ID A0A1S3NH95_SALSA Unreviewed; 286 AA.
AC A0A1S3NH95;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphatidate phosphatase PPAPDC1A-like {ECO:0000313|RefSeq:XP_014014824.1};
GN Name=LOC106579442 {ECO:0000313|RefSeq:XP_014014824.1};
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_014014824.1};
RN [1] {ECO:0000313|RefSeq:XP_014014824.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014014824.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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_014014824.1; XM_014159349.1.
DR AlphaFoldDB; A0A1S3NH95; -.
DR KEGG; sasa:106579442; -.
DR OrthoDB; 25293at2759; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000087266; Chromosome ssa19.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF90; PHOSPHOLIPID PHOSPHATASE 4; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..233
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 286 AA; 32264 MW; 1E1CF67DF0BBE4B5 CRC64;
MNMSPPDLRK NVRELALEIG IRVLLFGVFV FTEFLEPFER VIQPEEQWLY KNPLVESDHI
PKRVMFAISF LTPLAVIFVV KIIQRTDKTE IKEACLAVSL ALALNGVFTN TIKLIVGRPR
PDYFQRCFPD GQVNIKMLCT GEPDLVSEGR KSFPSSHSSF AFSGLGFTSF YLAGKLQCFT
DRGRGYSWRL CAMLLPLYSA LMIALSRTCD YKHHWQDAFV GGVIGLLFAY ICYRQHYPPF
LHMDCHLPYA SLAKAPHLIS AQGDPRVLPT ENATSLPLKG LTEGPL
//
