P21614 (VTDB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vitamin D-binding protein
Short name=DBP
Short name=VDB

Alternative name(s):
Gc-globulin
Group-specific component

Gene names

Name:

Gc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Actin-binding Vitamin D
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	vitamin D metabolic process Inferred from direct assay PubMed 15225763. Source: MGI
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB vitamin D binding Inferred from electronic annotation. Source: UniProtKB-KW vitamin transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Ref.4
	Chain	17 – 476	460	Vitamin D-binding protein		PRO_0000001103
Regions
	Domain	17 – 208	192	Albumin 1
	Domain	209 – 394	186	Albumin 2
	Domain	395 – 476	82	Albumin 3
Amino acid modifications
	Glycosylation	288	1	N-linked (GlcNAc...) Ref.5
	Disulfide bond	29 ↔ 75		By similarity
	Disulfide bond	74 ↔ 83		By similarity
	Disulfide bond	96 ↔ 112		By similarity
	Disulfide bond	111 ↔ 122		By similarity
	Disulfide bond	145 ↔ 190		By similarity
	Disulfide bond	189 ↔ 198		By similarity
	Disulfide bond	220 ↔ 266		By similarity
	Disulfide bond	265 ↔ 273		By similarity
	Disulfide bond	286 ↔ 300		By similarity
	Disulfide bond	299 ↔ 311		By similarity
	Disulfide bond	335 ↔ 376		By similarity
	Disulfide bond	375 ↔ 384		By similarity
	Disulfide bond	407 ↔ 453		By similarity
	Disulfide bond	452 ↔ 462		By similarity
Experimental info
	Sequence conflict	247	1	N → K in BAB27297. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21614 [UniParc]. Last modified October 10, 2003. Version 2. Checksum: 633B0CE183CD43FD	FASTA	476	53,600
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00126184.
PIR	A35327.
RefSeq	NP_032122.1. NM_008096.2.
UniGene	Mm.196595.
3D structure databases
ProteinModelPortal	P21614.
SMR	P21614. Positions 20-474.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21614. 1 interaction.
PTM databases
PhosphoSite	P21614.
2D gel databases
REPRODUCTION-2DPAGE	P21614.
Proteomic databases
PaxDb	P21614.
PRIDE	P21614.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049209; ENSMUSP00000046636; ENSMUSG00000035540.
GeneID	14473.
KEGG	mmu:14473.
UCSC	uc008yam.1. mouse.
Organism-specific databases
CTD	2638.
MGI	MGI:95669. Gc.
Phylogenomic databases
eggNOG	NOG40465.
GeneTree	ENSGT00390000000113.
HOGENOM	HOG000140946.
HOVERGEN	HBG009729.
InParanoid	P21614.
KO	K12258.
OMA	RKLCMAA.
OrthoDB	EOG4MKNG5.
Gene expression databases
Bgee	P21614.
CleanEx	MM_GC.
Genevestigator	P21614.
GermOnline	ENSMUSG00000035540. Mus musculus.
Family and domain databases
InterPro	IPR000264. ALB/AFP/VDB. IPR020858. Serum_albumin-like. IPR020857. Serum_albumin_CS. IPR014760. Serum_albumin_N. IPR000213. VitD-bd. IPR015247. VitD-bind_III. [Graphical view]
Pfam	PF00273. Serum_albumin. 2 hits. PF09164. VitD-bind_III. 1 hit. [Graphical view]
PRINTS	PR00802. SERUMALBUMIN. PR00804. VITAMNDBNDNG.
SMART	SM00103. ALBUMIN. 2 hits. [Graphical view]
SUPFAM	SSF48552. Serum_albumin. 3 hits.
PROSITE	PS00212. ALBUMIN_1. 1 hit. PS51438. ALBUMIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GC. mouse.
NextBio	286142.
SOURCE	Search...

Entry information

Entry name

VTDB_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program