CSS1_YEAST
ID CSS1_YEAST Reviewed; 995 AA.
AC P40442; D6VVC0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Secreted protein CSS1 {ECO:0000303|PubMed:26928762};
DE AltName: Full=Condition specific secretion protein 1 {ECO:0000303|PubMed:26928762};
DE AltName: Full=Haze protective factor 1' {ECO:0000303|PubMed:17024473};
DE Flags: Precursor;
GN Name=CSS1 {ECO:0000303|PubMed:26928762}; Synonyms=HPF1';
GN OrderedLocusNames=YIL169C; ORFNames=YI9402.07C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 INDUCTION.
RX PubMed=11050096; DOI=10.1074/jbc.m008381200;
RA Lamb T.M., Xu W., Diamond A., Mitchell A.P.;
RT "Alkaline response genes of Saccharomyces cerevisiae and their relationship
RT to the RIM101 pathway.";
RL J. Biol. Chem. 276:1850-1856(2001).
RN [4]
RP INDUCTION.
RX PubMed=11136466; DOI=10.1046/j.1365-2958.2001.02242.x;
RA Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H., Van Den Ende H.,
RA Klis F.M.;
RT "Low external pH induces HOG1-dependent changes in the organization of the
RT Saccharomyces cerevisiae cell wall.";
RL Mol. Microbiol. 39:469-479(2001).
RN [5]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17024473; DOI=10.1007/s00253-006-0606-0;
RA Brown S.L., Stockdale V.J., Pettolino F., Pocock K.F., de Barros Lopes M.,
RA Williams P.J., Bacic A., Fincher G.B., Hoej P.B., Waters E.J.;
RT "Reducing haziness in white wine by overexpression of Saccharomyces
RT cerevisiae genes YOL155c and YDR055w.";
RL Appl. Microbiol. Biotechnol. 73:1363-1376(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
CC -!- FUNCTION: Secreted protein that may be involved in cell wall
CC organization and biosynthesis. {ECO:0000269|PubMed:17024473}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26928762}.
CC -!- INDUCTION: Expression is induced in both high and low pH environments.
CC {ECO:0000269|PubMed:11050096, ECO:0000269|PubMed:11136466}.
CC -!- DISRUPTION PHENOTYPE: Decreases haze protective activity in white wine.
CC {ECO:0000269|PubMed:17024473}.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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DR EMBL; Z46921; CAA87023.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08386.1; -; Genomic_DNA.
DR PIR; S50358; S50358.
DR RefSeq; NP_012097.1; NM_001179517.1.
DR AlphaFoldDB; P40442; -.
DR SMR; P40442; -.
DR BioGRID; 34825; 20.
DR DIP; DIP-3929N; -.
DR IntAct; P40442; 2.
DR MINT; P40442; -.
DR STRING; 4932.YIL169C; -.
DR CarbonylDB; P40442; -.
DR iPTMnet; P40442; -.
DR MaxQB; P40442; -.
DR PaxDb; P40442; -.
DR PRIDE; P40442; -.
DR EnsemblFungi; YIL169C_mRNA; YIL169C; YIL169C.
DR GeneID; 854637; -.
DR KEGG; sce:YIL169C; -.
DR SGD; S000001431; CSS1.
DR VEuPathDB; FungiDB:YIL169C; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000179085; -.
DR HOGENOM; CLU_016111_1_0_1; -.
DR InParanoid; P40442; -.
DR OMA; CDDNGCK; -.
DR BioCyc; YEAST:G3O-31414-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P40442; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40442; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; HDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0061025; P:membrane fusion; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..995
FT /note="Secreted protein CSS1"
FT /id="PRO_0000014330"
FT DOMAIN 26..253
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 98..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 995 AA; 99736 MW; F63E287A03F137EC CRC64;
MFNRLNKFQA ALALALYSQS ALGQYYSNST SISSNSSSTS VVSSSSGSVS ISSSIAETSS
SATDILSSIT QSASSTSGVS SSVGPSSSSV VSSSVSQSSS SVSDVSSSVS QSSSSASDVS
SSVSQSASST SDVSSSVSQS SSSASDVSSS VSQSSSSASD VSSSVSQSAS SASDVSSSVS
QSASSTSDVS SSVSQSSSSA SDVSSSVSQS SSSASDVSSS VSQSASSTSD VSSSVSQSAS
STSGVSSSGS QSVSSASGSS SSFPQSTSSA STASGSATSN SLSSITSSAS SASATASNSL
SSSDGTIYLP TTTISGDLTL TGKVIATEGV VVAAGAKLTL LDGDKYSFSA DLKVYGDLLV
KKSKETYPGT EFDISGENFD VTGNFNAEES AATSASIYSF TPSSFDNSGD ISLSLSKSKK
GEVTFSPYSN SGAFSFSNAI LNGGSVSGLQ RRDDTEGSVN NGEINLDNGS TYVIVEPVSG
KGTVNIISGN LYLHYPDTFT GQTVVFKGEG VLAVDPTETN ATPIPVVGYT GKNQIAITAD
ITALSYDGTT GVLTATQGNR QFSFAIGTGF SSSDFSVSEG IFAGAYAYYL NYNGVVATSA
ASSSTASGAS ASVTGSTSFG ASVTGSTAST SFGASVTGST ASTSFGASVT GSTSVYTTTL
DYVNATSTVV VSCSETTDSN GNVYTITTTV PCSSTTATIT SCDETGCHVS TSTGAVVTET
VSSKSYTTAT VTHCDDNGCN TKTVTSECSK ETSATTASPK SYTTVTVTHC DDNGCNTKTV
TSEAPEATTT TTVSSQSYTT ATVTHCDDNG CKTKTVTSEA PEATTTTVSP KTYTTATVTQ
CDDNGCSTKT VTSECPEETS ATTTSPKSYT TVTVTHCDDN GCNTKTVTSE APEATTTTVS
PKTYTTATVT QCDDNGCSTK TVTSEAPKET SETSETSAAP KDIHYCHWLL NGDDNGCNVK
IITSKIPEAT STVTQLVLLQ SHTLLSLLRV LKQPH
