ID A0A1S3M155_SALSA Unreviewed; 238 AA.
AC A0A1S3M155;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dolichyldiphosphatase {ECO:0000256|RuleBase:RU367078};
DE EC=3.6.1.43 {ECO:0000256|RuleBase:RU367078};
GN Name=dolpp1 {ECO:0000313|RefSeq:XP_013996937.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013996937.1};
RN [1] {ECO:0000313|RefSeq:XP_013996937.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013996937.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Required for efficient N-glycosylation. Necessary for
CC maintaining optimal levels of dolichol-linked oligosaccharides.
CC Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl
CC monophosphate at a much lower rate. Does not act on phosphatidate.
CC {ECO:0000256|ARBA:ARBA00024907, ECO:0000256|RuleBase:RU367078}.
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:0000256|ARBA:ARBA00034028,
CC ECO:0000256|RuleBase:RU367078};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367078}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367078}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367078}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the dolichyldiphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005518, ECO:0000256|RuleBase:RU367078}.
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 RefSeq; XP_013996937.1; XM_014141462.1.
DR AlphaFoldDB; A0A1S3M155; -.
DR STRING; 8030.ENSSSAP00000071384; -.
DR PaxDb; 8030-ENSSSAP00000071384; -.
DR GeneID; 106569822; -.
DR KEGG; sasa:106569822; -.
DR CTD; 57171; -.
DR OrthoDB; 989449at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR CDD; cd03382; PAP2_dolichyldiphosphatase; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR039667; Dolichyldiphosphatase_PAP2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR11247:SF1; DOLICHYLDIPHOSPHATASE 1; 1.
DR PANTHER; PTHR11247; PALMITOYL-PROTEIN THIOESTERASE/DOLICHYLDIPHOSPHATASE 1; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367078};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367078};
KW Membrane {ECO:0000256|RuleBase:RU367078};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|RuleBase:RU367078};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367078}.
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 106..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367078"
FT DOMAIN 63..180
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 238 AA; 27427 MW; C1124FF45AEFB292 CRC64;
MASEEQCSVP LRWRSISLTH IEFPAGDLTG QVLAYTSLLP IAILIGFVTL IVFKRELHTI
SSFGGLVLNE GVNWLLKHIL REPRPCEGAH TTLTTEYGMP SSHSQFIWFF VVYFFLFLYL
RMHQTNNARC VELLWRHILS ITLLGVALSV SYSRVYLLYH TWSQVFYGGV AGSTIGVVWF
FFTQEVLTPL FPKIAAWPIS EFFLVRDTSL IPNILWFEYT VTRSEARNRQ RKLGTKLQ
//
