CCW14_YEAST
ID CCW14_YEAST Reviewed; 238 AA.
AC O13547; D6VZ26;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Covalently-linked cell wall protein 14;
DE AltName: Full=Inner cell wall protein;
DE Flags: Precursor;
GN Name=CCW14; Synonyms=ICWP, SSR1; OrderedLocusNames=YLR390W-A;
GN ORFNames=YLR391W-A;
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], CHARACTERIZATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9079899; DOI=10.1128/jb.179.7.2154-2162.1997;
RA Moukadiri I., Armero J., Abad A., Sentandreu R., Zueco J.;
RT "Identification of a mannoprotein present in the inner layer of the cell
RT wall of Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:2154-2162(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 23-35, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=10322008; DOI=10.1128/jb.181.10.3076-3086.1999;
RA Mrsa V., Ecker M., Strahl-Bolsinger S., Nimtz M., Lehle L., Tanner W.;
RT "Deletion of new covalently linked cell wall glycoproteins alters the
RT electrophoretic mobility of phosphorylated wall components of Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 181:3076-3086(1999).
RN [5]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR.
RX PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA de Koster C.G.;
RT "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT identification of proteins covalently attached via
RT glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL J. Biol. Chem. 280:20894-20901(2005).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Component of the inner layer of the cell wall.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP).
CC -!- PTM: Extensively O-glycosylated.
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 -!- SIMILARITY: Belongs to the CCW14 family. {ECO:0000305}.
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DR EMBL; U19729; AAB82348.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09692.1; -; Genomic_DNA.
DR PIR; S77699; S77699.
DR RefSeq; NP_013495.1; NM_001184303.1.
DR AlphaFoldDB; O13547; -.
DR BioGRID; 31650; 76.
DR DIP; DIP-1301N; -.
DR STRING; 4932.YLR390W-A; -.
DR iPTMnet; O13547; -.
DR MaxQB; O13547; -.
DR PaxDb; O13547; -.
DR PRIDE; O13547; -.
DR EnsemblFungi; YLR390W-A_mRNA; YLR390W-A; YLR390W-A.
DR GeneID; 851107; -.
DR KEGG; sce:YLR390W-A; -.
DR SGD; S000006429; CCW14.
DR VEuPathDB; FungiDB:YLR390W-A; -.
DR eggNOG; ENOG502S1X2; Eukaryota.
DR HOGENOM; CLU_078308_0_0_1; -.
DR InParanoid; O13547; -.
DR OMA; NCYYSSR; -.
DR BioCyc; YEAST:G3O-32518-MON; -.
DR PRO; PR:O13547; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; O13547; 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; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR Pfam; PF05730; CFEM; 1.
DR SMART; SM00747; CFEM; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Isopeptide bond; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10322008"
FT CHAIN 23..217
FT /note="Covalently-linked cell wall protein 14"
FT /id="PRO_0000020881"
FT PROPEP 218..238
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020882"
FT REGION 91..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 217
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 238 AA; 23268 MW; 450042DC144C12B8 CRC64;
MRATTLLSSV VSLALLSKEV LATPPACLLA CVAQVGKSSS TCDSLNQVTC YCEHENSAVK
KCLDSICPNN DADAAYSAFK SSCSEQNASL GDSSSSASSS ASSSSKASSS TKASSSSASS
STKASSSSAS SSTKASSSSA APSSSKASST ESSSSSSSST KAPSSEESSS TYVSSSKQAS
STSEAHSSSA ASSTVSQETV SSALPTSTAV ISTFSEGSGN VLEAGKSVFI AAVAAMLI
