GPI8_HUMAN
ID GPI8_HUMAN Reviewed; 395 AA.
AC Q92643; B2R7K3; B4E2M3; O14822; Q5TG77;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=GPI-anchor transamidase;
DE Short=GPI transamidase;
DE EC=3.-.-.-;
DE AltName: Full=GPI8 homolog;
DE Short=hGPI8;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class K protein;
DE Short=PIG-K;
DE Flags: Precursor;
GN Name=PIGK; Synonyms=GPI8;
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 [MRNA] (ISOFORM 1).
RX PubMed=8978684; DOI=10.1002/j.1460-2075.1996.tb01048.x;
RA Benghezal M., Benachour A., Rusconi S., Aebi M., Conzelmann A.;
RT "Yeast Gpi8p is essential for GPI anchor attachment onto proteins.";
RL EMBO J. 15:6575-6583(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9356492; DOI=10.1073/pnas.94.23.12580;
RA Yu J., Nagarajan S., Knez J.J., Udenfriend S., Chen R., Medof M.E.;
RT "The affected gene underlying the class K glycosylphosphatidylinositol
RT (GPI) surface protein defect codes for the GPI transamidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12580-12585(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [7]
RP SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-92; HIS-164; CYS-206 AND
RP 311-GLU--PHE-395.
RX PubMed=10793132; DOI=10.1091/mbc.11.5.1523;
RA Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., Kinoshita T.;
RT "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI)
RT transamidase that mediates attachment of GPI to proteins.";
RL Mol. Biol. Cell 11:1523-1533(2000).
RN [8]
RP PROTEIN SEQUENCE OF 28-47, SUBUNIT, SUBCELLULAR LOCATION, AND MEMBRANE
RP TOPOLOGY.
RX PubMed=11483512; DOI=10.1093/emboj/20.15.4088;
RA Ohishi K., Inoue N., Kinoshita T.;
RT "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a
RT complex with GAA1 and GPI8.";
RL EMBO J. 20:4088-4098(2001).
RN [9]
RP DISULFIDE BOND FORMATION WITH PIGT, AND MUTAGENESIS OF CYS-92.
RX PubMed=12582175; DOI=10.1074/jbc.m300586200;
RA Ohishi K., Nagamune K., Maeda Y., Kinoshita T.;
RT "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T,
RT form a functionally important intermolecular disulfide bridge.";
RL J. Biol. Chem. 278:13959-13967(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP INVOLVEMENT IN NEDHCAS, AND VARIANTS NEDHCAS 33-GLN--PHE-395 DEL; PHE-53;
RP PRO-86; VAL-87; ASN-88; SER-160; VAL-184; LYS-246 AND ARG-275.
RX PubMed=32220290; DOI=10.1016/j.ajhg.2020.03.001;
RA Nguyen T.T.M., Murakami Y., Mobilio S., Niceta M., Zampino G., Philippe C.,
RA Moutton S., Zaki M.S., James K.N., Musaev D., Mu W., Baranano K.,
RA Nance J.R., Rosenfeld J.A., Braverman N., Ciolfi A., Millan F.,
RA Person R.E., Bruel A.L., Thauvin-Robinet C., Ververi A., DeVile C.,
RA Male A., Efthymiou S., Maroofian R., Houlden H., Maqbool S., Rahman F.,
RA Baratang N.V., Rousseau J., St-Denis A., Elrick M.J., Anselm I.,
RA Rodan L.H., Tartaglia M., Gleeson J., Kinoshita T., Campeau P.M.;
RT "Bi-allelic variants in the GPI transamidase subunit PIGK cause a
RT neurodevelopmental syndrome with hypotonia, cerebellar atrophy, and
RT epilepsy.";
RL Am. J. Hum. Genet. 106:484-495(2020).
CC -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC replacing a protein's C-terminal GPI attachment signal peptide with a
CC pre-assembled GPI. During this transamidation reaction, the GPI
CC transamidase forms a carbonyl intermediate with the substrate protein.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGT, PIGS, PIGU and GAA1.
CC {ECO:0000269|PubMed:10793132, ECO:0000269|PubMed:11483512}.
CC -!- INTERACTION:
CC Q92643; O43292: GPAA1; NbExp=11; IntAct=EBI-8617711, EBI-720225;
CC Q92643; Q969N2: PIGT; NbExp=10; IntAct=EBI-8617711, EBI-726383;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11483512}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11483512}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92643-2; Sequence=VSP_056457;
CC -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC normal enzyme activity.
CC -!- DISEASE: Neurodevelopmental disorder with hypotonia and cerebellar
CC atrophy, with or without seizures (NEDHCAS) [MIM:618879]: An autosomal
CC recessive neurodevelopmental disorder characterized by global
CC developmental delay, intellectual disability, hypotonia, cerebellar
CC ataxia, cerebellar atrophy, delayed motor skills, poor or absent
CC speech, and epilepsy in most patients. Some patients manifest facial
CC dysmorphism. Disease onset is in infancy.
CC {ECO:0000269|PubMed:32220290}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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; Y07596; CAA68871.1; -; mRNA.
DR EMBL; AF022913; AAB81597.1; -; mRNA.
DR EMBL; AK304340; BAG65185.1; -; mRNA.
DR EMBL; AK313015; BAG35850.1; -; mRNA.
DR EMBL; AC093433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06380.1; -; Genomic_DNA.
DR EMBL; BC020737; AAH20737.1; -; mRNA.
DR CCDS; CCDS674.1; -. [Q92643-1]
DR RefSeq; NP_005473.1; NM_005482.2. [Q92643-1]
DR PDB; 7W72; EM; 3.10 A; K=1-395.
DR PDBsum; 7W72; -.
DR AlphaFoldDB; Q92643; -.
DR SMR; Q92643; -.
DR BioGRID; 115343; 91.
DR ComplexPortal; CPX-6503; GPI-anchor transamidase complex.
DR CORUM; Q92643; -.
DR IntAct; Q92643; 17.
DR MINT; Q92643; -.
DR STRING; 9606.ENSP00000359848; -.
DR MEROPS; C13.005; -.
DR iPTMnet; Q92643; -.
DR PhosphoSitePlus; Q92643; -.
DR BioMuta; PIGK; -.
DR DMDM; 22001630; -.
DR EPD; Q92643; -.
DR jPOST; Q92643; -.
DR MassIVE; Q92643; -.
DR MaxQB; Q92643; -.
DR PaxDb; Q92643; -.
DR PeptideAtlas; Q92643; -.
DR PRIDE; Q92643; -.
DR ProteomicsDB; 5832; -.
DR ProteomicsDB; 75395; -. [Q92643-1]
DR Antibodypedia; 33483; 183 antibodies from 23 providers.
DR DNASU; 10026; -.
DR Ensembl; ENST00000370812.8; ENSP00000359848.3; ENSG00000142892.15. [Q92643-1]
DR GeneID; 10026; -.
DR KEGG; hsa:10026; -.
DR MANE-Select; ENST00000370812.8; ENSP00000359848.3; NM_005482.3; NP_005473.1.
DR UCSC; uc001dhk.4; human. [Q92643-1]
DR CTD; 10026; -.
DR DisGeNET; 10026; -.
DR GeneCards; PIGK; -.
DR HGNC; HGNC:8965; PIGK.
DR HPA; ENSG00000142892; Low tissue specificity.
DR MalaCards; PIGK; -.
DR MIM; 605087; gene.
DR MIM; 618879; phenotype.
DR neXtProt; NX_Q92643; -.
DR OpenTargets; ENSG00000142892; -.
DR PharmGKB; PA33296; -.
DR VEuPathDB; HostDB:ENSG00000142892; -.
DR eggNOG; KOG1349; Eukaryota.
DR GeneTree; ENSGT00940000156273; -.
DR InParanoid; Q92643; -.
DR OMA; PGHTNNW; -.
DR OrthoDB; 1259741at2759; -.
DR PhylomeDB; Q92643; -.
DR TreeFam; TF300848; -.
DR PathwayCommons; Q92643; -.
DR Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR.
DR SignaLink; Q92643; -.
DR SIGNOR; Q92643; -.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 10026; 32 hits in 1072 CRISPR screens.
DR ChiTaRS; PIGK; human.
DR GeneWiki; PIGK; -.
DR GenomeRNAi; 10026; -.
DR Pharos; Q92643; Tbio.
DR PRO; PR:Q92643; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92643; protein.
DR Bgee; ENSG00000142892; Expressed in endothelial cell and 196 other tissues.
DR ExpressionAtlas; Q92643; baseline and differential.
DR Genevisible; Q92643; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IMP:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:UniProtKB.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; PTHR48067; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Disulfide bond; Endoplasmic reticulum; Epilepsy;
KW GPI-anchor biosynthesis; Hydrolase; Intellectual disability; Membrane;
KW Protease; Reference proteome; Signal; Thiol protease; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:11483512,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 28..395
FT /note="GPI-anchor transamidase"
FT /id="PRO_0000026529"
FT TOPO_DOM 28..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 311..321
FT /note="Essential for GPI attachment"
FT ACT_SITE 164
FT /evidence="ECO:0000269|PubMed:10793132"
FT ACT_SITE 206
FT /evidence="ECO:0000269|PubMed:10793132"
FT DISULFID 92
FT /note="Interchain (with C-182 in PIGT)"
FT /evidence="ECO:0000269|PubMed:12582175"
FT VAR_SEQ 50..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056457"
FT VARIANT 16
FT /note="T -> A (in dbSNP:rs12723684)"
FT /id="VAR_051518"
FT VARIANT 33..395
FT /note="Missing (in NEDHCAS)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084273"
FT VARIANT 53
FT /note="S -> F (in NEDHCAS)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084274"
FT VARIANT 86
FT /note="L -> P (in NEDHCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084275"
FT VARIANT 87
FT /note="A -> V (in NEDHCAS; dbSNP:rs772948495)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084276"
FT VARIANT 88
FT /note="D -> N (in NEDHCAS; dbSNP:rs771836178)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084277"
FT VARIANT 160
FT /note="Y -> S (in NEDHCAS; dbSNP:rs1164656857)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084278"
FT VARIANT 184
FT /note="A -> V (in NEDHCAS; unknown pathological
FT significance; dbSNP:rs780683566)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084279"
FT VARIANT 246
FT /note="M -> K (in NEDHCAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084280"
FT VARIANT 275
FT /note="C -> R (in NEDHCAS)"
FT /evidence="ECO:0000269|PubMed:32220290"
FT /id="VAR_084281"
FT MUTAGEN 92
FT /note="C->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:10793132,
FT ECO:0000269|PubMed:12582175"
FT MUTAGEN 92
FT /note="C->S: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:10793132,
FT ECO:0000269|PubMed:12582175"
FT MUTAGEN 164
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10793132"
FT MUTAGEN 206
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10793132"
FT MUTAGEN 311..395
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10793132"
FT CONFLICT 1..4
FT /note="MAVT -> SLHEA (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45252 MW; AF706DDDAD13EFB2 CRC64;
MAVTDSLSRA ATVLATVLLL SFGSVAASHI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR
HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNPRNPKPA TVFSHKNMEL NVYGDDVEVD
YRSYEVTVEN FLRVLTGRIP PSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN
IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA
IGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI
TDFFGSVRKV EITTETIKLQ QDSEIMESSY KEDQMDEKLM EPLKYAEQLP VAQIIHQKPK
LKDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF
