DAN4_YEAST
ID DAN4_YEAST Reviewed; 1161 AA.
AC P47179; D6VWW9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cell wall protein DAN4 {ECO:0000305};
DE AltName: Full=Delayed anaerobic protein 4 {ECO:0000303|PubMed:11292809};
DE Flags: Precursor;
GN Name=DAN4 {ECO:0000303|PubMed:11292809};
GN OrderedLocusNames=YJR151C {ECO:0000312|SGD:S000003912};
GN ORFNames=J2223 {ECO:0000312|SGD:S000003912};
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=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 [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.
RX PubMed=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
RN [4]
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).
RN [5]
RP INDUCTION.
RX PubMed=11160904; DOI=10.1093/nar/29.3.799;
RA Cohen B.D., Sertil O., Abramova N.E., Davies K.J.A., Lowry C.V.;
RT "Induction and repression of DAN1 and the family of anaerobic mannoprotein
RT genes in Saccharomyces cerevisiae occurs through a complex array of
RT regulatory sites.";
RL Nucleic Acids Res. 29:799-808(2001).
RN [6]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Component of the cell wall. {ECO:0000305|PubMed:16086015,
CC ECO:0000305|PubMed:9613572}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:9613572}.
CC Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CC -!- INDUCTION: Induced during anaerobic growth and completely repressed
CC during aerobic growth. {ECO:0000269|PubMed:11160904,
CC ECO:0000269|PubMed:11292809}.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains. {ECO:0000269|PubMed:16086015}.
CC -!- PTM: Extensively O-glycosylated. {ECO:0000305}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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DR EMBL; Z49651; CAA89684.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08935.1; -; Genomic_DNA.
DR PIR; S57180; S57180.
DR RefSeq; NP_012685.1; NM_001181809.2.
DR AlphaFoldDB; P47179; -.
DR BioGRID; 33906; 81.
DR STRING; 4932.YJR151C; -.
DR PaxDb; P47179; -.
DR PRIDE; P47179; -.
DR EnsemblFungi; YJR151C_mRNA; YJR151C; YJR151C.
DR GeneID; 853616; -.
DR KEGG; sce:YJR151C; -.
DR SGD; S000003912; DAN4.
DR VEuPathDB; FungiDB:YJR151C; -.
DR eggNOG; ENOG502S6R6; Eukaryota.
DR GeneTree; ENSGT00940000176276; -.
DR HOGENOM; CLU_277742_0_0_1; -.
DR InParanoid; P47179; -.
DR OMA; ATEWTTK; -.
DR BioCyc; YEAST:G3O-31764-MON; -.
DR PRO; PR:P47179; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47179; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR000992; SRP1_TIP1.
DR Pfam; PF00660; SRP1_TIP1; 1.
DR PROSITE; PS00724; SRP1_TIP1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1137
FT /note="Cell wall protein DAN4"
FT /id="PRO_0000033243"
FT PROPEP 1138..1161
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000033244"
FT REPEAT 373..384
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 385..396
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 397..408
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 409..420
FT /note="1-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 421..432
FT /note="1-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 433..444
FT /note="1-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 445..456
FT /note="1-7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 457..468
FT /note="1-8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 469..480
FT /note="1-9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 481..492
FT /note="1-10"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 493..504
FT /note="1-11"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 505..516
FT /note="1-12"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 517..528
FT /note="1-13"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 529..540
FT /note="1-14"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 826..913
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 914..1001
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 1002..1040
FT /note="2-3; truncated"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 123..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..286
FT /note="46 X 3 AA tandem repeats of T-[SP]-T"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..540
FT /note="14 X 12 AA approximate tandem repeats"
FT REGION 691..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..1040
FT /note="2.5 X 88 AA approximate tandem repeats"
FT LIPID 1137
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1161 AA; 118360 MW; 7954C15D69F0CA58 CRC64;
MVNISIVAGI VALATSAAAI TATTTLSPYD ERVNLIELAV YVSDIRAHIF QYYSFRNHHK
TETYPSEIAA AVFDYGDFTT RLTGISGDEV TRMITGVPWY STRLKPAISS ALSKDGIYTA
IPTSTSTTTT KSSTSTTPTT TITSTTSTTS TTPTTSTTST TPTTSTTSTT PTTSTTSTTP
TTSTTSTTPT TSTTSTTPTT STTSTTPTTS TTSTTPTTST TSTTPTTSTT PTTSTTSTTS
QTSTKSTTPT TSSTSTTPTT STTPTTSTTS TAPTTSTTST TSTTSTISTA PTTSTTSSTF
STSSASASSV ISTTATTSTT FASLTTPATS TASTDHTTSS VSTTNAFTTS ATTTTTSDTY
ISSSSPSQVT SSAEPTTVSE VTSSVEPTRS SQVTSSAEPT TVSEFTSSVE PTRSSQVTSS
AEPTTVSEFT SSVEPTRSSQ VTSSAEPTTV SEFTSSVEPT RSSQVTSSAE PTTVSEFTSS
VEPTRSSQVT SSAEPTTVSE FTSSVEPIRS SQVTSSAEPT TVSEVTSSVE PIRSSQVTTT
EPVSSFGSTF SEITSSAEPL SFSKATTSAE SISSNQITIS SELIVSSVIT SSSEIPSSIE
VLTSSGISSS VEPTSLVGPS SDESISSTES LSATSTFTSA VVSSSKAADF FTRSTVSAKS
DVSGNSSTQS TTFFATPSTP LAVSSTVVTS STDSVSPNIP FSEISSSPES STAITSTSTS
FIAERTSSLY LSSSNMSSFT LSTFTVSQSI VSSFSMEPTS SVASFASSSP LLVSSRSNCS
DARSSNTISS GLFSTIENVR NATSTFTNLS TDEIVITSCK SSCTNEDSVL TKTQVSTVET
TITSCSGGIC TTLMSPVTTI NAKANTLTTT ETSTVETTIT TCPGGVCSTL TVPVTTITSE
ATTTATISCE DNEEDITSTE TELLTLETTI TSCSGGICTT LMSPVTTINA KANTLTTTET
STVETTITTC SGGVCSTLTV PVTTITSEAT TTATISCEDN EEDVASTKTE LLTMETTITS
CSGGICTTLM SPVSSFNSKA TTSNNAESTI PKAIKVSCSA GACTTLTTVD AGISMFTRTG
LSITQTTVTN CSGGTCTMLT APIATATSKV ISPIPKASSA TSIAHSSASY TVSINTNGAY
NFDKDNIFGT AIVAVVALLL L
