ID DCW1_YEAST Reviewed; 449 AA. AC P36091; D6VXP1; Q66R60; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Mannan endo-1,6-alpha-mannosidase DCW1; DE EC=3.2.1.101; DE AltName: Full=Defective cell wall 1; DE AltName: Full=Endo-alpha-1->6-D-mannanase DCW1; DE Flags: Precursor; GN Name=DCW1; OrderedLocusNames=YKL046C; ORFNames=YKL259; 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 204508 / S288c; RX PubMed=8154189; DOI=10.1002/yea.320091212; RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.; RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a RT new gene encoding a putative histone and seven new open reading frames."; RL Yeast 9:1379-1384(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION. RX PubMed=12421307; DOI=10.1046/j.1365-2958.2002.03244.x; RA Kitagaki H., Wu H., Shimoi H., Ito K.; RT "Two homologous genes, DCW1 (YKL046c) and DFG5, are essential for cell RT growth and encode glycosylphosphatidylinositol (GPI)-anchored membrane RT proteins required for cell wall biogenesis in Saccharomyces cerevisiae."; RL Mol. Microbiol. 46:1011-1022(2002). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Required for normal synthesis of the cell wall. CC {ECO:0000269|PubMed:12421307}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in CC unbranched (1->6)-mannans.; EC=3.2.1.101; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12421307}; CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12421307}. Note=GPI- CC anchored plasma membrane protein (GPI-PMP). CC -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}. 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; X71621; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z28046; CAA81881.1; -; Genomic_DNA. DR EMBL; AY723839; AAU09756.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09111.1; -; Genomic_DNA. DR PIR; S37867; S37867. DR RefSeq; NP_012878.1; NM_001179612.1. DR AlphaFoldDB; P36091; -. DR SMR; P36091; -. DR BioGRID; 34087; 94. DR IntAct; P36091; 2. DR MINT; P36091; -. DR STRING; 4932.YKL046C; -. DR CAZy; GH76; Glycoside Hydrolase Family 76. DR GlyCosmos; P36091; 12 sites, No reported glycans. DR GlyGen; P36091; 12 sites. DR PaxDb; 4932-YKL046C; -. DR PeptideAtlas; P36091; -. DR EnsemblFungi; YKL046C_mRNA; YKL046C; YKL046C. DR GeneID; 853820; -. DR KEGG; sce:YKL046C; -. DR AGR; SGD:S000001529; -. DR SGD; S000001529; DCW1. DR VEuPathDB; FungiDB:YKL046C; -. DR eggNOG; ENOG502QSWP; Eukaryota. DR HOGENOM; CLU_025694_1_2_1; -. DR InParanoid; P36091; -. DR OMA; QQSFKGY; -. DR OrthoDB; 2718577at2759; -. DR BioCyc; YEAST:G3O-31847-MONOMER; -. DR BioGRID-ORCS; 853820; 1 hit in 10 CRISPR screens. DR PRO; PR:P36091; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36091; Protein. DR GO; GO:0005933; C:cellular bud; HDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC. DR GO; GO:0007117; P:budding cell bud growth; IGI:SGD. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IDA:SGD. DR Gene3D; 1.50.10.20; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR005198; Glyco_hydro_76. DR InterPro; IPR014480; Mannan-1_6-alpha_mannosidase. DR PANTHER; PTHR12145:SF36; MANNAN ENDO-1,6-ALPHA-MANNOSIDASE DCW1; 1. DR PANTHER; PTHR12145; UNCHARACTERIZED; 1. DR Pfam; PF03663; Glyco_hydro_76; 1. DR PIRSF; PIRSF016302; Man_a_manosd; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. PE 1: Evidence at protein level; KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..428 FT /note="Mannan endo-1,6-alpha-mannosidase DCW1" FT /id="PRO_0000012125" FT PROPEP 429..449 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000012126" FT LIPID 428 FT /note="GPI-anchor amidated glycine" FT /evidence="ECO:0000255" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 84 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 225 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 281 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 362 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 420 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 276 FT /note="T -> A (in Ref. 4; AAU09756)" FT /evidence="ECO:0000305" SQ SEQUENCE 449 AA; 49565 MW; DECFE9CAFD9579D5 CRC64; MLVNKVIGLL GVLFATRFTN AVELDLDNYE SLQNATSLIA YGLMDYYTGN QYGKTVGMFS DPYYWWEAGG AWGCMLDYWF FMDNDTYNDE IIAAMIHQAG DDNDYIPLNQ STTEGNDDQA FWGIAAMTAA ERNFTNPPEN EPQWLYLAQA VFNTMALRWD ADSCGGGLRW QIFVWNSGYD YKNTVSNGAL FHIAARLARY TGNQTYVDWA EKVYEWMVGV NLISNGTYKY VYDGVSIDDN CTKVTSYQWT YNQGLLLAGS AYLYNFTGSD LWHTRTKEFL NASQVFFHDG IVYEAACQGP NSCNTDQRSF KAYFARFLGV TAQLVPETRN QIMSWLNTSA IAAAKSCSGG TDGHTCGLNW FNGTWDGMYG LGEQMSALEV MVNTRALDKP APYTAENGGS SVGDGAAGTQ AQPTNLAPLN ITKGSKAGAG IITAVIGISI VACALWLVF //