MPC54_YEAST
ID MPC54_YEAST Reviewed; 464 AA.
AC Q08550; D6W2N3;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Meiotic plaque component protein 54;
GN Name=MPC54; OrderedLocusNames=YOR177C;
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=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 [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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP SPO21; NUD1 AND SPC42.
RX PubMed=10899120; DOI=10.1093/emboj/19.14.3657;
RA Knop M., Strasser K.;
RT "Role of the spindle pole body of yeast in mediating assembly of the
RT prospore membrane during meiosis.";
RL EMBO J. 19:3657-3667(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11553705; DOI=10.1091/mbc.12.9.2646;
RA Deng C., Saunders W.S.;
RT "ADY1, a novel gene required for prospore membrane formation at selected
RT spindle poles in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 12:2646-2659(2001).
RN [5]
RP FUNCTION, COMPOSITION OF A SPB COMPLEX, AND INTERACTION WITH ADY3.
RX PubMed=11742972; DOI=10.1093/emboj/20.24.6946;
RA Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A.,
RA Shevchenko A., Knop M.;
RT "Prospore membrane formation linked to the leading edge protein (LEP) coat
RT assembly.";
RL EMBO J. 20:6946-6957(2001).
RN [6]
RP INTERACTION WITH SPO74.
RX PubMed=12796288; DOI=10.1128/ec.2.3.431-445.2003;
RA Nickas M.E., Schwartz C., Neiman A.M.;
RT "Ady4p and Spo74p are components of the meiotic spindle pole body that
RT promote growth of the prospore membrane in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:431-445(2003).
CC -!- FUNCTION: Involved in the pathway that organizes the shaping and sizing
CC of the prospore membrane (PSM) during sporulation.
CC {ECO:0000269|PubMed:10899120, ECO:0000269|PubMed:11742972}.
CC -!- SUBUNIT: Interacts directly with SPO21/MPC70, NUD1, SPO74 and SPC42.
CC Probable component of a spindle pole body (SPB) complex composed of
CC ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
CC {ECO:0000269|PubMed:10899120, ECO:0000269|PubMed:11742972,
CC ECO:0000269|PubMed:12796288}.
CC -!- INTERACTION:
CC Q08550; Q07732: ADY3; NbExp=3; IntAct=EBI-34513, EBI-33406;
CC Q08550; P32336: NUD1; NbExp=2; IntAct=EBI-34513, EBI-12361;
CC Q08550; Q12411: SPO21; NbExp=3; IntAct=EBI-34513, EBI-36275;
CC -!- SUBCELLULAR LOCATION: Prospore membrane. Cytoplasm, cytoskeleton,
CC microtubule organizing center, spindle pole body. Cytoplasm,
CC cytoskeleton, spindle pole. Note=Localizes to the ends of spindle
CC microtubules in cells in meiosis. Localizes to all four spindle pole
CC bodies during meiosis, ADY1 is required for this localization.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Expressed during meiosis II,
CC from 3 to 9 hours after induction of sporulation. Not expressed during
CC mitosis. {ECO:0000269|PubMed:10899120}.
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DR EMBL; Z75085; CAA99386.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10949.1; -; Genomic_DNA.
DR PIR; S67069; S67069.
DR RefSeq; NP_014820.1; NM_001183596.1.
DR AlphaFoldDB; Q08550; -.
DR SMR; Q08550; -.
DR BioGRID; 34572; 75.
DR DIP; DIP-2886N; -.
DR IntAct; Q08550; 8.
DR MINT; Q08550; -.
DR STRING; 4932.YOR177C; -.
DR PaxDb; Q08550; -.
DR PRIDE; Q08550; -.
DR EnsemblFungi; YOR177C_mRNA; YOR177C; YOR177C.
DR GeneID; 854349; -.
DR KEGG; sce:YOR177C; -.
DR SGD; S000005703; MPC54.
DR VEuPathDB; FungiDB:YOR177C; -.
DR HOGENOM; CLU_588136_0_0_1; -.
DR InParanoid; Q08550; -.
DR OMA; ITHETNR; -.
DR BioCyc; YEAST:G3O-33689-MON; -.
DR PRO; PR:Q08550; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08550; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048278; P:vesicle docking; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Meiosis;
KW Membrane; Reference proteome; Sporulation.
FT CHAIN 1..464
FT /note="Meiotic plaque component protein 54"
FT /id="PRO_0000096555"
FT REGION 71..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..119
FT /evidence="ECO:0000255"
FT COILED 156..193
FT /evidence="ECO:0000255"
FT COILED 231..365
FT /evidence="ECO:0000255"
FT COMPBIAS 71..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 54358 MW; 74C614223B385CAC CRC64;
MPEDTSYSNS FEDYYNNSHA ISPYKDSFYK EMTPSKPNVR FGDDDVNIFD QRKKVNEINK
NNTVKRSIPS SISTTITPNK SSLKSPRGKR ASKNSFDNET KLESKNETLK EVNDAVNRCY
ALCNIPTKHV SINSISDLAQ TFETLAVGIT HETNRKAECE RSKNAIDSLY YHEQLEKKEL
NEKSLQMAID HLLKVTKQNL RQADDGNKLK ETEALKSFIE EIEEVDDNKI SINSLQQQLL
EEKTANNILR RDYYKLQERG RRLCHEFQEL QDDYSKQMKQ KEYEVQKLKN EIKVLLNMND
NLKAEKAHYS QKEKQYFQKY TYIEKYMNHV KEEYNRKEDE CKKLNFIIDK SMKKIEHLER
SLQTQFTAQN SFSTAMIQEE GPKDAHLKDR YHKVKEFMEQ KLQTSKINDP SCSEAEALDN
VLCLIESSMK TLDKNSKCYP IATKKCIKYV TDSPRLKENE HVTN
