GNPAT_HUMAN
ID GNPAT_HUMAN Reviewed; 680 AA.
AC O15228; B4DNM9; Q5TBH7; Q9BWC2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Dihydroxyacetone phosphate acyltransferase {ECO:0000305};
DE Short=DAP-AT;
DE Short=DHAP-AT {ECO:0000303|PubMed:15687349};
DE EC=2.3.1.42;
DE AltName: Full=Acyl-CoA:dihydroxyacetonephosphateacyltransferase;
DE AltName: Full=Glycerone-phosphate O-acyltransferase;
GN Name=GNPAT {ECO:0000312|HGNC:HGNC:4416};
GN Synonyms=DAPAT, DHAPAT {ECO:0000303|PubMed:15687349};
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).
RC TISSUE=Brain;
RX PubMed=9459311; DOI=10.1016/s0014-5793(97)01495-6;
RA Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K., Just W.W.;
RT "Ether lipid biosynthesis: isolation and molecular characterization of
RT human dihydroxyacetonephosphate acyltransferase.";
RL FEBS Lett. 420:205-211(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 12-33, AND
RP VARIANTS RCDP2 CYS-211 AND HIS-211.
RX PubMed=9536089; DOI=10.1093/hmg/7.5.847;
RA Ofman R., Hettema E.H., Hogenhout E.M., Caruso U., Muijsers A.O.,
RA Wanders R.J.A.;
RT "Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human
RT cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia
RT punctata type 2.";
RL Hum. Mol. Genet. 7:847-853(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11237722; DOI=10.1006/bbrc.2001.4407;
RA Ofman R., Lajmir S., Wanders R.J.A.;
RT "Etherphospholipid biosynthesis and dihydroxyactetone-phosphate
RT acyltransferase: resolution of the genomic organization of the human GNPAT
RT gene and its use in the identification of novel mutations.";
RL Biochem. Biophys. Res. Commun. 281:754-760(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-586.
RC TISSUE=Lung;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15687349; DOI=10.1194/jlr.m400364-jlr200;
RA Liu D., Nagan N., Just W.W., Rodemer C., Thai T.P., Zoeller R.A.;
RT "Role of dihydroxyacetonephosphate acyltransferase in the biosynthesis of
RT plasmalogens and nonether glycerolipids.";
RL J. Lipid Res. 46:727-735(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-643, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
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 [10]
RP INVOLVEMENT IN RCDP2.
RX PubMed=21990100; DOI=10.1002/humu.21623;
RA Itzkovitz B., Jiralerspong S., Nimmo G., Loscalzo M., Horovitz D.D.,
RA Snowden A., Moser A., Steinberg S., Braverman N.;
RT "Functional characterization of novel mutations in GNPAT and AGPS, causing
RT rhizomelic chondrodysplasia punctata (RCDP) types 2 and 3.";
RL Hum. Mutat. 33:189-197(2012).
RN [11]
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 VARIANTS RCDP2 HIS-211 AND GLY-519, AND CHARACTERIZATION OF VARIANTS RCDP2
RP HIS-211 AND GLY-519.
RX PubMed=11152660; DOI=10.1093/hmg/10.2.127;
RA Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K.,
RA Just W.W.;
RT "Impaired membrane traffic in defective ether lipid biosynthesis.";
RL Hum. Mol. Genet. 10:127-136(2001).
CC -!- FUNCTION: Dihydroxyacetonephosphate acyltransferase involved in
CC plasmalogen biosynthesis. {ECO:0000269|PubMed:15687349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone
CC 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + hexadecanoyl-CoA = 1-
CC hexadecanoylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:40715,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:58303; Evidence={ECO:0000269|PubMed:15687349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716;
CC Evidence={ECO:0000305|PubMed:15687349};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBUNIT: May be part of a heterotrimeric complex composed of DAP-AT,
CC ADAP-S and a modified form of DAP-AT.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q9ES71}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9ES71}; Matrix side
CC {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the
CC lumenal side of the peroxisomal membrane. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ES71}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15228-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15228-2; Sequence=VSP_056435;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- DISEASE: Rhizomelic chondrodysplasia punctata 2 (RCDP2) [MIM:222765]: A
CC form of rhizomelic chondrodysplasia punctata, a disease characterized
CC by severely disturbed endochondral bone formation, rhizomelic
CC shortening of femur and humerus, vertebral disorders, dwarfism,
CC cataract, cutaneous lesions, facial dysmorphism, and severe
CC intellectual disability with spasticity. {ECO:0000269|PubMed:11152660,
CC ECO:0000269|PubMed:21990100, ECO:0000269|PubMed:9536089}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AJ002190; CAA05242.1; -; mRNA.
DR EMBL; AF043937; AAC24505.1; -; mRNA.
DR EMBL; AF218233; AAG17547.1; -; Genomic_DNA.
DR EMBL; AF218223; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218224; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218225; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218226; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218227; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218228; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218229; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218230; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218231; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AF218232; AAG17547.1; JOINED; Genomic_DNA.
DR EMBL; AK297982; BAG60291.1; -; mRNA.
DR EMBL; AL117352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000450; AAH00450.1; -; mRNA.
DR CCDS; CCDS1592.1; -. [O15228-1]
DR RefSeq; NP_001303279.1; NM_001316350.1. [O15228-2]
DR RefSeq; NP_055051.1; NM_014236.3. [O15228-1]
DR AlphaFoldDB; O15228; -.
DR BioGRID; 114021; 75.
DR CORUM; O15228; -.
DR IntAct; O15228; 35.
DR STRING; 9606.ENSP00000355607; -.
DR BindingDB; O15228; -.
DR ChEMBL; CHEMBL4494; -.
DR SwissLipids; SLP:000000148; -.
DR iPTMnet; O15228; -.
DR MetOSite; O15228; -.
DR PhosphoSitePlus; O15228; -.
DR SwissPalm; O15228; -.
DR BioMuta; GNPAT; -.
DR EPD; O15228; -.
DR jPOST; O15228; -.
DR MassIVE; O15228; -.
DR MaxQB; O15228; -.
DR PaxDb; O15228; -.
DR PeptideAtlas; O15228; -.
DR PRIDE; O15228; -.
DR ProteomicsDB; 4711; -.
DR ProteomicsDB; 48518; -. [O15228-1]
DR Antibodypedia; 34685; 289 antibodies from 30 providers.
DR DNASU; 8443; -.
DR Ensembl; ENST00000366647.9; ENSP00000355607.4; ENSG00000116906.13. [O15228-1]
DR GeneID; 8443; -.
DR KEGG; hsa:8443; -.
DR MANE-Select; ENST00000366647.9; ENSP00000355607.4; NM_014236.4; NP_055051.1.
DR UCSC; uc001hup.5; human. [O15228-1]
DR CTD; 8443; -.
DR DisGeNET; 8443; -.
DR GeneCards; GNPAT; -.
DR HGNC; HGNC:4416; GNPAT.
DR HPA; ENSG00000116906; Low tissue specificity.
DR MalaCards; GNPAT; -.
DR MIM; 222765; phenotype.
DR MIM; 602744; gene.
DR neXtProt; NX_O15228; -.
DR OpenTargets; ENSG00000116906; -.
DR Orphanet; 309796; Rhizomelic chondrodysplasia punctata type 2.
DR PharmGKB; PA28795; -.
DR VEuPathDB; HostDB:ENSG00000116906; -.
DR eggNOG; KOG3730; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; O15228; -.
DR OMA; RFNLEWY; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; O15228; -.
DR TreeFam; TF313360; -.
DR BioCyc; MetaCyc:HS04068-MON; -.
DR BRENDA; 2.3.1.42; 2681.
DR PathwayCommons; O15228; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-75896; Plasmalogen biosynthesis.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; O15228; -.
DR UniPathway; UPA00940; -.
DR BioGRID-ORCS; 8443; 27 hits in 1080 CRISPR screens.
DR ChiTaRS; GNPAT; human.
DR GenomeRNAi; 8443; -.
DR Pharos; O15228; Tchem.
DR PRO; PR:O15228; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15228; protein.
DR Bgee; ENSG00000116906; Expressed in gluteal muscle and 211 other tissues.
DR ExpressionAtlas; O15228; baseline and differential.
DR Genevisible; O15228; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0030913; P:paranodal junction assembly; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR028353; DHAPAT.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500063; DHAPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Cataract;
KW Direct protein sequencing; Disease variant; Dwarfism; Membrane; Peroxisome;
KW Phosphoprotein; Reference proteome; Rhizomelic chondrodysplasia punctata;
KW Transferase.
FT CHAIN 1..680
FT /note="Dihydroxyacetone phosphate acyltransferase"
FT /id="PRO_0000195246"
FT MOTIF 162..167
FT /note="HXXXXD motif"
FT MOTIF 678..680
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98192"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES71"
FT MOD_RES 643
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 27..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056435"
FT VARIANT 211
FT /note="R -> C (in RCDP2; dbSNP:rs121434440)"
FT /evidence="ECO:0000269|PubMed:9536089"
FT /id="VAR_006357"
FT VARIANT 211
FT /note="R -> H (in RCDP2; complete loss of activity;
FT dbSNP:rs121434439)"
FT /evidence="ECO:0000269|PubMed:11152660,
FT ECO:0000269|PubMed:9536089"
FT /id="VAR_006358"
FT VARIANT 495
FT /note="V -> I (in dbSNP:rs11122266)"
FT /id="VAR_030696"
FT VARIANT 519
FT /note="D -> G (in RCDP2; 70% reduction in activity;
FT dbSNP:rs11558492)"
FT /evidence="ECO:0000269|PubMed:11152660"
FT /id="VAR_025897"
FT VARIANT 586
FT /note="Y -> H (in dbSNP:rs17849315)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030697"
FT CONFLICT 26
FT /note="S -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 77188 MW; BDF624CCD4D92477 CRC64;
MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF AMKCYTPLVY
KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR EEVSEILDEM SHKLRLGAIR
FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL
PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF
FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV
PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE
DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL WLKGLTQAFG
GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG DSEVVDGLML QHITLLMCSA
YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC
YLLCKSEAIQ VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY
LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC IFNVNEPATT
KLEEMLGCKT PIGKPATAKL
