MUM3_YEAST
ID MUM3_YEAST Reviewed; 479 AA.
AC Q08750; D6W2Z7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein MUM3;
DE AltName: Full=Muddled meiosis protein 3;
GN Name=MUM3; OrderedLocusNames=YOR298W;
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].
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
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 FUNCTION.
RX PubMed=9504908; DOI=10.1093/genetics/148.2.581;
RA Engebrecht J., Masse S., Davis L., Rose K., Kessel T.;
RT "Yeast meiotic mutants proficient for the induction of ectopic
RT recombination.";
RL Genetics 148:581-598(1998).
RN [5]
RP FUNCTION.
RX PubMed=12432101; DOI=10.1073/pnas.202604399;
RA Deutschbauer A.M., Williams R.M., Chu A.M., Davis R.W.;
RT "Parallel phenotypic analysis of sporulation and postgermination growth in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15530-15535(2002).
RN [6]
RP FUNCTION.
RX PubMed=15590821; DOI=10.1128/ec.3.6.1464-1475.2004;
RA Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P.,
RA Neiman A.M.;
RT "Morphogenetic pathway of spore wall assembly in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 3:1464-1475(2004).
CC -!- FUNCTION: Involved in the organization of the outer spore wall layers
CC and especially in the assembly of the chitosan layer.
CC {ECO:0000269|PubMed:12432101, ECO:0000269|PubMed:15590821,
CC ECO:0000269|PubMed:9504908}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; Z75206; CAA99526.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11063.1; -; Genomic_DNA.
DR PIR; S67202; S67202.
DR RefSeq; NP_014941.1; NM_001183717.1.
DR AlphaFoldDB; Q08750; -.
DR BioGRID; 34686; 41.
DR DIP; DIP-4079N; -.
DR IntAct; Q08750; 1.
DR STRING; 4932.YOR298W; -.
DR PaxDb; Q08750; -.
DR PRIDE; Q08750; -.
DR EnsemblFungi; YOR298W_mRNA; YOR298W; YOR298W.
DR GeneID; 854473; -.
DR KEGG; sce:YOR298W; -.
DR SGD; S000005824; MUM3.
DR VEuPathDB; FungiDB:YOR298W; -.
DR eggNOG; ENOG502QWMQ; Eukaryota.
DR HOGENOM; CLU_045029_0_0_1; -.
DR InParanoid; Q08750; -.
DR OMA; YDITIVY; -.
DR BioCyc; YEAST:G3O-33783-MON; -.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR Reactome; R-SCE-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q08750; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08750; protein.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; ISS:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:SGD.
PE 4: Predicted;
KW Glycoprotein; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="Protein MUM3"
FT /id="PRO_0000255970"
FT TRANSMEM 33..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 57237 MW; 52ACF3D16872A411 CRC64;
MGFVDFFETY MVGSRVQFKQ LDISDWLSLT PRLLILFGYF YLHSFFTAIN QFLQFINTNS
FCLRLHLLYD RFWSHVPIIG EYKIRLLSRA LTYSKLKIIP TLDKVLEAIE IWFQLHLVEM
TFEKKKNVQI FITEGSDDLN FFKDSKFQTT LMICNHRSVN DYTLINYLFL KSCPTKFYTK
WEFLQKLRKG EDLAEWPQLK FLGWGKMFNF PRLDLLKNIF FKDETLALSS NELRDILERQ
NNQAITIFPE VNIMSLELSI IQRKLHQDFP FVINFYNLLY PRFKNFTTLM AAFSSIKNIK
RKKNRNNIIK EARYLFHREL DKLVHKSMKM ESSKVSDKTT PPMIVDNSYL LTKKEEISSG
KPKVVRINPY IYDVTIIYYR VKYTDSGHDH TNGDLRLHKG YQLEQISPTI FEMIQPEMES
ENNIKDKDPI VVMVNVKKHQ IQPLLAYNDE SLEKWLENRW IEKDRLIESL QKNIKIETK
