ID A0A1A6GWD6_NEOLE Unreviewed; 392 AA.
AC A0A1A6GWD6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Metallophosphoesterase 1 {ECO:0000256|ARBA:ARBA00017804};
DE AltName: Full=Post-GPI attachment to proteins factor 5 {ECO:0000256|ARBA:ARBA00032172};
GN ORFNames=A6R68_01197 {ECO:0000313|EMBL:OBS70264.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS70264.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS70264.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS70264.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS70264.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metallophosphoesterase required for transport of GPI-anchor
CC proteins from the endoplasmic reticulum to the Golgi. Acts in lipid
CC remodeling steps of GPI-anchor maturation by mediating the removal of a
CC side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of
CC the GPI intermediate, an essential step for efficient transport of GPI-
CC anchor proteins. {ECO:0000256|ARBA:ARBA00025587}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Interacts with GPI-anchor proteins. Interacts with TMED10.
CC {ECO:0000256|ARBA:ARBA00025873}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000256|ARBA:ARBA00004457}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004457}. Golgi apparatus, cis-
CC Golgi network membrane {ECO:0000256|ARBA:ARBA00004257}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004257}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC family. {ECO:0000256|ARBA:ARBA00008895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS70264.1}.
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; LZPO01066357; OBS70264.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6GWD6; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR CDD; cd08165; MPP_MPPE1; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR039541; MPP_MPPE1.
DR InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR PANTHER; PTHR13315; METALLO PHOSPHOESTERASE RELATED; 1.
DR PANTHER; PTHR13315:SF0; METALLOPHOSPHOESTERASE 1; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..302
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 392 AA; 45552 MW; 906BC9D9995E9831 CRC64;
MALFRWGWRR QNFHPPSRVL LLKLTVVVIS VLLFCEYFIY YIVIFQCRWP EVKXXAHGXR
QEPVLKAMFL ADTHLLGERR GHWLDKLRRE WQMERAFQTA LWLLQPEVVF ILGDIFDEGK
WSTAQAWADD VQRFQKMFXH GSHVQLKVVI GNHDIGFHYQ MSKYRIKRFE KVFGSERLFS
WKGVNFVMVN SVAMEGDGCS ICSEXEAELR EISRKLNCSR EQVQGXSQCE GEQRLPFSAP
VLLQHYPLYR ASDANCSGED AAPPEEKNVL FKEKYDVLSR EASQKLLWWF QPRLVLSGHT
HSACEVLHPG GAPEVSVPSF SWRNRNNPSF IMGSLTSRDF ALSKCYLPFE DRVLTVYGTA
AAVLAILILV HFEHLPSSFL FGWKPCRMFT RR
//