ID AWA1_YEASK Reviewed; 1713 AA. AC Q8TGE1; G2WM83; Q76C74; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 13-SEP-2023, entry version 80. DE RecName: Full=Cell wall protein AWA1; DE Flags: Precursor; GN Name=AWA1; ORFNames=SYK7_061821; OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=721032; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND BIOTECHNOLOGY. RC STRAIN=Kyokai no. 7 / NBRC 101557; RX PubMed=11916725; DOI=10.1128/aem.68.4.2018-2025.2002; RA Shimoi H., Sakamoto K., Okuda M., Atthi R., Iwashita K., Ito K.; RT "The Awa1 gene is required for the foam-forming phenotype and cell surface RT hydrophobicity of sake yeast."; RL Appl. Environ. Microbiol. 68:2018-2025(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557, and Kyokai no. 701; RX PubMed=16233582; DOI=10.1016/s1389-1723(04)70158-9; RA Miyashita K., Sakamoto K., Kitagaki H., Iwashita K., Ito K., Shimoi H.; RT "Cloning and analysis of the AWA1 gene of a nonfoaming mutant of a sake RT Yeast."; RL J. Biosci. Bioeng. 97:14-18(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557; RX PubMed=21900213; DOI=10.1093/dnares/dsr029; RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D., RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S., RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T., RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A., RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A., RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.; RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no. RT 7."; RL DNA Res. 18:423-434(2011). CC -!- FUNCTION: Involved in cell wall organization and biosynthesis. Confers CC cell surface hydrophobicity (CSH). CC -!- SUBCELLULAR LOCATION: Secreted, cell wall CC {ECO:0000269|PubMed:11916725}. Membrane {ECO:0000269|PubMed:11916725}; CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11916725}. CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). 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 -!- POLYMORPHISM: Half of the downstream region (residues 1035 to 1713) of CC the AWA1 gene was lost in the nonfoaming strain K701 due to a CC chromosomal recombination event. CC -!- BIOTECHNOLOGY: Responsible for the thick foam layer formation on the CC sake mash during the fermentation process. CC {ECO:0000269|PubMed:11916725}. CC -!- MISCELLANEOUS: 'Awa' means 'foam' in Japanese. CC -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB071164; BAB85832.1; -; Genomic_DNA. DR EMBL; AB110100; BAD06576.1; -; Genomic_DNA. DR EMBL; AB110101; BAD06577.1; -; Genomic_DNA. DR EMBL; DG000051; GAA26176.1; -; Genomic_DNA. DR AlphaFoldDB; Q8TGE1; -. DR SMR; Q8TGE1; -. DR GlyCosmos; Q8TGE1; 4 sites, No reported glycans. DR HOGENOM; CLU_240507_0_0_1; -. DR Proteomes; UP000001608; Chromosome XV. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR InterPro; IPR000992; SRP1_TIP1. DR PANTHER; PTHR31002:SF34; CELL WALL PROTEIN CWP1-RELATED; 1. DR PANTHER; PTHR31002; SERIPAUPERIN; 1. DR Pfam; PF00660; SRP1_TIP1; 1. DR PROSITE; PS00724; SRP1_TIP1; 1. PE 1: Evidence at protein level; KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor; KW Lipoprotein; Membrane; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..1692 FT /note="Cell wall protein AWA1" FT /id="PRO_0000268175" FT PROPEP 1693..1713 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000268176" FT REGION 80..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 256..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 359..939 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1582..1603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 1692 FT /note="GPI-anchor amidated alanine" FT /evidence="ECO:0000255" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 1036..1713 FT /note="Missing (in strain: Kyokai no. 701, non-foaming FT mutant derivative of Kyokai no. 7)" SQ SEQUENCE 1713 AA; 166884 MW; 9321A296EB586404 CRC64; MFNRFNKLQA ALALVLYSQS ALGQYYTSSS IASNSSTAVS STSSGSVSIS SSIELTSSTS DVSSSLTELT SSFTEVSSSI APSTSSSEVS SSITSSGSSV SGSSSITSSG SSVSSSSPYD ERFNSLDLSV HVSAGFSAGV SVGLEPSATT ASVTTTLSPY DERVNLIELG VYVSDMRAHL VEYLLFQAAH STEPHPTEIA AAFLDHGDFT TRLTGISGDE VTRMITGVPW YSTRLKPAIS EALAKDGIYT AIPTSTSTTS DTYISSSSPS QVTSSAEPTT VSGVTSSVEP TRSSQVTSSA EPTTVSEITS SAEPLSSSKA TTSAESISSN QITISSELIV SSVITSSSEI PSSIEVLTSS GISSSVEPTS LVGPSSDESI SSTESLSATS TPLAVSSTVV TSSTDSVSPN IPFSEISSSP ESSTAITSGS SSATESGSSV SGSTSATESG SSASGSSSAT ESGSSVSGST SATESGSASS VPSSSGSVTE SGSSSSASES SITQSGTASG SSVSSTSGSV TQSGSSVSGS SASSAPGISS SIPQSTSSAS TASGSITSGT LTSITSGSSS ATESGSSVSG SSSATESGSS VSGSTSATES GSSVSGSTSA TESGSSASGS SSATESGSSV SGSTSATESG SSVSGSTSAT ESGSSASGSS SATESGSASS VPSSSGSVTE SGSSSSASES SITQSGTASG SSASSTSGSV TQSGSSVSGS SASSAPGISS SIPQSTSSAS TASGSITSGT LTSITSGSSS ATESGSSASG SSSATESGSS VSGSTSATES GSSVSGSTSA TESGSSASGS SSATESGSSV SGSTSATESG SSASGSSSAT ESGSASSVPS SSGSVTESGS SSSASESSIT QSGTASGSSA SSTSGSVTQS GSSVSGSSAS STSGSVTQSG SSVSGSSASS APGISSSIPQ STSSASTASG SITSGTLTSI TSSASSASAT ASNSLSSSDG TIYLPTTTIS GDLTLTGKVI ATEGVVVAAG AKLTLLDGDK YSFSADLKVY GDLLVKKSKE TYPGTEFDIS GENFDVTGNF NAEESAATSA SIYSFTPSSF DNSGDISLSL SKSKKGEVTF SPYSNSGAFS FSNAILNGGS VSGLQRRDDT EGSVNNGEIN LDNGSTYVIV EPVSGKGTVN IISGNLYLHY PDTFTGQTVV FKGEGVLAVD PTESNTTPIP VVGYTGENQI AITADVTALS YDSATGVLTA TQGNSQFSFS IGTGFSSSGF NVSEGTFAGA YAYYLNYGGV VASSATPSST STTSGATNST SGSTSFGASV TGSTASTSFG ASVTGSTAST LISGSPSVYT TTLTYATTTS TVVVSCSETT DSNGNVYTIT TTVPCSSTTA TITSCDETGC HVTTSTGTVA TETVSSKSYT TVTVTHCDNN GCNTKTVTSE APEATTTTVS PKTYTTATVT QCDDNGCSTK TVTSECPEET SATTTSPKSY TTVTVTHCDD NGCNTKTVTS EAPEATTTTV SPKTYTTATV TQCDDNGCST KTVTSECPEE TSATTTSPKS YTTVTVTHCD DNGCNTKTVT SEAPEATTTT VSPKTYTTAT VTQCDDNGCS TKTVTSEAPK ETSETSETSA APKTYTTATV TQCDDNGCNV KIITSQIPEA TSTVTATSAS PKSYTTVTSE GSKATSLTTA ISKASSAIST YSKSAAPIKT STGIIVQSEG IAAGLNANTL NALVGIFVLA FFN //