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Q53F39 (MPPE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metallophosphoesterase 1

EC=3.1.-.-
Alternative name(s):
Post-GPI attachment to proteins factor 5
Gene names
Name:MPPE1
Synonyms:PGAP5
ORF Names:PP579
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins. Ref.9

Cofactor

Binds 2 manganese ions per subunit Probable. Ref.9

Subunit structure

Interacts with GPI-anchor proteins. Interacts with TMED10. Ref.9

Subcellular location

Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatuscis-Golgi network membrane; Multi-pass membrane protein. Note: Also localizes to endoplasmic reticulum exit site. Ref.9

Tissue specificity

Expressed in brain. Ref.1

Domain

The di-lysine motif (KxKxx) acts as an endoplasmic reticulum retrieval signal. Ref.9

Sequence similarities

Belongs to the metallophosphoesterase superfamily. MPPE1 family.

Sequence caution

The sequence BAB13863.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14378.1 differs from that shown. Reason: Frameshift at position 201.

Ontologies

Keywords
   Biological processER-Golgi transport
GPI-anchor biosynthesis
Transport
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

GPI anchor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cis-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum exit site

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionGPI anchor binding

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoric diester hydrolase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q53F39-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q53F39-2)

The sequence of this isoform differs from the canonical sequence as follows:
     338-396: SITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNLLGKRKTR → TDA
Isoform 3 (identifier: Q53F39-3)

The sequence of this isoform differs from the canonical sequence as follows:
     226-226: E → EQ
     338-396: SITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNLLGKRKTR → TDA
Isoform 4 (identifier: Q53F39-4)

The sequence of this isoform differs from the canonical sequence as follows:
     227-289: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q53F39-5)

The sequence of this isoform differs from the canonical sequence as follows:
     227-256: ARGSSRCGPGPLLPTSAPVLLQHYPLYRRS → VGEHLNATGAFCPVLLRFGCSLSPLALLAL
     257-396: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Metallophosphoesterase 1
PRO_0000315727

Regions

Transmembrane27 – 4721Helical; Potential
Transmembrane356 – 37621Helical; Potential
Motif392 – 3965Di-lysine motif

Sites

Metal binding771Divalent metal cation 2 Probable
Metal binding1191Divalent metal cation 1 Probable
Metal binding1191Divalent metal cation 2 Probable
Metal binding1571Divalent metal cation 1 Probable
Metal binding2491Divalent metal cation 1 Probable
Metal binding3031Divalent metal cation 1 Probable
Metal binding3051Divalent metal cation 2 Probable

Natural variations

Alternative sequence2261E → EQ in isoform 3.
VSP_030679
Alternative sequence227 – 28963Missing in isoform 4.
VSP_030680
Alternative sequence227 – 25630ARGSS…LYRRS → VGEHLNATGAFCPVLLRFGC SLSPLALLAL in isoform 5.
VSP_030681
Alternative sequence257 – 396140Missing in isoform 5.
VSP_030682
Alternative sequence338 – 39659SITPT…KRKTR → TDA in isoform 2 and isoform 3.
VSP_030683
Natural variant1381R → Q.
Corresponds to variant rs11872520 [ dbSNP | Ensembl ].
VAR_038294
Natural variant1971V → M.
Corresponds to variant rs35611363 [ dbSNP | Ensembl ].
VAR_038295
Natural variant2681A → P. Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs662515 [ dbSNP | Ensembl ].
VAR_038296
Natural variant3361M → L.
Corresponds to variant rs16976814 [ dbSNP | Ensembl ].
VAR_038297

Experimental info

Mutagenesis771D → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis791H → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis1191D → A or N: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis1571N → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis1581H → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis2491H → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis3031H → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis3051H → A: Affects transport of GPI-anchor proteins. Ref.9
Mutagenesis392 – 3943KRK → ARA: Affects subcellular localization. Ref.9
Sequence conflict221L → S in BAB14378. Ref.2
Sequence conflict321A → T in BAB14378. Ref.2
Sequence conflict971Q → R in AAL55744. Ref.4
Sequence conflict3011S → I in AAH73994. Ref.8
Sequence conflict3641V → E in AAM00279. Ref.1
Sequence conflict3641V → E in AAM00277. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: D117BCDB1630560A

FASTA39645,141
        10         20         30         40         50         60 
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 

        70         80         90        100        110        120 
GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 

       130        140        150        160        170        180 
FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 

       190        200        210        220        230        240 
ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP 

       250        260        270        280        290        300 
TSAPVLLQHY PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL 

       310        320        330        340        350        360 
SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGSIT PTDYTLSKCY LPREDVVLII 

       370        380        390 
YCGVVGFLVV LTLTHFGLLA SPFLSGLNLL GKRKTR 

« Hide

Isoform 2 [UniParc].

Checksum: 3F0B26CB0C48B354
Show »

FASTA34038,933
Isoform 3 [UniParc].

Checksum: 39DED2417CD4BBD4
Show »

FASTA34139,061
Isoform 4 [UniParc].

Checksum: 6691B3999DC34E9E
Show »

FASTA33338,270
Isoform 5 [UniParc].

Checksum: 4BBDA145C3984B9D
Show »

FASTA25629,351

References

« Hide 'large scale' references
[1]"cDNA cloning, genomic organization and expression of the novel human metallophosphoesterase gene MPPE1 on chromosome 18p11.2."
Vuoristo J.T., Ala-Kokko L.
Cytogenet. Cell Genet. 95:60-63(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), VARIANT PRO-268.
Tissue: Embryo and Teratocarcinoma.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-268.
Tissue: Dermoid cancer.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-268.
[5]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-268.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Lung and PNS.
[9]"GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF363483, AF363482 Genomic DNA. Translation: AAM00277.1.
AF363483, AF363482 Genomic DNA. Translation: AAM00278.1.
AF363484 mRNA. Translation: AAM00279.1.
AK021647 mRNA. Translation: BAB13863.1. Different initiation.
AK023052 mRNA. Translation: BAB14378.1. Frameshift.
AK223450 mRNA. Translation: BAD97170.1.
AF289560 mRNA. Translation: AAL55744.1.
EF444996 Genomic DNA. Translation: ACA06017.1.
EF444996 Genomic DNA. Translation: ACA06018.1.
EF444996 Genomic DNA. Translation: ACA06019.1.
AP001269 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01562.1.
CH471113 Genomic DNA. Translation: EAX01565.1.
CH471113 Genomic DNA. Translation: EAX01564.1.
CH471113 Genomic DNA. Translation: EAX01569.1.
CH471113 Genomic DNA. Translation: EAX01571.1.
CH471113 Genomic DNA. Translation: EAX01567.1.
CH471113 Genomic DNA. Translation: EAX01568.1.
BC002877 mRNA. Translation: AAH02877.1.
BC073994 mRNA. Translation: AAH73994.1.
RefSeqNP_001229833.1. NM_001242904.1.
NP_075563.3. NM_023075.5.
UniGeneHs.712666.
Hs.734268.

3D structure databases

ProteinModelPortalQ53F39.
SMRQ53F39. Positions 70-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122415. 1 interaction.

PTM databases

PhosphoSiteQ53F39.

Polymorphism databases

DMDM215274110.

Proteomic databases

PaxDbQ53F39.
PRIDEQ53F39.

Protocols and materials databases

DNASU65258.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309976; ENSP00000311200; ENSG00000154889. [Q53F39-4]
ENST00000317235; ENSP00000327257; ENSG00000154889. [Q53F39-4]
ENST00000399978; ENSP00000382860; ENSG00000154889. [Q53F39-3]
ENST00000496196; ENSP00000433950; ENSG00000154889. [Q53F39-2]
ENST00000588072; ENSP00000465894; ENSG00000154889. [Q53F39-1]
GeneID65258.
KEGGhsa:65258.
UCSCuc002kqf.3. human. [Q53F39-1]
uc002kqm.3. human. [Q53F39-4]
uc010dla.2. human. [Q53F39-3]

Organism-specific databases

CTD65258.
GeneCardsGC18M012841.
H-InvDBHIX0014342.
HGNCHGNC:15988. MPPE1.
HPAHPA012639.
MIM611900. gene.
neXtProtNX_Q53F39.
PharmGKBPA134913534.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246417.
HOVERGENHBG101555.
OMAHSACEVH.
OrthoDBEOG722J8P.
PhylomeDBQ53F39.

Gene expression databases

ArrayExpressQ53F39.
BgeeQ53F39.
GenevestigatorQ53F39.

Family and domain databases

InterProIPR024654. Calcineurin-like_PHP_lpxH.
[Graphical view]
PfamPF12850. Metallophos_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMPPE1. human.
GenomeRNAi65258.
NextBio67378.
PROQ53F39.
SOURCESearch...

Entry information

Entry nameMPPE1_HUMAN
AccessionPrimary (citable) accession number: Q53F39
Secondary accession number(s): B0YJ39 expand/collapse secondary AC list , B0YJ40, B0YJ41, B5ME53, B7WNJ3, D3DUI5, D3DUI7, Q6GMP1, Q8TAD6, Q8TE26, Q8WZ32, Q9BU58, Q9H958, Q9HAI4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM