HPF1_YEAST
ID HPF1_YEAST Reviewed; 967 AA.
AC Q05164; D6W1R6; Q08294;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Haze protective factor 1;
DE Flags: Precursor;
GN Name=HPF1; OrderedLocusNames=YOL155C; ORFNames=AOF1001;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8810044;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<709::aid-yea957>3.0.co;2-1;
RA Gamo F.-J., Lafuente M.J., Casamayor A., Arino J., Aldea M., Casas C.,
RA Herrero E., Gancedo C.;
RT "Analysis of the DNA sequence of a 15,500 bp fragment near the left
RT telomere of chromosome XV from Saccharomyces cerevisiae reveals a putative
RT sugar transporter, a carboxypeptidase homologue and two new open reading
RT frames.";
RL Yeast 12:709-714(1996).
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 PROTEIN SEQUENCE OF 479-504, FUNCTION, AND BIOTECHNOLOGY.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=10775354; DOI=10.1021/jf9905020;
RA Dupin I.V.S., Stockdale V.J., Williams P.J., Jones G.P., Markides A.J.,
RA Waters E.J.;
RT "Saccharomyces cerevisiae mannoproteins that protect wine from protein
RT haze: evaluation of extraction methods and immunolocalization.";
RL J. Agric. Food Chem. 48:1086-1095(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11748726; DOI=10.1002/yea.790;
RA Horie T., Isono K.;
RT "Cooperative functions of the mannoprotein-encoding genes in the biogenesis
RT and maintenance of the cell wall in Saccharomyces cerevisiae.";
RL Yeast 18:1493-1503(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11935221; DOI=10.1007/s00294-001-0264-9;
RA Terashima H., Fukuchi S., Nakai K., Arisawa M., Hamada K., Yabuki N.,
RA Kitada K.;
RT "Sequence-based approach for identification of cell wall proteins in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 40:311-316(2002).
RN [8]
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: Involved in cell wall organization and biosynthesis.
CC {ECO:0000269|PubMed:10775354, ECO:0000269|PubMed:11748726,
CC ECO:0000269|PubMed:17024473}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP), enriched at bud sites and their neighborhood.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains.
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 -!- BIOTECHNOLOGY: Probable mannoprotein called haze protective factor from
CC wine that is able to prevent visible wine protein haze formation. This
CC mannoprotein showed haze-protective activity against wine proteins and
CC BSA when either was heated in white wine. {ECO:0000269|PubMed:10775354,
CC ECO:0000269|PubMed:17024473}.
CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61860.1; Type=Miscellaneous discrepancy; Note=Erroneous sequence assembling in the Ser-rich region leading to a longer sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of froth and haze - Issue 78
CC of January 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/078";
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DR EMBL; X89715; CAA61860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z74897; CAA99177.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10632.1; -; Genomic_DNA.
DR PIR; S66852; S66852.
DR RefSeq; NP_014487.1; NM_001183408.1.
DR AlphaFoldDB; Q05164; -.
DR SMR; Q05164; -.
DR BioGRID; 34263; 98.
DR IntAct; Q05164; 1.
DR MINT; Q05164; -.
DR STRING; 4932.YOL155C; -.
DR iPTMnet; Q05164; -.
DR MaxQB; Q05164; -.
DR PaxDb; Q05164; -.
DR PRIDE; Q05164; -.
DR EnsemblFungi; YOL155C_mRNA; YOL155C; YOL155C.
DR GeneID; 854010; -.
DR KEGG; sce:YOL155C; -.
DR SGD; S000005515; HPF1.
DR VEuPathDB; FungiDB:YOL155C; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000179085; -.
DR HOGENOM; CLU_016111_1_0_1; -.
DR InParanoid; Q05164; -.
DR OMA; NIWINTG; -.
DR BioCyc; YEAST:G3O-33543-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q05164; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q05164; 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; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0015926; F:glucosidase activity; ISS:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..946
FT /note="Haze protective factor 1"
FT /id="PRO_0000268177"
FT PROPEP 947..967
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000268178"
FT REPEAT 93..105
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 106..118
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 119..131
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 132..144
FT /note="1-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 153..165
FT /note="1-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 166..178
FT /note="1-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 179..191
FT /note="1-7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 192..204
FT /note="1-8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 205..217
FT /note="1-9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 218..230
FT /note="1-10; approximate"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 234..247
FT /note="1-11; approximate"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 248..259
FT /note="1-12; approximate"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 266..278
FT /note="1-13"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 745..780
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 781..815
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 816..854
FT /note="2-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 855..893
FT /note="2-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 894..902
FT /note="2-5; truncated"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 72..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..278
FT /note="13 X approximate repeats, Ser-rich"
FT REGION 745..902
FT /note="4.5 X approximate tandem repeats, Thr-rich"
FT REGION 836..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 946
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
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 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 967 AA; 94706 MW; 7BFC01EA243A561E CRC64;
MFNRFNKLQA ALALVLYSQS ALGQYYTNSS SIASNSSTAV SSTSSGSVSI SSSIELTSST
SDVSSSLTEL TSSSTEVSSS IAPSTSSSEV SSSITSSGSS VSGSSSITSS GSSVSSSSSA
TESGSSASGS SSATESGSSV SGSSTSITSG SSSATESGSS VSGSTSATES GSSASGSSSA
TESGSSASGS SSATESGSSV SGSSSATESG SSVSGSSSAT ESGSASSVPS SSGSVTESGS
SSSASESSIT QSGTASGSSA SSTSGSVTQS GSSVSGSSAS SAPGISSSIP QSTSSASTAS
GSITSGTLSS ITSSASSATA TASNSLSSSD GTIYLPSTTI SGDITLTGSV IATEAVEVAA
GGKLTLLDGD KYVFSADFII HGGVFVEKSK PTYPGTEFDI SGENFDVSGT FNAEEPAASS
ASAYSFTPGS FDNSGDISLS LSESTKGEVT FSPYSNSGAF SFSNAILNGG SVSGLQRRAE
SGSVNNGEIN LENGSTYVVV EPVSGSGTIN IISGNLYLHY PDTFTGQTVV FKGEGVLAVD
PTETNTTPIP VVGYTGENQI AITADVTALS YDSATGVLTA TQGNSQFSFS IGTGFSSSGF
NVSEGTFAGA YAYYLNYGGV VASSATPSST STTSGATNST SGSTSFGASV TGSTASTSFG
ASVTGSTAST LISGSPSVYT TTLTYATTTS TVVVSCSETT DSNGNVYTIT TTVPCSSTTA
TITSCDETGC HVTTSTGTVA TETVSSKSYT TVTVTHCDNN GCNTKTVTSE CPEETSATTT
SPKSYTTVTV THCDDNGCNT KTVTSEAPEA TTTTVSPKTY TTATVTQCDD NGCSTKTVTS
EAPKETSETS ETSAAPKTYT TATVTQCDDN GCNVKIITSQ IPEATSTVTA TSASPKSYTT
VTSEGSKATS LTTAISKASS AISTYSKSAA PIKTSTGIIV QSEGIAAGLN ANTLNALVGI
FVLAFFN
