ID   DOPP_NEUCR              Reviewed;         282 AA.
AC   Q9C2M6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative dolichyldiphosphatase;
DE            EC=3.6.1.43;
DE   AltName: Full=Dolichyl pyrophosphate phosphatase;
GN   ORFNames=17E5.220, NCU03718;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dolichyldiphosphatase 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; AL513467; CAC28848.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32258.1; -; Genomic_DNA.
DR   RefSeq; XP_961494.1; XM_956401.2.
DR   AlphaFoldDB; Q9C2M6; -.
DR   STRING; 5141.EFNCRP00000003484; -.
DR   EnsemblFungi; EAA32258; EAA32258; NCU03718.
DR   GeneID; 3877658; -.
DR   KEGG; ncr:NCU03718; -.
DR   VEuPathDB; FungiDB:NCU03718; -.
DR   HOGENOM; CLU_074922_0_0_1; -.
DR   InParanoid; Q9C2M6; -.
DR   OMA; VYATLIW; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0047874; F:dolichyldiphosphatase activity; IBA:GO_Central.
DR   GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..282
FT                   /note="Putative dolichyldiphosphatase"
FT                   /id="PRO_0000215628"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          121..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  31635 MW;  C052B616E9FA8C02 CRC64;
     MADNVTPLAS LSLTHVYYNP DDPISLLCAW LALVPQALCV VYATLIWSTR EAEVILMFAG
     QLACEAANFA LKRLIKEERP ARIHSTGGKG YGMPSSHAQF VSFWAVALGL FLLARHTPRE
     QQQQQQQKQK QRERKKQVTN VKTTTTNGSG NGSLFKTLTD SATDLERYAH EPWSFAHRFV
     ASLGALVLAG AVAWSRTYLG YHTEKQVLVG CGAGTLCAVA WFVVTHVVRQ SGLLGQILDF
     PVVRWFRVRD LVVEEDLPQA GWEKWEEQRV ARREVEERKK AL