ID A6MKP2_CALJA Unreviewed; 133 AA.
AC A6MKP2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Lipid phosphate phosphohydrolase 2-like protein {ECO:0000313|EMBL:ABQ22633.1};
DE Flags: Fragment;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:ABQ22633.1};
RN [1] {ECO:0000313|EMBL:ABQ22633.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hippocampus {ECO:0000313|EMBL:ABQ22633.1};
RX PubMed=17592630; DOI=10.1186/1471-2164-8-190;
RA Datson N.A., Morsink M.C., Atanasova S., Armstrong V.W., Zischler H.,
RA Schlumbohm C., Dutilh B.E., Huynen M.A., Waegele B., Ruepp A.,
RA de Kloet E.R., Fuchs E.;
RT "Development of the first marmoset-specific DNA microarray (EUMAMA): a new
RT genetic tool for large-scale expression profiling in a non-human primate.";
RL BMC Genomics 8:190-190(2007).
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 EMBL; EF215140; ABQ22633.1; -; mRNA.
DR AlphaFoldDB; A6MKP2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03384; PAP2_wunen; 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:SF25; PHOSPHOLIPID PHOSPHATASE 2; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000313|EMBL:ABQ22633.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..85
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ22633.1"
SQ SEQUENCE 133 AA; 15206 MW; B55F3473BCC8CB60 CRC64;
DVTEARLSFY SGHASFGMYC MVFLALYVQA RLCWKWARLL RPTVQFFLVA FALYVGYTRV
SDHKHHWNDV LAGLLQGALV AGLTVRYISD FFKARPPQHC PKEEELERKP SLSLTVTLGE
ADHNHYGYPH SSS
//