MPPE1_HUMAN
ID MPPE1_HUMAN Reviewed; 396 AA.
AC Q53F39; B0YJ39; B0YJ40; B0YJ41; B5ME53; B7WNJ3; D3DUI5; D3DUI7; Q6GMP1;
AC Q8TAD6; Q8TE26; Q8WZ32; Q9BU58; Q9H958; Q9HAI4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Metallophosphoesterase 1 {ECO:0000305};
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 5 {ECO:0000303|PubMed:29374258};
GN Name=MPPE1 {ECO:0000312|HGNC:HGNC:15988};
GN Synonyms=PGAP5 {ECO:0000303|PubMed:29374258}; ORFNames=PP579;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RX PubMed=11978971; DOI=10.1159/000057018;
RA Vuoristo J.T., Ala-Kokko L.;
RT "cDNA cloning, genomic organization and expression of the novel human
RT metallophosphoesterase gene MPPE1 on chromosome 18p11.2.";
RL Cytogenet. Cell Genet. 95:60-63(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), AND VARIANT PRO-268.
RC TISSUE=Embryo, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-268.
RC TISSUE=Dermoid cancer;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-268.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-268.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Lung, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303;
RP HIS-305 AND 392-LYS--LYS-394, AND INTERACTION WITH GPI-ANCHOR PROTEINS AND
RP TMED10.
RX PubMed=19837036; DOI=10.1016/j.cell.2009.08.040;
RA Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.;
RT "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored
RT proteins from the ER to the Golgi.";
RL Cell 139:352-365(2009).
RN [10]
RP FUNCTION.
RX PubMed=29374258; DOI=10.1038/s41467-017-02799-0;
RA Hirata T., Mishra S.K., Nakamura S., Saito K., Motooka D., Takada Y.,
RA Kanzawa N., Murakami Y., Maeda Y., Fujita M., Yamaguchi Y., Kinoshita T.;
RT "Identification of a Golgi GPI-N-acetylgalactosamine transferase with
RT tandem transmembrane regions in the catalytic domain.";
RL Nat. Commun. 9:405-405(2018).
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:0000269|PubMed:19837036,
CC ECO:0000269|PubMed:29374258}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:19837036};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305|PubMed:19837036};
CC -!- SUBUNIT: Interacts with GPI-anchor proteins. Interacts with TMED10.
CC {ECO:0000269|PubMed:19837036}.
CC -!- INTERACTION:
CC Q53F39; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-10242229, EBI-10172181;
CC Q53F39; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-10242229, EBI-743265;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:19837036}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:19837036}. Note=Also localizes to
CC endoplasmic reticulum exit site.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q53F39-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53F39-2; Sequence=VSP_030683;
CC Name=3;
CC IsoId=Q53F39-3; Sequence=VSP_030679, VSP_030683;
CC Name=4;
CC IsoId=Q53F39-4; Sequence=VSP_030680;
CC Name=5;
CC IsoId=Q53F39-5; Sequence=VSP_030681, VSP_030682;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:11978971}.
CC -!- DOMAIN: The di-lysine motif (KxKxx) acts as an endoplasmic reticulum
CC retrieval signal. {ECO:0000269|PubMed:19837036}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13863.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14378.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF363483; AAM00277.1; -; Genomic_DNA.
DR EMBL; AF363482; AAM00277.1; JOINED; Genomic_DNA.
DR EMBL; AF363483; AAM00278.1; -; Genomic_DNA.
DR EMBL; AF363482; AAM00278.1; JOINED; Genomic_DNA.
DR EMBL; AF363484; AAM00279.1; -; mRNA.
DR EMBL; AK021647; BAB13863.1; ALT_INIT; mRNA.
DR EMBL; AK023052; BAB14378.1; ALT_FRAME; mRNA.
DR EMBL; AK223450; BAD97170.1; -; mRNA.
DR EMBL; AF289560; AAL55744.1; -; mRNA.
DR EMBL; EF444996; ACA06017.1; -; Genomic_DNA.
DR EMBL; EF444996; ACA06018.1; -; Genomic_DNA.
DR EMBL; EF444996; ACA06019.1; -; Genomic_DNA.
DR EMBL; AP001269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01562.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01565.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01564.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01569.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01571.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01567.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01568.1; -; Genomic_DNA.
DR EMBL; BC002877; AAH02877.1; -; mRNA.
DR EMBL; BC073994; AAH73994.1; -; mRNA.
DR CCDS; CCDS11853.1; -. [Q53F39-1]
DR CCDS; CCDS56054.1; -. [Q53F39-4]
DR RefSeq; NP_001229833.1; NM_001242904.1. [Q53F39-4]
DR RefSeq; NP_001306083.1; NM_001319154.1. [Q53F39-4]
DR RefSeq; NP_075563.3; NM_023075.5. [Q53F39-1]
DR RefSeq; XP_006722409.1; XM_006722346.2. [Q53F39-1]
DR RefSeq; XP_011524034.1; XM_011525732.1. [Q53F39-3]
DR RefSeq; XP_016881411.1; XM_017025922.1. [Q53F39-1]
DR RefSeq; XP_016881412.1; XM_017025923.1. [Q53F39-1]
DR RefSeq; XP_016881413.1; XM_017025924.1. [Q53F39-1]
DR RefSeq; XP_016881414.1; XM_017025925.1. [Q53F39-1]
DR RefSeq; XP_016881415.1; XM_017025926.1. [Q53F39-1]
DR RefSeq; XP_016881419.1; XM_017025930.1. [Q53F39-2]
DR AlphaFoldDB; Q53F39; -.
DR BioGRID; 122415; 88.
DR IntAct; Q53F39; 72.
DR STRING; 9606.ENSP00000465894; -.
DR GlyGen; Q53F39; 1 site.
DR iPTMnet; Q53F39; -.
DR PhosphoSitePlus; Q53F39; -.
DR BioMuta; MPPE1; -.
DR DMDM; 215274110; -.
DR EPD; Q53F39; -.
DR jPOST; Q53F39; -.
DR MassIVE; Q53F39; -.
DR MaxQB; Q53F39; -.
DR PaxDb; Q53F39; -.
DR PeptideAtlas; Q53F39; -.
DR PRIDE; Q53F39; -.
DR ProteomicsDB; 62456; -. [Q53F39-1]
DR ProteomicsDB; 62457; -. [Q53F39-2]
DR ProteomicsDB; 62458; -. [Q53F39-3]
DR ProteomicsDB; 62459; -. [Q53F39-4]
DR ProteomicsDB; 62460; -. [Q53F39-5]
DR Antibodypedia; 1617; 135 antibodies from 22 providers.
DR DNASU; 65258; -.
DR Ensembl; ENST00000309976.13; ENSP00000311200.9; ENSG00000154889.17. [Q53F39-4]
DR Ensembl; ENST00000317235.11; ENSP00000327257.6; ENSG00000154889.17. [Q53F39-4]
DR Ensembl; ENST00000496196.5; ENSP00000433950.1; ENSG00000154889.17. [Q53F39-2]
DR Ensembl; ENST00000588072.6; ENSP00000465894.1; ENSG00000154889.17. [Q53F39-1]
DR GeneID; 65258; -.
DR KEGG; hsa:65258; -.
DR MANE-Select; ENST00000588072.6; ENSP00000465894.1; NM_023075.6; NP_075563.3.
DR UCSC; uc002kqf.5; human. [Q53F39-1]
DR CTD; 65258; -.
DR DisGeNET; 65258; -.
DR GeneCards; MPPE1; -.
DR HGNC; HGNC:15988; MPPE1.
DR HPA; ENSG00000154889; Low tissue specificity.
DR MIM; 611900; gene.
DR neXtProt; NX_Q53F39; -.
DR OpenTargets; ENSG00000154889; -.
DR PharmGKB; PA134913534; -.
DR VEuPathDB; HostDB:ENSG00000154889; -.
DR eggNOG; KOG3662; Eukaryota.
DR GeneTree; ENSGT00390000013236; -.
DR InParanoid; Q53F39; -.
DR OMA; SRTLHCM; -.
DR OrthoDB; 1094620at2759; -.
DR PhylomeDB; Q53F39; -.
DR PathwayCommons; Q53F39; -.
DR SignaLink; Q53F39; -.
DR BioGRID-ORCS; 65258; 45 hits in 1080 CRISPR screens.
DR ChiTaRS; MPPE1; human.
DR GenomeRNAi; 65258; -.
DR Pharos; Q53F39; Tbio.
DR PRO; PR:Q53F39; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q53F39; protein.
DR Bgee; ENSG00000154889; Expressed in granulocyte and 194 other tissues.
DR ExpressionAtlas; Q53F39; baseline and differential.
DR Genevisible; Q53F39; HS.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR GO; GO:0062050; F:GPI-mannose ethanolamine phosphate phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:UniProtKB.
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; PTHR13315; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus;
KW GPI-anchor biosynthesis; Hydrolase; Manganese; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..396
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000315727"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 392..396
FT /note="Di-lysine motif"
FT BINDING 77
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 305
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT VAR_SEQ 226
FT /note="E -> EQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030679"
FT VAR_SEQ 227..289
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030680"
FT VAR_SEQ 227..256
FT /note="ARGSSRCGPGPLLPTSAPVLLQHYPLYRRS -> VGEHLNATGAFCPVLLRF
FT GCSLSPLALLAL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030681"
FT VAR_SEQ 257..396
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030682"
FT VAR_SEQ 338..396
FT /note="SITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNL
FT LGKRKTR -> TDA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11978971,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_030683"
FT VARIANT 138
FT /note="R -> Q (in dbSNP:rs11872520)"
FT /id="VAR_038294"
FT VARIANT 197
FT /note="V -> M (in dbSNP:rs35611363)"
FT /id="VAR_038295"
FT VARIANT 268
FT /note="A -> P (in dbSNP:rs662515)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15498874, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.7"
FT /id="VAR_038296"
FT VARIANT 336
FT /note="M -> L (in dbSNP:rs16976814)"
FT /id="VAR_038297"
FT MUTAGEN 77
FT /note="D->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 79
FT /note="H->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 119
FT /note="D->A,N: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 157
FT /note="N->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 158
FT /note="H->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 249
FT /note="H->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 303
FT /note="H->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 305
FT /note="H->A: Affects transport of GPI-anchor proteins."
FT /evidence="ECO:0000269|PubMed:19837036"
FT MUTAGEN 392..394
FT /note="KRK->ARA: Affects subcellular localization."
FT /evidence="ECO:0000269|PubMed:19837036"
FT CONFLICT 22
FT /note="L -> S (in Ref. 2; BAB14378)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> T (in Ref. 2; BAB14378)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="Q -> R (in Ref. 4; AAL55744)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> I (in Ref. 8; AAH73994)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="V -> E (in Ref. 1; AAM00279/AAM00277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45141 MW; D117BCDB1630560A CRC64;
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD
GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI
FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS
ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP
TSAPVLLQHY PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL
SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGSIT PTDYTLSKCY LPREDVVLII
YCGVVGFLVV LTLTHFGLLA SPFLSGLNLL GKRKTR
