CAX4_YEAST
ID CAX4_YEAST Reviewed; 239 AA.
AC P53223; D6VUH3; Q45U47;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000303|PubMed:10024662};
DE EC=3.6.1.43 {ECO:0000269|PubMed:11504728};
DE AltName: Full=Dolichyl pyrophosphate phosphatase {ECO:0000303|PubMed:10024662};
GN Name=CAX4; Synonyms=CWH8 {ECO:0000303|PubMed:10024662};
GN OrderedLocusNames=YGR036C;
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=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=10024662; DOI=10.1093/glycob/9.3.243;
RA van Berkel M.A.A., Rieger M., te Heesen S., Ram A.F.J., van den Ende H.,
RA Aebi M., Klis F.M.;
RT "The Saccharomyces cerevisiae CWH8 gene is required for full levels of
RT dolichol-linked oligosaccharides in the endoplasmic reticulum and for
RT efficient N-glycosylation.";
RL Glycobiology 9:243-253(1999).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=11504728; DOI=10.1074/jbc.m105544200;
RA Fernandez F., Rush J.S., Toke D.A., Han G.-S., Quinn J.E., Carman G.M.,
RA Choi J.-Y., Voelker D.R., Aebi M., Waechter C.J.;
RT "The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a
RT luminally oriented active site in the endoplasmic reticulum of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:41455-41464(2001).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Non-essential protein which is required for efficient N-
CC glycosylation. Necessary for maintaining optimal levels of dolichol-
CC linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very
CC high rate and dolichyl monophosphate at a much lower rate. Does not act
CC on phosphatidate. {ECO:0000269|PubMed:10024662,
CC ECO:0000269|PubMed:11504728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphate + H2O = a dolichyl phosphate + H(+) +
CC phosphate; Xref=Rhea:RHEA:14385, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC COMP:9529, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57497, ChEBI:CHEBI:57683; EC=3.6.1.43;
CC Evidence={ECO:0000269|PubMed:11504728};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for dolichyl diphosphate {ECO:0000269|PubMed:11504728};
CC KM=40 uM for dolichyl phosphate {ECO:0000269|PubMed:11504728};
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:11504728};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11504728}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11504728}.
CC -!- DISRUPTION PHENOTYPE: Causes an elevation in dolichyl diphosphate
CC levels. {ECO:0000269|PubMed:11504728}.
CC -!- SIMILARITY: Belongs to the dolichyldiphosphatase family. {ECO:0000305}.
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DR EMBL; DQ115390; AAZ22452.1; -; Genomic_DNA.
DR EMBL; Z72821; CAA97024.1; -; Genomic_DNA.
DR EMBL; AY557771; AAS56097.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08134.1; -; Genomic_DNA.
DR PIR; S64327; S64327.
DR RefSeq; NP_011550.3; NM_001181165.3.
DR AlphaFoldDB; P53223; -.
DR SMR; P53223; -.
DR BioGRID; 33281; 68.
DR DIP; DIP-5237N; -.
DR IntAct; P53223; 2.
DR MINT; P53223; -.
DR STRING; 4932.YGR036C; -.
DR MaxQB; P53223; -.
DR PaxDb; P53223; -.
DR PRIDE; P53223; -.
DR EnsemblFungi; YGR036C_mRNA; YGR036C; YGR036C.
DR GeneID; 852924; -.
DR KEGG; sce:YGR036C; -.
DR SGD; S000003268; CAX4.
DR VEuPathDB; FungiDB:YGR036C; -.
DR eggNOG; KOG3146; Eukaryota.
DR GeneTree; ENSGT00390000013112; -.
DR HOGENOM; CLU_074922_0_1_1; -.
DR InParanoid; P53223; -.
DR OMA; VYATLIW; -.
DR BioCyc; YEAST:YGR036C-MON; -.
DR Reactome; R-SCE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:P53223; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53223; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IDA:SGD.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR InterPro; IPR039666; Dolpp1/Cax4.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR11247:SF1; PTHR11247:SF1; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..239
FT /note="Dolichyldiphosphatase"
FT /id="PRO_0000215629"
FT TOPO_DOM 1..34
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 27649 MW; C8EC49CBFC08F8F8 CRC64;
MNSTAAAINP NPNVIPFDDT YILYDSHDFL SFLSAYFSLM PILVLAFYLS WFIITRELEA
CIVAFGQLMN EIFNNVIKNI IKQPRPVSFG ASFQNDTIRS GYGMPSAHSQ FMGFCFTYNS
LKIYTSWKNL NFLEKCIFSG ALALLSFCVC FSRVYLHYHN LDQVIVGFSV GALTGSLYFF
IVGIIRELGL INWFLKLRIV RLFYMTDSYN LAPLTLKENY EAYWKRINQR SFNDKSKRD
