ID   CIS3_YEAS7              Reviewed;         225 AA.
AC   A6ZQH4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 38.
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=SCY_3135;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000044; EDN63226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQH4; -.
DR   EnsemblFungi; EDN63226; EDN63226; SCY_3135.
DR   HOGENOM; CLU_039662_2_0_1; -.
DR   Proteomes; UP000007060; 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_0000377612"
FT   CHAIN           65..225
FT                   /note="Cell wall mannoprotein CIS3"
FT                   /id="PRO_0000377613"
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