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P02774 (VTDB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitamin D-binding protein

Short name=DBP
Short name=VDB
Alternative name(s):
Gc-globulin
Group-specific component
Gene names
Name:GC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. In plasma, it carries the vitamin D sterols and prevents polymerization of actin by binding its monomers. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes.

Subcellular location

Secreted.

Polymorphism

Over 80 variants of human DBP have been identified. The three most common alleles are called GC*1F, GC*1S, and GC*2. The sequence shown is that of the GC*2 allele.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Sequence caution

The sequence BAG60654.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02774-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P02774-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: P02774-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLWSWSEERGGAARLSGRKM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.11 Ref.12
Chain17 – 474458Vitamin D-binding protein
PRO_0000001102

Regions

Domain17 – 208192Albumin 1
Domain209 – 394186Albumin 2
Domain395 – 47480Albumin 3

Amino acid modifications

Glycosylation2881N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 75
Disulfide bond74 ↔ 83 By similarity
Disulfide bond96 ↔ 112
Disulfide bond111 ↔ 122
Disulfide bond145 ↔ 190
Disulfide bond189 ↔ 198
Disulfide bond220 ↔ 266
Disulfide bond265 ↔ 273
Disulfide bond286 ↔ 300
Disulfide bond299 ↔ 311
Disulfide bond335 ↔ 376
Disulfide bond375 ↔ 384
Disulfide bond407 ↔ 453
Disulfide bond452 ↔ 462

Natural variations

Alternative sequence1 – 122122Missing in isoform 2.
VSP_038427
Alternative sequence11M → MLWSWSEERGGAARLSGRKM in isoform 3.
VSP_044523
Natural variant4321D → E in allele GC*1S. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs7041 [ dbSNP | Ensembl ].
VAR_000548
Natural variant4361K → T in allele GC*1F, allele GC*1A1 and allele GC*1S. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.13
Corresponds to variant rs4588 [ dbSNP | Ensembl ].
VAR_000549
Natural variant4451R → C in allele GC*2A9. Ref.13
VAR_014120
Natural variant4451R → H in allele GC*1A1. Ref.5 Ref.7 Ref.13
Corresponds to variant rs9016 [ dbSNP | Ensembl ].
VAR_014121

Experimental info

Sequence conflict1681G → E in AAA52173. Ref.1
Sequence conflict1831L → P in AK309595. Ref.5
Sequence conflict3271E → R in AAA52173. Ref.1

Secondary structure

....................................................... 474
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 6AD8F163B551F1E4

FASTA47452,964
        10         20         30         40         50         60 
MKRVLVLLLA VAFGHALERG RDYEKNKVCK EFSHLGKEDF TSLSLVLYSR KFPSGTFEQV 

        70         80         90        100        110        120 
SQLVKEVVSL TEACCAEGAD PDCYDTRTSA LSAKSCESNS PFPVHPGTAE CCTKEGLERK 

       130        140        150        160        170        180 
LCMAALKHQP QEFPTYVEPT NDEICEAFRK DPKEYANQFM WEYSTNYGQA PLSLLVSYTK 

       190        200        210        220        230        240 
SYLSMVGSCC TSASPTVCFL KERLQLKHLS LLTTLSNRVC SQYAAYGEKK SRLSNLIKLA 

       250        260        270        280        290        300 
QKVPTADLED VLPLAEDITN ILSKCCESAS EDCMAKELPE HTVKLCDNLS TKNSKFEDCC 

       310        320        330        340        350        360 
QEKTAMDVFV CTYFMPAAQL PELPDVELPT NKDVCDPGNT KVMDKYTFEL SRRTHLPEVF 

       370        380        390        400        410        420 
LSKVLEPTLK SLGECCDVED STTCFNAKGP LLKKELSSFI DKGQELCADY SENTFTEYKK 

       430        440        450        460        470 
KLAERLKAKL PDATPKELAK LVNKRSDFAS NCCSINSPPL YCDSEIDAEL KNIL 

« Hide

Isoform 2 [UniParc].

Checksum: 13170DD8F989B341
Show »

FASTA35239,542
Isoform 3 [UniParc].

Checksum: C4738F41F3B76713
Show »

FASTA49355,123

References

« Hide 'large scale' references
[1]"Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family."
Cooke N.E., David E.V.
J. Clin. Invest. 76:2420-2424(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-432 AND THR-436.
[2]"Human group-specific component (Gc) is a member of the albumin family."
Yang F., Brune J.L., Naylor S.L., Cupples R.L., Naberhaus K.H., Bowman B.H.
Proc. Natl. Acad. Sci. U.S.A. 82:7994-7998(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Sequence and organization of the human vitamin D-binding protein gene."
Braun A., Kofler A., Morawietz S., Cleve H.
Biochim. Biophys. Acta 1216:385-394(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
[4]"Complete structure of the human Gc gene: differences and similarities between members of the albumin gene family."
Witke W.F., Gibbs P.E., Zielinski R., Yang F., Bowman B.H., Dugaiczyk A.
Genomics 16:751-754(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-47 (ISOFORM 2), VARIANTS GLU-432; THR-436 AND HIS-445.
Tissue: Liver.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-432 AND THR-436.
Tissue: Kidney.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS THR-436 AND HIS-445.
[8]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-436.
Tissue: Liver.
[10]"The vitamin D-binding protein gene contains conserved nucleotide sequences that respond to heavy metal, adipocyte and mitotic signals."
Yang F., Naberhaus K.H., Adrian G.S., Gardella J.M., Brissenden J.E., Bowman B.H.
Gene 54:285-290(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[11]"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein."
Schoentgen F., Metz-Boutigue M.-H., Jolles J., Constans J., Jolles P.
Biochim. Biophys. Acta 871:189-198(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-474.
[12]"Molecular basis for the three major forms of human serum vitamin D binding protein (group-specific component)."
Svasti J., Kurosky A., Bennett A., Bowman B.H.
Biochemistry 18:1611-1617(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-31 AND 431-441.
[13]"Characterization of mutants of the vitamin-D-binding protein/group specific component: GC aborigine (1A1) from Australian aborigines and South African blacks, and 2A9 from south Germany."
Kofler A., Braun A., Jenkins T., Serjeantson S.W., Cleve H.
Vox Sang. 68:50-54(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-446, VARIANTS GC*1A1 THR-436 AND HIS-445, VARIANT GC*2A9 CYS-445.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Molecular analysis of the gene for the human vitamin-D-binding protein (group-specific component): allelic differences of the common genetic GC types."
Braun A., Bichlmaier R., Cleve H.
Hum. Genet. 89:401-406(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GC*2; GC*1F AND GC*1S.
[16]"A structural basis for the unique binding features of the human vitamin D-binding protein."
Verboven C., Rabijns A., De Maeyer M., Van Baelen H., Bouillon R., De Ranter C.
Nat. Struct. Biol. 9:131-136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 29-473.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12654 mRNA. Translation: AAA52173.1.
X03178 mRNA. Translation: CAA26938.1.
S67480 expand/collapse EMBL AC list , S67474, S67476, S67478, S67479, S67526 Genomic DNA. Translation: AAB29423.1.
L10641 Genomic DNA. Translation: AAA61704.1.
AK290827 mRNA. Translation: BAF83516.1.
AK298433 mRNA. Translation: BAG60654.1. Sequence problems.
AK309595 mRNA. No translation available.
AK315853 mRNA. Translation: BAF98744.1.
AK223458 mRNA. Translation: BAD97178.1.
AC024722 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05645.1.
BC057228 mRNA. Translation: AAH57228.1.
M17156 Genomic DNA. Translation: AAA19662.2.
S77129 Genomic DNA. Translation: AAD14249.1. Sequence problems.
S77130 Genomic DNA. Translation: AAD14250.1. Sequence problems.
PIRVYHUD. A94076.
RefSeqNP_000574.2. NM_000583.3.
NP_001191235.1. NM_001204306.1.
NP_001191236.1. NM_001204307.1.
UniGeneHs.418497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J78X-ray2.31A/B17-474[»]
1J7EX-ray2.55A/B17-474[»]
1KW2X-ray2.15A/B17-474[»]
1KXPX-ray2.10D17-474[»]
1LOTX-ray2.50A17-474[»]
1MA9X-ray2.40A17-474[»]
ProteinModelPortalP02774.
SMRP02774. Positions 20-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108908. 10 interactions.
DIPDIP-17038N.
IntActP02774. 7 interactions.
MINTMINT-239255.
STRING9606.ENSP00000273951.

Chemistry

BindingDBP02774.
ChEMBLCHEMBL2259.
DrugBankDB00169. Cholecalciferol.

PTM databases

PhosphoSiteP02774.
UniCarbKBP02774.

Polymorphism databases

DMDM139641.

2D gel databases

DOSAC-COBS-2DPAGEP02774.
REPRODUCTION-2DPAGEIPI00555812.
P02774.
SWISS-2DPAGEP02774.

Proteomic databases

PaxDbP02774.
PeptideAtlasP02774.
PRIDEP02774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273951; ENSP00000273951; ENSG00000145321.
ENST00000504199; ENSP00000421725; ENSG00000145321.
GeneID2638.
KEGGhsa:2638.

Organism-specific databases

CTD2638.
GeneCardsGC04M072596.
HGNCHGNC:4187. GC.
HPACAB008596.
HPA001526.
HPA019855.
MIM139200. gene+phenotype.
neXtProtNX_P02774.
PharmGKBPA28601.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40465.
HOGENOMHOG000140946.
HOVERGENHBG009729.
InParanoidP02774.
KOK12258.
OrthoDBEOG7B05CR.
PhylomeDBP02774.
TreeFamTF335561.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.

Gene expression databases

ArrayExpressP02774.
BgeeP02774.
CleanExHS_GC.
GenevestigatorP02774.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
IPR000213. VitD-bd.
IPR015247. VitD-bind_III.
[Graphical view]
PfamPF00273. Serum_albumin. 2 hits.
PF09164. VitD-bind_III. 1 hit.
[Graphical view]
PRINTSPR00802. SERUMALBUMIN.
PR00804. VITAMNDBNDNG.
SMARTSM00103. ALBUMIN. 2 hits.
[Graphical view]
SUPFAMSSF48552. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 1 hit.
PS51438. ALBUMIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02774.
GeneWikiVitamin_D-binding_protein.
GenomeRNAi2638.
NextBio10400.
PROP02774.
SOURCESearch...

Entry information

Entry nameVTDB_HUMAN
AccessionPrimary (citable) accession number: P02774
Secondary accession number(s): B4DPP2 expand/collapse secondary AC list , D6RAK8, Q16309, Q16310, Q53F31, Q6GTG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM