ADAS_HUMAN
ID ADAS_HUMAN Reviewed; 658 AA.
AC O00116; A5D8U9; Q2TU35;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26 {ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9553082};
DE AltName: Full=Aging-associated gene 5 protein;
DE AltName: Full=Alkylglycerone-phosphate synthase;
DE Flags: Precursor;
GN Name=AGPS; ORFNames=AAG5;
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].
RC TISSUE=Liver;
RX PubMed=9187299; DOI=10.1016/s0005-2760(97)00014-3;
RA de Vet E.C.J.M., van den Broek B.T.E., van den Bosch H.;
RT "Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA
RT reveals the presence of a peroxisomal targeting signal 2.";
RL Biochim. Biophys. Acta 1346:25-29(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human aging-associated gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 MRNA].
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8399344; DOI=10.1016/0005-2760(93)90070-p;
RA Zomer A.W., de Weerd W.F., Langeveld J., van den Bosch H.;
RT "Ether lipid synthesis: purification and identification of alkyl
RT dihydroxyacetone phosphate synthase from guinea-pig liver.";
RL Biochim. Biophys. Acta 1170:189-196(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-347, AND
RP IDENTIFICATION BY MASS 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND THR-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND THR-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 VARIANT RCDP3 HIS-419, CHARACTERIZATION OF VARIANT RCDP3, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9553082; DOI=10.1074/jbc.273.17.10296;
RA de Vet E.C.J.M., Ijlst L., Oostheim W., Wanders R.J.A., van den Bosch H.;
RT "Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome biogenesis
RT disorders and identification of the point mutation underlying a single
RT enzyme deficiency.";
RL J. Biol. Chem. 273:10296-10301(1998).
RN [13]
RP VARIANTS RCDP3 ILE-309 AND PRO-469.
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).
RN [14]
RP VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568, AND CHARACTERIZATION OF
RP VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568.
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).
CC -!- FUNCTION: Catalyzes the exchange of the acyl chain in acyl-
CC dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol,
CC yielding the first ether linked intermediate, i.e. alkyl-
CC dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid
CC biosynthesis. {ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9553082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol =
CC 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+);
CC Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26;
CC Evidence={ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9553082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36172;
CC Evidence={ECO:0000305|PubMed:8399344, ECO:0000305|PubMed:9553082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-
CC hexadecylglycerone 3-phosphate + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40659, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16125, ChEBI:CHEBI:58303, ChEBI:CHEBI:77429;
CC Evidence={ECO:0000269|PubMed:9553082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40660;
CC Evidence={ECO:0000305|PubMed:9553082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid
CC = a 1-acylglycerone 3-phosphate + hexadecanoate;
CC Xref=Rhea:RHEA:40727, ChEBI:CHEBI:7896, ChEBI:CHEBI:57534,
CC ChEBI:CHEBI:57560, ChEBI:CHEBI:58303;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40728;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P97275};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P97275}.
CC -!- INTERACTION:
CC O00116; Q9BQQ3: GORASP1; NbExp=7; IntAct=EBI-2838732, EBI-2561458;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P97275}. Peroxisome
CC {ECO:0000250|UniProtKB:P97275}.
CC -!- DISEASE: Rhizomelic chondrodysplasia punctata 3 (RCDP3) [MIM:600121]: 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:9553082}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; Y09443; CAA70591.1; -; mRNA.
DR EMBL; AY544121; AAT11152.1; -; mRNA.
DR EMBL; AK314259; BAG36924.1; -; mRNA.
DR EMBL; BC141820; AAI41821.1; -; mRNA.
DR CCDS; CCDS2275.1; -.
DR RefSeq; NP_003650.1; NM_003659.3.
DR AlphaFoldDB; O00116; -.
DR SMR; O00116; -.
DR BioGRID; 114110; 176.
DR CORUM; O00116; -.
DR IntAct; O00116; 24.
DR MINT; O00116; -.
DR STRING; 9606.ENSP00000264167; -.
DR ChEMBL; CHEMBL4295643; -.
DR SwissLipids; SLP:000000611; -.
DR GlyGen; O00116; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00116; -.
DR MetOSite; O00116; -.
DR PhosphoSitePlus; O00116; -.
DR SwissPalm; O00116; -.
DR BioMuta; AGPS; -.
DR EPD; O00116; -.
DR jPOST; O00116; -.
DR MassIVE; O00116; -.
DR MaxQB; O00116; -.
DR PaxDb; O00116; -.
DR PeptideAtlas; O00116; -.
DR PRIDE; O00116; -.
DR ProteomicsDB; 47718; -.
DR Antibodypedia; 33922; 199 antibodies from 29 providers.
DR DNASU; 8540; -.
DR Ensembl; ENST00000264167.11; ENSP00000264167.4; ENSG00000018510.18.
DR GeneID; 8540; -.
DR KEGG; hsa:8540; -.
DR MANE-Select; ENST00000264167.11; ENSP00000264167.4; NM_003659.4; NP_003650.1.
DR UCSC; uc002ull.3; human.
DR CTD; 8540; -.
DR DisGeNET; 8540; -.
DR GeneCards; AGPS; -.
DR HGNC; HGNC:327; AGPS.
DR HPA; ENSG00000018510; Low tissue specificity.
DR MalaCards; AGPS; -.
DR MIM; 600121; phenotype.
DR MIM; 603051; gene.
DR neXtProt; NX_O00116; -.
DR OpenTargets; ENSG00000018510; -.
DR Orphanet; 309803; Rhizomelic chondrodysplasia punctata type 3.
DR PharmGKB; PA24624; -.
DR VEuPathDB; HostDB:ENSG00000018510; -.
DR eggNOG; KOG1233; Eukaryota.
DR GeneTree; ENSGT00940000156112; -.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; O00116; -.
DR OMA; PRCHDEV; -.
DR OrthoDB; 824020at2759; -.
DR PhylomeDB; O00116; -.
DR TreeFam; TF313830; -.
DR BioCyc; MetaCyc:HS00389-MON; -.
DR BRENDA; 2.5.1.26; 2681.
DR PathwayCommons; O00116; -.
DR Reactome; R-HSA-75896; Plasmalogen biosynthesis.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins.
DR SignaLink; O00116; -.
DR UniPathway; UPA00781; -.
DR BioGRID-ORCS; 8540; 34 hits in 1095 CRISPR screens.
DR ChiTaRS; AGPS; human.
DR GenomeRNAi; 8540; -.
DR Pharos; O00116; Tbio.
DR PRO; PR:O00116; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00116; protein.
DR Bgee; ENSG00000018510; Expressed in sperm and 191 other tissues.
DR ExpressionAtlas; O00116; baseline and differential.
DR Genevisible; O00116; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
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:0008609; F:alkylglycerone-phosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:MGI.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR46568; PTHR46568; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cataract; Disease variant; Dwarfism; FAD; Flavoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; Rhizomelic chondrodysplasia punctata; Transferase;
KW Transit peptide.
FT TRANSIT 1..58
FT /note="Peroxisome"
FT /evidence="ECO:0000250"
FT CHAIN 59..658
FT /note="Alkyldihydroxyacetonephosphate synthase,
FT peroxisomal"
FT /id="PRO_0000020431"
FT DOMAIN 202..384
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..617
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT REGION 654..658
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 578
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 234..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 303..309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 316..319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 368..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT SITE 419
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000269|PubMed:9553082"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 347
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 182
FT /note="R -> Q (in RCDP3; severely reduced protein levels)"
FT /evidence="ECO:0000269|PubMed:21990100"
FT /id="VAR_066929"
FT VARIANT 309
FT /note="T -> I (in RCDP3; dbSNP:rs121434412)"
FT /evidence="ECO:0000269|PubMed:11152660"
FT /id="VAR_025895"
FT VARIANT 419
FT /note="R -> H (in RCDP3; loss of enzyme activity;
FT dbSNP:rs121434411)"
FT /evidence="ECO:0000269|PubMed:9553082"
FT /id="VAR_005002"
FT VARIANT 469
FT /note="L -> P (in RCDP3; dbSNP:rs121434413)"
FT /evidence="ECO:0000269|PubMed:11152660"
FT /id="VAR_025896"
FT VARIANT 471
FT /note="E -> K (in RCDP3; severely reduced protein levels)"
FT /evidence="ECO:0000269|PubMed:21990100"
FT /id="VAR_066930"
FT VARIANT 568
FT /note="T -> M (in RCDP3; does not affect protein levels;
FT dbSNP:rs387907214)"
FT /evidence="ECO:0000269|PubMed:21990100"
FT /id="VAR_066931"
SQ SEQUENCE 658 AA; 72912 MW; 0E97AE86B513DF32 CRC64;
MAEAAAAAGG TGLGAGASYG SAADRDRDPD PDRAGRRLRV LSGHLLGRPR EALSTNECKA
RRAASAATAA PTATPAAQES GTIPKKRQEV MKWNGWGYND SKFIFNKKGQ IELTGKRYPL
SGMGLPTFKE WIQNTLGVNV EHKTTSKASL NPSDTPPSVV NEDFLHDLKE TNISYSQEAD
DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS
VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
EPDSLEFSTV GGWVSTRASG MKKNIYGNIE DLVVHIKMVT PRGIIEKSCQ GPRMSTGPDI
HHFIMGSEGT LGVITEATIK IRPVPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL
MDNKQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH
EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYIRDLALE YYVLGESFET SAPWDRVVDL
CRNVKERITR ECKEKGVQFA PFSTCRVTQT YDAGACIYFY FAFNYRGISD PLTVFEQTEA
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKEYVDPNN IFGNRNLL
