ID   CIS3_YEAS6              Reviewed;         225 AA.
AC   B5VL27;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Cell wall mannoprotein CIS3;
DE   AltName: Full=Covalently-linked cell wall protein 5/11;
DE   AltName: Full=Protein with internal repeats 4;
DE   AltName: Full=Soluble cell wall protein 8;
DE   Flags: Precursor;
GN   Name=CIS3; ORFNames=AWRI1631_100510;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- FUNCTION: Component of the outer cell wall layer. Required for
CC       stability of the cell wall and for optimal growth. Required for
CC       resistance against several antifungal and cell wall-perturbing agents
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC       Note=Covalently attached to the cell wall. Localizes predominantly on
CC       the surface of growing buds (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The PIR1/2/3 repeat is required for the covalent linkage to the
CC       cell wall. {ECO:0000250}.
CC   -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC       via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC       of glutamic acid, arising from Gln-74 within the PIR1/2/3 repeat, and
CC       hydroxyl groups of glucoses of beta-1,3-glucan chains. {ECO:0000250}.
CC   -!- PTM: Extensively O-mannosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR   EMBL; ABSV01001268; EDZ71363.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VL27; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR000420; Yeast_PIR.
DR   Pfam; PF00399; PIR; 1.
DR   PROSITE; PS00929; PIR_REPEAT_1; 1.
DR   PROSITE; PS50256; PIR_REPEAT_2; 1.
PE   3: Inferred from homology;
KW   Cell wall; Cell wall biogenesis/degradation;
KW   Cleavage on pair of basic residues; Glycoprotein; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   PROPEP          22..64
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377610"
FT   CHAIN           65..225
FT                   /note="Cell wall mannoprotein CIS3"
FT                   /id="PRO_0000377611"
FT   REPEAT          65..82
FT                   /note="PIR1/2/3"
FT   REGION          78..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            64..65
FT                   /note="Cleavage; by KEX2"
FT                   /evidence="ECO:0000250"
FT   SITE            74
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        68
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        78
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        102
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        104
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        108
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        109
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        111
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        114
FT                   /note="O-linked (Man) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        115
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        116
FT                   /note="O-linked (Man) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  23028 MW;  D3B6FBDFED5E6A50 CRC64;
     MQFKNVALAA SVAALSATAS AEGYTPGEPW STLTPTGSIS CGAAEYTTTF GIAVQAITSS
     KAKRDVISQI GDGQVQATSA AATDSQVQAS STATPTSSEK ISSSASKTSS TNATSSSCAT
     PSLKDSSCKN SGTLELTLKD GVLTDAKGRI GSIVANRQFQ FDGPPPQAGA IYAAGWSITE
     DGYLALGDSD VFYQCLSGNF YNLYDQNVAE QCSAIHLEAV SLVDC