ID DHC24_HUMAN Reviewed; 516 AA. AC Q15392; B7Z817; D3DQ51; Q9HBA8; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 02-NOV-2016, entry version 158. DE RecName: Full=Delta(24)-sterol reductase; DE EC=1.3.1.72; DE AltName: Full=24-dehydrocholesterol reductase; DE AltName: Full=3-beta-hydroxysterol delta-24-reductase; DE AltName: Full=Diminuto/dwarf1 homolog; DE AltName: Full=Seladin-1; DE Flags: Precursor; GN Name=DHCR24; Synonyms=KIAA0018; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=11007892; RA Greeve I., Hermans-Borgmeyer I., Brellinger C., Kasper D., RA Gomez-Isla T., Behl C., Levkau B., Nitsch R.M.; RT "The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to RT Alzheimer's disease-associated neurodegeneration and oxidative RT stress."; RL J. Neurosci. 20:7345-7352(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND RP VARIANTS DESMOS LYS-191; THR-294; ASN-306 AND SER-471. RX PubMed=11519011; DOI=10.1086/323473; RA Waterham H.R., Koster J., Romeijn G.J., Hennekam R.C.M., Vreken P., RA Andersson H.C., FitzPatrick D.R., Kelley R.I., Wanders R.J.A.; RT "Mutations in the 3beta-hydroxysterol delta24-reductase gene cause RT desmosterolosis, an autosomal recessive disorder of cholesterol RT biosynthesis."; RL Am. J. Hum. Genet. 69:685-694(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by RT analysis of randomly sampled cDNA clones from human immature myeloid RT cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [4] RP SEQUENCE REVISION TO C-TERMINUS. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6] 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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., RA Buerckstuemmer T., 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 FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=22010141; DOI=10.1530/JME-11-0132; RA Lu X., Li Y., Liu J., Cao X., Wang X., Wang D., Seo H., Gao B.; RT "The membrane topological analysis of 3 {beta}-hydroxysteroid-delta24 RT reductase (DHCR24) on endoplasmic reticulum."; RL J. Mol. Endocrinol. 48:1-9(2012). RN [11] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] 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., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Catalyzes the reduction of the delta-24 double bond of CC sterol intermediates. Protects cells from oxidative stress by CC reducing caspase 3 activity during apoptosis induced by oxidative CC stress. Also protects against amyloid-beta peptide-induced CC apoptosis. {ECO:0000269|PubMed:11007892, CC ECO:0000269|PubMed:11519011, ECO:0000269|PubMed:22010141}. CC -!- CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 5- CC alpha-cholesta-7,24-dien-3-beta-ol + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Golgi apparatus membrane; Single-pass membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15392-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15392-2; Sequence=VSP_056479; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and adrenal gland CC with moderate expression in liver, lung, spleen, prostate and CC spinal cord. Low expression in heart, uterus and prostate. CC Undetectable in blood cells. In the brain, strongly expressed in CC cortical regions, substantia nigra, caudate nucleus, hippocampus, CC medulla oblongata and pons. In brains affected by Alzheimer CC disease, expression in the inferior temporal lobe is substantially CC lower than in the frontal cortex. {ECO:0000269|PubMed:11007892, CC ECO:0000269|PubMed:11519011}. CC -!- DISEASE: Desmosterolosis (DESMOS) [MIM:602398]: Rare autosomal CC recessive disorder characterized by multiple congenital anomalies CC and elevated levels of the cholesterol precursor desmosterol in CC plasma, tissue, and cultured cells. {ECO:0000269|PubMed:11519011}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase CC type 4 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00718}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA02806.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF261758; AAG17288.1; -; mRNA. DR EMBL; AF398342; AAL15644.1; -; Genomic_DNA. DR EMBL; AF398336; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; AF398337; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; AF398338; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; AF398339; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; AF398340; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; AF398341; AAL15644.1; JOINED; Genomic_DNA. DR EMBL; D13643; BAA02806.3; ALT_INIT; mRNA. DR EMBL; AK302774; BAH13803.1; -; mRNA. DR EMBL; AC096536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06663.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06664.1; -; Genomic_DNA. DR EMBL; BC004375; AAH04375.1; -; mRNA. DR EMBL; BC011669; AAH11669.1; -; mRNA. DR CCDS; CCDS600.1; -. [Q15392-1] DR RefSeq; NP_055577.1; NM_014762.3. [Q15392-1] DR UniGene; Hs.498727; -. DR ProteinModelPortal; Q15392; -. DR BioGrid; 108064; 26. DR IntAct; Q15392; 16. DR STRING; 9606.ENSP00000360316; -. DR ChEMBL; CHEMBL2331059; -. DR SwissLipids; SLP:000001223; -. DR iPTMnet; Q15392; -. DR PhosphoSitePlus; Q15392; -. DR SwissPalm; Q15392; -. DR BioMuta; DHCR24; -. DR DMDM; 20141421; -. DR EPD; Q15392; -. DR MaxQB; Q15392; -. DR PaxDb; Q15392; -. DR PeptideAtlas; Q15392; -. DR PRIDE; Q15392; -. DR DNASU; 1718; -. DR Ensembl; ENST00000371269; ENSP00000360316; ENSG00000116133. [Q15392-1] DR GeneID; 1718; -. DR KEGG; hsa:1718; -. DR UCSC; uc001cyc.2; human. [Q15392-1] DR CTD; 1718; -. DR DisGeNET; 1718; -. DR GeneCards; DHCR24; -. DR HGNC; HGNC:2859; DHCR24. DR HPA; CAB037247; -. DR HPA; HPA063005; -. DR MalaCards; DHCR24; -. DR MIM; 602398; phenotype. DR MIM; 606418; gene. DR neXtProt; NX_Q15392; -. DR OpenTargets; ENSG00000116133; -. DR Orphanet; 35107; Desmosterolosis. DR PharmGKB; PA27320; -. DR eggNOG; KOG1262; Eukaryota. DR eggNOG; COG0277; LUCA. DR GeneTree; ENSGT00390000008338; -. DR HOGENOM; HOG000243421; -. DR HOVERGEN; HBG051349; -. DR InParanoid; Q15392; -. DR KO; K09828; -. DR OMA; VKKTYDP; -. DR OrthoDB; EOG091G044Z; -. DR PhylomeDB; Q15392; -. DR TreeFam; TF313170; -. DR BioCyc; ZFISH:HS03985-MONOMER; -. DR BRENDA; 1.3.1.72; 2681. DR Reactome; R-HSA-6807047; Cholesterol biosynthesis via desmosterol. DR Reactome; R-HSA-6807062; Cholesterol biosynthesis via lathosterol. DR UniPathway; UPA00063; -. DR ChiTaRS; DHCR24; human. DR GeneWiki; 24-dehydrocholesterol_reductase; -. DR GenomeRNAi; 1718; -. DR PRO; PR:Q15392; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000116133; -. DR CleanEx; HS_DHCR24; -. DR ExpressionAtlas; Q15392; baseline and differential. DR Genevisible; Q15392; HS. DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000246; F:delta24(24-1) sterol reductase activity; IMP:UniProtKB. DR GO; GO:0050614; F:delta24-sterol reductase activity; EXP:Reactome. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IPI:UniProtKB. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; NAS:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB. DR GO; GO:0033489; P:cholesterol biosynthetic process via desmosterol; TAS:Reactome. DR GO; GO:0033490; P:cholesterol biosynthetic process via lathosterol; TAS:Reactome. DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl. DR GO; GO:0061024; P:membrane organization; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0055114; P:oxidation-reduction process; IMP:UniProtKB. DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:1901214; P:regulation of neuron death; NAS:UniProtKB. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB. DR GO; GO:0043588; P:skin development; ISS:UniProtKB. DR GO; GO:0009888; P:tissue development; IMP:UniProtKB. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cholesterol biosynthesis; KW Cholesterol metabolism; Complete proteome; Disease mutation; KW Endoplasmic reticulum; FAD; Flavoprotein; Golgi apparatus; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Signal; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 516 Delta(24)-sterol reductase. FT /FTId=PRO_0000007230. FT TOPO_DOM 23 31 Lumenal. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TOPO_DOM 53 516 Cytoplasmic. {ECO:0000255}. FT DOMAIN 58 234 FAD-binding PCMH-type. FT {ECO:0000255|PROSITE-ProRule:PRU00718}. FT NP_BIND 163 175 FAD. {ECO:0000255}. FT SITE 122 123 Cleavage; by caspase. {ECO:0000255}. FT SITE 383 384 Cleavage; by caspase. {ECO:0000255}. FT VAR_SEQ 1 76 MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLP FT LSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQK -> MG FT AGEQNRQSAHCVQGICGYLEGDEEGEEGEVRST (in FT isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056479. FT VARIANT 191 191 E -> K (in DESMOS; dbSNP:rs28939093). FT {ECO:0000269|PubMed:11519011}. FT /FTId=VAR_012732. FT VARIANT 294 294 N -> T (in DESMOS; dbSNP:rs281797257). FT {ECO:0000269|PubMed:11519011}. FT /FTId=VAR_012733. FT VARIANT 306 306 K -> N (in DESMOS; dbSNP:rs281797256). FT {ECO:0000269|PubMed:11519011}. FT /FTId=VAR_012734. FT VARIANT 471 471 Y -> S (in DESMOS; dbSNP:rs28939092). FT {ECO:0000269|PubMed:11519011}. FT /FTId=VAR_012735. SQ SEQUENCE 516 AA; 60101 MW; F9A769446FE19E59 CRC64; MEPAVSLAVC ALLFLLWVRL KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY YVRAWVVFKL SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV SLRVGKYKKT HKNIMINLMD ILEVDTKKQI VRVEPLVTMG QVTALLTSIG WTLPVLPELD DLTVGGLIMG TGIESSSHKY GLFQHICTAY ELVLADGSFV RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL RFEPVRGLEA ICAKFTHESQ RQENHFVEGL LYSLDEAVIM TGVMTDEAEP SKLNSIGNYY KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI FRYLFGWMVP PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCLQQALHT FQNDIHVYPI WLCPFILPSQ PGLVHPKGNE AELYIDIGAY GEPRVKHFEA RSCMRQLEKF VRSVHGFQML YADCYMNREE FWEMFDGSLY HKLREKLGCQ DAFPEVYDKI CKAARH //