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Database: UniProt
Entry: H9FYN2_MACMU
LinkDB: H9FYN2_MACMU
Original site: H9FYN2_MACMU 
ID   H9FYN2_MACMU            Unreviewed;       396 AA.
AC   H9FYN2;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Metallophosphoesterase 1 {ECO:0000256|ARBA:ARBA00017804};
DE   AltName: Full=Post-GPI attachment to proteins factor 5 {ECO:0000256|ARBA:ARBA00032172};
GN   Name=MPPE1 {ECO:0000313|EMBL:AFE79741.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE79741.1};
RN   [1] {ECO:0000313|EMBL:AFE79741.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE79741.1}, Testis
RC   {ECO:0000313|EMBL:AFI38049.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH33677.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
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}.
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DR   EMBL; JU335988; AFE79741.1; -; mRNA.
DR   EMBL; JU335989; AFE79742.1; -; mRNA.
DR   EMBL; JU476873; AFH33677.1; -; mRNA.
DR   EMBL; JV047978; AFI38049.1; -; mRNA.
DR   AlphaFoldDB; H9FYN2; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..306
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
SQ   SEQUENCE   396 AA;  45269 MW;  755C4A2CD9AD8EFA CRC64;
     MAMIEVGFER QNFYPLKRKS ALLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTAYD
     GEQASHEPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDV
     FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS
     ERLFSWKGIN FVMVNSVALN GDGCGICSEA EAELIEVSHR LNCSREARGS RRCGPGPLLP
     VSAPVLLQHY PLYRRSDANC SGDDAAPPEE RNIPFKENYD VLSREASQKL LWWLQPRLVL
     SGHTHSACEV HHGGRVPEFS VPSFSWRNRN NPSFIMGSIT PTDYALSKCY LPREDVVLVI
     YCGAVGFLVV LTLSHLGLLA SPFLSGLNLL RKRKTR
//
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