MSC7_YEAST
ID MSC7_YEAST Reviewed; 644 AA.
AC P38694; D3DKY6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Putative aldehyde dehydrogenase-like protein YHR039C;
DE EC=1.2.1.-;
DE AltName: Full=Meiotic sister-chromatid recombination protein 7;
GN Name=MSC7; OrderedLocusNames=YHR039C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 2500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U00062; AAB68915.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06730.1; -; Genomic_DNA.
DR PIR; S46746; S46746.
DR RefSeq; NP_011904.1; NM_001179169.1.
DR AlphaFoldDB; P38694; -.
DR SMR; P38694; -.
DR BioGRID; 36470; 116.
DR DIP; DIP-1878N; -.
DR IntAct; P38694; 14.
DR MINT; P38694; -.
DR STRING; 4932.YHR039C; -.
DR iPTMnet; P38694; -.
DR MaxQB; P38694; -.
DR PaxDb; P38694; -.
DR PRIDE; P38694; -.
DR EnsemblFungi; YHR039C_mRNA; YHR039C; YHR039C.
DR GeneID; 856434; -.
DR KEGG; sce:YHR039C; -.
DR SGD; S000001081; MSC7.
DR VEuPathDB; FungiDB:YHR039C; -.
DR eggNOG; KOG2454; Eukaryota.
DR HOGENOM; CLU_005391_1_0_1; -.
DR InParanoid; P38694; -.
DR OMA; PVAHHVC; -.
DR BioCyc; YEAST:G3O-31098-MON; -.
DR PRO; PR:P38694; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38694; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..644
FT /note="Putative aldehyde dehydrogenase-like protein
FT YHR039C"
FT /id="PRO_0000056596"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT SITE 248
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 644 AA; 71321 MW; 54DADDAEB2A16D4D CRC64;
MSKVYLNSDM INHLNSTVQA YFNLWLEKQN AIMRSQPQII QDNQKLIGIT TLVASIFTLY
VLVKIISTPA KCSSSYKPVK FSLPAPEAAQ NNWKGKRSVS TNIWNPEEPN FIQCHCPATG
QYLGSFPSKT EADIDEMVSK AGKAQSTWGN SDFSRRLRVL ASLHDYILNN QDLIARVACR
DSGKTMLDAS MGEILVTLEK IQWTIKHGQR ALQPSRRPGP TNFFMKWYKG AEIRYEPLGV
ISSIVSWNYP FHNLLGPIIA ALFTGNAIVV KCSEQVVWSS EFFVELIRKC LEACDEDPDL
VQLCYCLPPT ENDDSANYFT SHPGFKHITF IGSQPVAHYI LKCAAKSLTP VVVELGGKDA
FIVLDSAKNL DALSSIIMRG TFQSSGQNCI GIERVIVSKE NYDDLVKILN DRMTANPLRQ
GSDIDHLENV DMGAMISDNR FDELEALVKD AVAKGARLLQ GGSRFKHPKY PQGHYFQPTL
LVDVTPEMKI AQNEVFGPIL VMMKAKNTDH CVQLANSAPF GLGGSVFGAD IKECNYVANS
LQTGNVAIND FATFYVCQLP FGGINGSGYG KFGGEEGLLG LCNAKSVCFD TLPFVSTQIP
KPLDYPIRNN AKAWNFVKSF IVGAYTNSTW QRIKSLFSLA KEAS
