DAN1_YEAST
ID DAN1_YEAST Reviewed; 298 AA.
AC P47178; D6VWW8; O94102;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cell wall protein DAN1;
DE AltName: Full=Covalently-linked cell wall protein 13;
DE AltName: Full=Delayed anaerobic protein 1;
DE Flags: Precursor;
GN Name=DAN1; Synonyms=CCW13; OrderedLocusNames=YJR150C; ORFNames=J2217;
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], AND INDUCTION.
RX PubMed=9224891; DOI=10.1016/s0378-1119(97)00028-0;
RA Sertil O., Cohen B.D., Davies K.J.A., Lowry C.V.;
RT "The DAN1 gene of S. cerevisiae is regulated in parallel with the hypoxic
RT genes, but by a different mechanism.";
RL Gene 192:199-205(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 115.
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 PROTEIN SEQUENCE OF 20-27, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=10322008; DOI=10.1128/jb.181.10.3076-3086.1999;
RA Mrsa V., Ecker M., Strahl-Bolsinger S., Nimtz M., Lehle L., Tanner W.;
RT "Deletion of new covalently linked cell wall glycoproteins alters the
RT electrophoretic mobility of phosphorylated wall components of Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 181:3076-3086(1999).
RN [5]
RP INDUCTION.
RX PubMed=11292809; DOI=10.1128/jb.183.9.2881-2887.2001;
RA Abramova N.E., Sertil O., Mehta S., Lowry C.V.;
RT "Reciprocal regulation of anaerobic and aerobic cell wall mannoprotein gene
RT expression in Saccharomyces cerevisiae.";
RL J. Bacteriol. 183:2881-2887(2001).
CC -!- FUNCTION: Component of the cell wall.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:10322008}. Membrane {ECO:0000269|PubMed:10322008};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10322008}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC -!- INDUCTION: Induced during anaerobic growth and completely repressed
CC during aerobic growth. {ECO:0000269|PubMed:11292809,
CC ECO:0000269|PubMed:9224891}.
CC -!- PTM: Extensively O-glycosylated.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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DR EMBL; U69874; AAC49762.1; -; Genomic_DNA.
DR EMBL; Z49650; CAA89683.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08934.2; -; Genomic_DNA.
DR PIR; S57179; S57179.
DR RefSeq; NP_012684.4; NM_001181808.4.
DR AlphaFoldDB; P47178; -.
DR BioGRID; 33905; 75.
DR STRING; 4932.YJR150C; -.
DR PaxDb; P47178; -.
DR EnsemblFungi; YJR150C_mRNA; YJR150C; YJR150C.
DR GeneID; 853615; -.
DR KEGG; sce:YJR150C; -.
DR SGD; S000003911; DAN1.
DR VEuPathDB; FungiDB:YJR150C; -.
DR eggNOG; ENOG502SR1B; Eukaryota.
DR GeneTree; ENSGT00940000176276; -.
DR HOGENOM; CLU_071083_1_0_1; -.
DR InParanoid; P47178; -.
DR OMA; TNGANKF; -.
DR BioCyc; YEAST:G3O-31763-MON; -.
DR PRO; PR:P47178; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47178; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0015918; P:sterol transport; IMP:SGD.
DR InterPro; IPR000992; SRP1_TIP1.
DR Pfam; PF00660; SRP1_TIP1; 1.
DR PROSITE; PS00724; SRP1_TIP1; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10322008"
FT CHAIN 20..275
FT /note="Cell wall protein DAN1"
FT /id="PRO_0000033239"
FT PROPEP 276..298
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000033240"
FT REGION 122..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 275
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 115
FT /note="E -> G (in Ref. 2; CAA89683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 29606 MW; 26CCF5DE7CD59E9F CRC64;
MSRISILAVA AALVASATAA SVTTTLSPYD ERVNLIELAV YVSDIGAHLS EYYAFQALHK
TETYPPEIAK AVFAGGDFTT MLTGISGDEV TRMITGVPWY STRLMGAISE ALANEGIATA
VPASTTEASS TSTSEASSAA TESSSSSESS AETSSNAAST QATVSSESSS AASTIASSAE
SSVASSVASS VASSASFANT TAPVSSTSSI SVTPVVQNGT DSTVTKTQAS TVETTITSCS
NNVCSTVTKP VSSKAQSTAT SVTSSASRVI DVTTNGANKF NNGVFGAAAI AGAAALLL
