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25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1)

 CP27B_HUMAN             Reviewed;         508 AA.
O15528; B2RC61; Q548T3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
13-FEB-2019, entry version 178.
RecName: Full=25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial;
EC=1.14.15.18 {ECO:0000269|PubMed:10518789};
AltName: Full=25-OHD-1 alpha-hydroxylase;
AltName: Full=25-hydroxyvitamin D(3) 1-alpha-hydroxylase;
Short=VD3 1A hydroxylase;
AltName: Full=Calcidiol 1-monooxygenase;
AltName: Full=Cytochrome P450 subfamily XXVIIB polypeptide 1;
AltName: Full=Cytochrome P450C1 alpha;
AltName: Full=Cytochrome P450VD1-alpha;
AltName: Full=Cytochrome p450 27B1;
Flags: Precursor;
Name=CYP27B1; Synonyms=CYP1ALPHA, CYP27B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9428799; DOI=10.1089/dna.1997.16.1499;
Fu G.K., Portale A.P., Miller W.L.;
"Complete structure of the human gene for the vitamin D 1alpha-
hydroxylase, P450c1alpha.";
DNA Cell Biol. 16:1499-1507(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Kidney;
PubMed=9344864; DOI=10.1006/bbrc.1997.7508;
Monkawa T., Yoshida T., Wakino S., Shinki T., Anazawa H., Deluca H.F.,
Suda T., Hayashi M., Saruta T.;
"Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin
D3 1 alpha-hydroxylase.";
Biochem. Biophys. Res. Commun. 239:527-533(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9415400; DOI=10.1210/mend.11.13.0035;
Fu G.K., Lin D., Zhang Y.H., Bikle D.D., Shackleton C.H., Miller W.L.,
Portale A.A.;
"Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and
mutations causing vitamin D-dependent rickets type 1.";
Mol. Endocrinol. 11:1961-1970(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12496369;
Huang D.C., Papavasiliou V., Rhim J.S., Horst R.L., Kremer R.;
"Targeted disruption of the 25-hydroxyvitamin D3 1alpha-hydroxylase
gene in ras-transformed keratinocytes demonstrates that locally
produced 1alpha,25-dihydroxyvitamin D3 suppresses growth and induces
differentiation in an autocrine fashion.";
Mol. Cancer Res. 1:56-67(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Huang D.C., Papavasiliou J., Rhim J., Kremer R.;
"Targeted disruption of the 25-hydroxyvitamin D3 1 a-hydroxylase gene
in a Ras-transformed human keratinocyte cell line: evidence for an
autocrine growth regulatory function of 1 alpha, 25-dihydroxyvitamin
D3 in vitro and in vivo.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-166.
NIEHS SNPs program;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10518789; DOI=10.1046/j.1432-1327.1999.00794.x;
Sawada N., Sakaki T., Kitanaka S., Takeyama K., Kato S., Inouye K.;
"Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase
coexpression with adrenodoxin and NADPH-adrenodoxin reductase in
Escherichia coli.";
Eur. J. Biochem. 265:950-956(1999).
[11]
VARIANTS VDDR1A HIS-107; GLU-125; PRO-335 AND SER-382.
PubMed=9486994; DOI=10.1056/NEJM199803053381004;
Kitanaka S., Takeyama K., Murayama A., Sato T., Okumura K., Nogami M.,
Hasegawa Y., Niimi H., Yanagisawa J., Tanaka T., Kato S.;
"Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase
gene in patients with pseudovitamin D-deficiency rickets.";
N. Engl. J. Med. 338:653-661(1998).
[12]
VARIANTS VDDR1A HIS-65; LYS-189; HIS-389; ILE-409; PRO-429; CYS-453
AND ARG-497.
PubMed=9837822; DOI=10.1086/302156;
Wang J.T., Lin C.-J., Burridge S.M., Fu G.K., Labuda M., Portale A.A.,
Miller W.L.;
"Genetics of vitamin D 1-alpha-hydroxylase deficiency in 17
families.";
Am. J. Hum. Genet. 63:1694-1702(1998).
[13]
VARIANTS VDDR1A TYR-323 AND GLY-478.
PubMed=10320521; DOI=10.1359/jbmr.1999.14.5.730;
Smith S.J., Rucka A.K., Berry J.L., Davies M., Mylchreest S.,
Paterson C.R., Heath D.A., Tassabehji M., Read A.P., Mee A.P.,
Mawer E.B.;
"Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three
families with pseudovitamin D-deficiency rickets resulting in loss of
functional enzyme activity in blood-derived macrophages.";
J. Bone Miner. Res. 14:730-739(1999).
[14]
VARIANTS VDDR1A ARG-321 AND CYS-389.
PubMed=10566658; DOI=10.1210/jcem.84.11.6131;
Kitanaka S., Murayama A., Sakaki T., Inouye K., Seino Y., Fukumoto S.,
Shima M., Yukizane S., Takayanagi M., Niimi H., Takeyama K., Kato S.;
"No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene
product in pseudovitamin D deficiency rickets, including that with
mild clinical manifestation.";
J. Clin. Endocrinol. Metab. 84:4111-4117(1999).
[15]
VARIANTS VDDR1A GLY-189; PHE-343; GLY-389; HIS-389 AND ILE-409.
PubMed=12050193; DOI=10.1210/jcem.87.6.8534;
Wang X., Zhang M.Y., Miller W.L., Portale A.A.;
"Novel gene mutations in patients with 1alpha-hydroxylase deficiency
that confer partial enzyme activity in vitro.";
J. Clin. Endocrinol. Metab. 87:2424-2430(2002).
-!- FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3
(25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3),
and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-
alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also
active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role
in normal bone growth, calcium metabolism, and tissue
differentiation. {ECO:0000269|PubMed:10518789}.
-!- CATALYTIC ACTIVITY:
Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
calcitriol + H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:20573, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737,
ChEBI:CHEBI:33738; EC=1.14.15.18;
Evidence={ECO:0000269|PubMed:10518789};
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol =
calcitetrol + H2O + 2 oxidized [adrenodoxin];
Xref=Rhea:RHEA:49064, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
ChEBI:CHEBI:47799; EC=1.14.15.18;
Evidence={ECO:0000269|PubMed:10518789};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.7 uM for 25-hydroxyvitamin D3
{ECO:0000269|PubMed:10518789};
KM=1.1 uM for 24,25-dihydroxyvitamin D3
{ECO:0000269|PubMed:10518789};
Vmax=3.9 pmol/min/mg enzyme with 25-hydroxyvitamin D3 as
substrate {ECO:0000269|PubMed:10518789};
Vmax=3.2 pmol/min/mg enzyme with 24,25-dihydroxyvitamin D3 as
substrate {ECO:0000269|PubMed:10518789};
-!- PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane.
-!- TISSUE SPECIFICITY: Kidney.
-!- DISEASE: Rickets vitamin D-dependent 1A (VDDR1A) [MIM:264700]: A
disorder caused by a selective deficiency of the active form of
vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective
bone mineralization and clinical features of rickets.
{ECO:0000269|PubMed:10320521, ECO:0000269|PubMed:10566658,
ECO:0000269|PubMed:12050193, ECO:0000269|PubMed:9486994,
ECO:0000269|PubMed:9837822}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp27b1/";
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EMBL; AF027152; AAC51854.1; -; Genomic_DNA.
EMBL; AB005038; BAA23416.1; -; mRNA.
EMBL; AB005989; BAA22656.1; -; mRNA.
EMBL; AB005990; BAA22657.1; -; Genomic_DNA.
EMBL; AB006987; BAA23418.1; -; Genomic_DNA.
EMBL; AF020192; AAC51853.1; -; mRNA.
EMBL; AF256213; AAG00416.1; -; Genomic_DNA.
EMBL; AF246895; AAF64299.1; -; mRNA.
EMBL; AY288916; AAP31972.1; -; Genomic_DNA.
EMBL; AK314953; BAG37458.1; -; mRNA.
EMBL; CH471054; EAW97067.1; -; Genomic_DNA.
EMBL; BC136386; AAI36387.1; -; mRNA.
CCDS; CCDS8954.1; -.
PIR; JC5713; JC5713.
RefSeq; NP_000776.1; NM_000785.3.
UniGene; Hs.524528; -.
ProteinModelPortal; O15528; -.
SMR; O15528; -.
BioGrid; 107966; 3.
STRING; 9606.ENSP00000228606; -.
BindingDB; O15528; -.
ChEMBL; CHEMBL5993; -.
DrugBank; DB01436; Alfacalcidol.
DrugBank; DB00146; Calcidiol.
DrugBank; DB01285; Corticotropin.
DrugBank; DB00153; Ergocalciferol.
GuidetoPHARMACOLOGY; 1370; -.
SwissLipids; SLP:000001478; -.
PhosphoSitePlus; O15528; -.
BioMuta; CYP27B1; -.
EPD; O15528; -.
PaxDb; O15528; -.
PeptideAtlas; O15528; -.
PRIDE; O15528; -.
ProteomicsDB; 48734; -.
TopDownProteomics; O15528; -.
Ensembl; ENST00000228606; ENSP00000228606; ENSG00000111012.
GeneID; 1594; -.
KEGG; hsa:1594; -.
UCSC; uc001spz.2; human.
CTD; 1594; -.
DisGeNET; 1594; -.
EuPathDB; HostDB:ENSG00000111012.9; -.
GeneCards; CYP27B1; -.
H-InvDB; HIX0171662; -.
HGNC; HGNC:2606; CYP27B1.
MalaCards; CYP27B1; -.
MIM; 264700; phenotype.
MIM; 609506; gene.
neXtProt; NX_O15528; -.
OpenTargets; ENSG00000111012; -.
Orphanet; 289157; Hypocalcemic vitamin D-dependent rickets.
PharmGKB; PA27099; -.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00940000153297; -.
HOGENOM; HOG000253961; -.
HOVERGEN; HBG106909; -.
InParanoid; O15528; -.
KO; K07438; -.
OMA; NSWRFAP; -.
OrthoDB; 826997at2759; -.
PhylomeDB; O15528; -.
TreeFam; TF105094; -.
BRENDA; 1.14.13.13; 2681.
Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
Reactome; R-HSA-211916; Vitamins.
Reactome; R-HSA-5579014; Defective CYP27B1 causes Rickets vitamin D-dependent 1A (VDDR1A).
SIGNOR; O15528; -.
UniPathway; UPA00955; -.
GeneWiki; 25-Hydroxyvitamin_D3_1-alpha-hydroxylase; -.
GenomeRNAi; 1594; -.
PRO; PR:O15528; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111012; Expressed in 98 organ(s), highest expression level in adult mammalian kidney.
ExpressionAtlas; O15528; baseline and differential.
Genevisible; O15528; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
GO; GO:0004498; F:calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0030282; P:bone mineralization; IEP:BHF-UCL.
GO; GO:0036378; P:calcitriol biosynthetic process from calciol; IDA:BHF-UCL.
GO; GO:0055074; P:calcium ion homeostasis; IMP:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; ISS:BHF-UCL.
GO; GO:0046697; P:decidualization; IEP:BHF-UCL.
GO; GO:0070314; P:G1 to G0 transition; IMP:BHF-UCL.
GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:BHF-UCL.
GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IDA:BHF-UCL.
GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0030500; P:regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IEP:BHF-UCL.
GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0033280; P:response to vitamin D; IDA:BHF-UCL.
GO; GO:0042369; P:vitamin D catabolic process; IEA:Ensembl.
GO; GO:0042359; P:vitamin D metabolic process; IDA:BHF-UCL.
GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Heme; Iron; Membrane;
Metal-binding; Mitochondrion; Monooxygenase; Oxidoreductase;
Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 508 25-hydroxyvitamin D-1 alpha hydroxylase,
mitochondrial.
/FTId=PRO_0000003622.
METAL 455 455 Iron (heme axial ligand). {ECO:0000250}.
VARIANT 65 65 Q -> H (in VDDR1A; dbSNP:rs868704228).
{ECO:0000269|PubMed:9837822}.
/FTId=VAR_016969.
VARIANT 107 107 R -> H (in VDDR1A; complete loss of
activity; dbSNP:rs28934604).
{ECO:0000269|PubMed:9486994}.
/FTId=VAR_016952.
VARIANT 125 125 G -> E (in VDDR1A; complete loss of
activity; dbSNP:rs28934605).
{ECO:0000269|PubMed:9486994}.
/FTId=VAR_016953.
VARIANT 166 166 V -> L (in dbSNP:rs8176344).
{ECO:0000269|Ref.6}.
/FTId=VAR_018841.
VARIANT 189 189 E -> G (in VDDR1A; 22% of wild-type
activity; dbSNP:rs118204012).
{ECO:0000269|PubMed:12050193}.
/FTId=VAR_016954.
VARIANT 189 189 E -> K (in VDDR1A; 11% of wild-type
activity). {ECO:0000269|PubMed:9837822}.
/FTId=VAR_016967.
VARIANT 321 321 T -> R (in VDDR1A; complete loss of
activity; dbSNP:rs118204007).
{ECO:0000269|PubMed:10566658}.
/FTId=VAR_016955.
VARIANT 323 323 S -> Y (in VDDR1A).
{ECO:0000269|PubMed:10320521}.
/FTId=VAR_016970.
VARIANT 335 335 R -> P (in VDDR1A; complete loss of
activity; dbSNP:rs28934606).
{ECO:0000269|PubMed:9486994}.
/FTId=VAR_016956.
VARIANT 343 343 L -> F (in VDDR1A; 2.3% of wild-type
activity; dbSNP:rs118204011).
{ECO:0000269|PubMed:12050193}.
/FTId=VAR_016957.
VARIANT 382 382 P -> S (in VDDR1A; complete loss of
activity; dbSNP:rs28934607).
{ECO:0000269|PubMed:9486994}.
/FTId=VAR_016958.
VARIANT 389 389 R -> C (in VDDR1A; complete loss of
activity; dbSNP:rs118204010).
{ECO:0000269|PubMed:10566658}.
/FTId=VAR_016968.
VARIANT 389 389 R -> G (in VDDR1A; complete loss of
activity; dbSNP:rs118204010).
{ECO:0000269|PubMed:12050193}.
/FTId=VAR_016960.
VARIANT 389 389 R -> H (in VDDR1A; complete loss of
activity; dbSNP:rs118204009).
{ECO:0000269|PubMed:12050193,
ECO:0000269|PubMed:9837822}.
/FTId=VAR_016959.
VARIANT 409 409 T -> I (in VDDR1A; dbSNP:rs118204008).
{ECO:0000269|PubMed:12050193,
ECO:0000269|PubMed:9837822}.
/FTId=VAR_016961.
VARIANT 429 429 R -> P (in VDDR1A; dbSNP:rs568165874).
{ECO:0000269|PubMed:9837822}.
/FTId=VAR_016971.
VARIANT 453 453 R -> C (in VDDR1A; dbSNP:rs767480544).
{ECO:0000269|PubMed:9837822}.
/FTId=VAR_016972.
VARIANT 478 478 V -> G (in VDDR1A).
{ECO:0000269|PubMed:10320521}.
/FTId=VAR_016973.
VARIANT 497 497 P -> R (in VDDR1A; dbSNP:rs1161799032).
{ECO:0000269|PubMed:9837822}.
/FTId=VAR_016974.
CONFLICT 320 320 D -> N (in Ref. 7; BAG37458).
{ECO:0000305}.
SEQUENCE 508 AA; 56504 MW; 7F0611EFAD1B5C1C CRC64;
MTQTLKYASR VFHRVRWAPE LGASLGYREY HSARRSLADI PGPSTPSFLA ELFCKGGLSR
LHELQVQGAA HFGPVWLASF GTVRTVYVAA PALVEELLRQ EGPRPERCSF SPWTEHRRCR
QRACGLLTAE GEEWQRLRSL LAPLLLRPQA AARYAGTLNN VVCDLVRRLR RQRGRGTGPP
ALVRDVAGEF YKFGLEGIAA VLLGSRLGCL EAQVPPDTET FIRAVGSVFV STLLTMAMPH
WLRHLVPGPW GRLCRDWDQM FAFAQRHVER REAEAAMRNG GQPEKDLESG AHLTHFLFRE
ELPAQSILGN VTELLLAGVD TVSNTLSWAL YELSRHPEVQ TALHSEITAA LSPGSSAYPS
ATVLSQLPLL KAVVKEVLRL YPVVPGNSRV PDKDIHVGDY IIPKNTLVTL CHYATSRDPA
QFPEPNSFRP ARWLGEGPTP HPFASLPFGF GKRSCMGRRL AELELQMALA QILTHFEVQP
EPGAAPVRPK TRTVLVPERS INLQFLDR


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