxP"
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 4..12
FT /note="Missing: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 9..11
FT /note="PEP->AEA: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 187
FT /note="H->A: Disrupts activity."
FT /evidence="ECO:0000269|PubMed:28864540"
FT MUTAGEN 237
FT /note="H->A: Disrupts activity."
FT /evidence="ECO:0000269|PubMed:28864540"
FT MUTAGEN 241
FT /note="G->A: Disrupts activity."
FT /evidence="ECO:0000269|PubMed:28864540"
SQ SEQUENCE 302 AA; 33989 MW; 3B6672DA9F292718 CRC64;
MIKLHEVPPE PVDPASLPHD VNAHSPEGDG NPDKRKKIFG IPYPFSRSSC RRFLWNCQKI
SVLPMALYFP LHAANTLITP AVSPDSAPDD VLMMVREILP SITTKLLVAG ITLHVSAGVL
LRIVNNWNKP RRNRHRHLKI SAEQDLSQDS IGLTGGISGY LFGLYKTFRI PPQVISGYIL
VPVLIYHLLI MKWVPNSIST EVDFASIKQL LSSKNRWWKW LGGLVPLAIL LESGVYHIGS
GLCRYFGVRK MTSRKKWSTA INLLTLVGFV SLIRLMKEDS TKLGPNQFES IFKKIRLLLH
VN
