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P21614 (VTDB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length476 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.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.4
Chain17 – 476460Vitamin D-binding protein
PRO_0000001103

Regions

Domain17 – 208192Albumin 1
Domain209 – 394186Albumin 2
Domain395 – 47682Albumin 3

Amino acid modifications

Glycosylation2881N-linked (GlcNAc...) Ref.5
Disulfide bond29 ↔ 75 By similarity
Disulfide bond74 ↔ 83 By similarity
Disulfide bond96 ↔ 112 By similarity
Disulfide bond111 ↔ 122 By similarity
Disulfide bond145 ↔ 190 By similarity
Disulfide bond189 ↔ 198 By similarity
Disulfide bond220 ↔ 266 By similarity
Disulfide bond265 ↔ 273 By similarity
Disulfide bond286 ↔ 300 By similarity
Disulfide bond299 ↔ 311 By similarity
Disulfide bond335 ↔ 376 By similarity
Disulfide bond375 ↔ 384 By similarity
Disulfide bond407 ↔ 453 By similarity
Disulfide bond452 ↔ 462 By similarity

Experimental info

Sequence conflict2471N → K in BAB27297. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21614 [UniParc].

Last modified October 10, 2003. Version 2.
Checksum: 633B0CE183CD43FD

FASTA47653,600
        10         20         30         40         50         60 
MKRVLVLLLA LAFGHALERG RDYEKDKVCN ELAMLGKEDF RSLSLILYSR KFSSSTFEQV 

        70         80         90        100        110        120 
NQLVKEVVSL TEECCAEGAD PTCYDTRTSE LSVKSCESDA PFPVHPGTPE CCTKEGLERK 

       130        140        150        160        170        180 
LCMAALSHQP QEFPTYVEPT NDEICEAFRR DPKGFADQFL YEYSSNYGQA PLPLLVAYTK 

       190        200        210        220        230        240 
NYLSMVGSCC TSANPTVCFV KERLQMKHLS LLTTMSNRVC SQYAAYGKEK SRLSHLIKLA 

       250        260        270        280        290        300 
QKVPTANLEN VLPLAEDFTE ILSRCCESTS EDCMASELPE HTIKICQNLS KKNSKFEECC 

       310        320        330        340        350        360 
QENTPMNIFM CTYFMPAAEP LQLPAIKLPT GKDLCGQSTT QAMDQYTFEL SRRTQVPEVF 

       370        380        390        400        410        420 
LSKVLEPTLK TLRECCDTQD SVACFSTQSP LLKRQLTSFI EKGQEMCADY SENTFTEYKK 

       430        440        450        460        470 
KLAERLRTKT PNTSPAELKD MVEKHSDFAS KCCSINSPPL YCSSQIDAEM IDTLQS 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic liver.
[2]"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].
Strain: FVB/N.
Tissue: Kidney and Liver.
[3]"Mapping and conservation of the group-specific component gene in mouse."
Yang F., Bergeron J.M., Linehan L.A., Lalley P.A., Sakaguchi A.Y., Bowman B.H.
Genomics 7:509-516(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-476.
[4]"The isolation, characterization and amino terminal sequence of the vitamin D-binding protein (group specific component) from mouse plasma."
Borke J.L., Litwiller R.D., Bell M.P., Fass D.N., McKean D.J., Kumar R.
Int. J. Biochem. 20:1343-1349(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-38.
[5]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-288.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010965 mRNA. Translation: BAB27297.1.
BC010762 mRNA. Translation: AAH10762.1.
BC051395 mRNA. Translation: AAH51395.2.
M55413 mRNA. Translation: AAA37669.1.
PIRA35327.
RefSeqNP_032122.1. NM_008096.2.
UniGeneMm.196595.

3D structure databases

ProteinModelPortalP21614.
SMRP21614. Positions 20-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21614. 5 interactions.
MINTMINT-1857787.

PTM databases

PhosphoSiteP21614.

2D gel databases

REPRODUCTION-2DPAGEP21614.

Proteomic databases

PaxDbP21614.
PRIDEP21614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049209; ENSMUSP00000046636; ENSMUSG00000035540.
GeneID14473.
KEGGmmu:14473.
UCSCuc008yam.2. mouse.

Organism-specific databases

CTD2638.
MGIMGI:95669. Gc.

Phylogenomic databases

eggNOGNOG40465.
GeneTreeENSGT00390000000113.
HOGENOMHOG000140946.
HOVERGENHBG009729.
InParanoidP21614.
KOK12258.
OMARKLCMAA.
OrthoDBEOG7B05CR.
PhylomeDBP21614.
TreeFamTF335561.

Gene expression databases

BgeeP21614.
CleanExMM_GC.
GenevestigatorP21614.

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

ChiTaRSGC. mouse.
NextBio286142.
PROP21614.
SOURCESearch...

Entry information

Entry nameVTDB_MOUSE
AccessionPrimary (citable) accession number: P21614
Secondary accession number(s): Q7TS97, Q91XG1, Q9CY31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 10, 2003
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot