RMD8_YEAST
ID RMD8_YEAST Reviewed; 662 AA.
AC P43620; D6VTT1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Sporulation protein RMD8;
DE AltName: Full=Required for meiotic nuclear division protein 8;
GN Name=RMD8; OrderedLocusNames=YFR048W;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686379;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g;
RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:149-167(1996).
RN [4]
RP FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for sporulation. {ECO:0000269|PubMed:12586695}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RMD1/sif2 family. {ECO:0000305}.
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DR EMBL; D50617; BAA09287.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12491.1; -; Genomic_DNA.
DR PIR; S56303; S56303.
DR RefSeq; NP_683716.1; NM_001180013.1.
DR AlphaFoldDB; P43620; -.
DR BioGRID; 31206; 111.
DR IntAct; P43620; 2.
DR MINT; P43620; -.
DR STRING; 4932.YFR048W; -.
DR iPTMnet; P43620; -.
DR MaxQB; P43620; -.
DR PaxDb; P43620; -.
DR PRIDE; P43620; -.
DR EnsemblFungi; YFR048W_mRNA; YFR048W; YFR048W.
DR GeneID; 850609; -.
DR KEGG; sce:YFR048W; -.
DR SGD; S000001944; RMD8.
DR VEuPathDB; FungiDB:YFR048W; -.
DR eggNOG; KOG2861; Eukaryota.
DR GeneTree; ENSGT00390000013337; -.
DR HOGENOM; CLU_011220_3_0_1; -.
DR InParanoid; P43620; -.
DR OMA; NERCQVF; -.
DR BioCyc; YEAST:G3O-30494-MON; -.
DR PRO; PR:P43620; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43620; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR003734; DUF155.
DR Pfam; PF02582; DUF155; 1.
PE 1: Evidence at protein level;
KW Acetylation; Meiosis; Membrane; Reference proteome; Sporulation;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..662
FT /note="Sporulation protein RMD8"
FT /id="PRO_0000202698"
FT TRANSMEM 630..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 662 AA; 75914 MW; 1B5B7964A6520FF1 CRC64;
MSYKANQPSP GEMPKRSPSI LVTDARTSKN RMSAPFAGHA AGSRKNMENA GVTKSQGVRS
SAIGPSPLQS FTHPRRRSSG RFSDISIDNI LSDNSDIPSA RREERLSSSS SDRPRQYERL
SSRRKMINPL PPRTSKTSQK LVLIPEDDNL NHFQTLPTNA LDRQRPKVGS MKSNSFDRLP
RYSKEKSMAR ITAYNVADGF NLNQLYKFLQ ETHEVSPRLY DECLYVAYTL PLLPGKGGFR
IKSNLSKKTM GGKTLIDNLI DTSEQRDHHY EYYSGVETVE DANNNYELET SGNNNNANQD
TTTVPDHLPN PVGQQDSFNP MEPQFFAEET PLEIEKRERT ERINMLKKEE NDSDASCGND
NNNKNNDKSK LYAVEGNDQY VQSSRSPASP SSISTPSPPS SSQNDFDRVY KMHRDNDHEG
NDRHAEIFIF HYGVIVFWNF TEIQEKNILG DITFADYKNL MIRPLDEQDI ETEQFHFEYD
RDTERPRIFN DIVTLRSGDH IIELTLSHAI AQSSKLSRFE SRISPILISV TKLPKRLALY
GTLGLKREQL LKKSGKLFKL RVDVNLSSTI LDTPEFFWSF EPSLHPLYVA MREYLEIDQR
VQVLNDRCKV FLEFFDICVD SVAERNMARV TWWFILVILF GVIFSLTEIF VRYVIIHRHT
ST
