VTDB_MOUSE
ID VTDB_MOUSE Reviewed; 476 AA.
AC P21614; Q7TS97; Q91XG1; Q9CY31;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Vitamin D-binding protein;
DE Short=DBP;
DE Short=VDB;
DE AltName: Full=Gc-globulin;
DE AltName: Full=Group-specific component;
DE Flags: Precursor;
GN Name=Gc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-476.
RX PubMed=1696927; DOI=10.1016/0888-7543(90)90193-x;
RA Yang F., Bergeron J.M., Linehan L.A., Lalley P.A., Sakaguchi A.Y.,
RA Bowman B.H.;
RT "Mapping and conservation of the group-specific component gene in mouse.";
RL Genomics 7:509-516(1990).
RN [4]
RP PROTEIN SEQUENCE OF 17-24, INTERACTION WITH LRP2, AND SUBCELLULAR LOCATION.
RX PubMed=10052453; DOI=10.1016/s0092-8674(00)80655-8;
RA Nykjaer A., Dragun D., Walther D., Vorum H., Jacobsen C., Herz J.,
RA Melsen F., Christensen E.I., Willnow T.E.;
RT "An endocytic pathway essential for renal uptake and activation of the
RT steroid 25-(OH) vitamin D3.";
RL Cell 96:507-515(1999).
RN [5]
RP PROTEIN SEQUENCE OF 17-38.
RX PubMed=3243374; DOI=10.1016/s0020-711x(98)90002-7;
RA Borke J.L., Litwiller R.D., Bell M.P., Fass D.N., McKean D.J., Kumar R.;
RT "The isolation, characterization and amino terminal sequence of the vitamin
RT D-binding protein (group specific component) from mouse plasma.";
RL Int. J. Biochem. 20:1343-1349(1988).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-288.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in vitamin D transport and storage, scavenging of
CC extracellular G-actin, enhancement of the chemotactic activity of C5
CC alpha for neutrophils in inflammation and macrophage activation.
CC {ECO:0000250|UniProtKB:P02774}.
CC -!- SUBUNIT: Associates with membrane-bound immunoglobulin on the surface
CC of B-lymphocytes and with IgG Fc receptor on the membranes of T-
CC lymphocytes (By similarity). Interacts with LRP2; the interaction is
CC required for renal uptake of GC in complex with 25-hydroxyvitamin D3
CC (PubMed:10052453). {ECO:0000250|UniProtKB:P02774,
CC ECO:0000269|PubMed:10052453}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10052453}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; AK010965; BAB27297.1; -; mRNA.
DR EMBL; BC010762; AAH10762.1; -; mRNA.
DR EMBL; BC051395; AAH51395.2; -; mRNA.
DR EMBL; M55413; AAA37669.1; -; mRNA.
DR CCDS; CCDS19407.1; -.
DR PIR; A35327; A35327.
DR RefSeq; NP_032122.1; NM_008096.2.
DR AlphaFoldDB; P21614; -.
DR SMR; P21614; -.
DR BioGRID; 199850; 3.
DR IntAct; P21614; 1.
DR STRING; 10090.ENSMUSP00000046636; -.
DR GlyGen; P21614; 1 site.
DR iPTMnet; P21614; -.
DR PhosphoSitePlus; P21614; -.
DR SwissPalm; P21614; -.
DR REPRODUCTION-2DPAGE; P21614; -.
DR CPTAC; non-CPTAC-3321; -.
DR jPOST; P21614; -.
DR MaxQB; P21614; -.
DR PaxDb; P21614; -.
DR PeptideAtlas; P21614; -.
DR PRIDE; P21614; -.
DR ProteomicsDB; 297592; -.
DR Antibodypedia; 871; 797 antibodies from 40 providers.
DR DNASU; 14473; -.
DR Ensembl; ENSMUST00000049209; ENSMUSP00000046636; ENSMUSG00000035540.
DR GeneID; 14473; -.
DR KEGG; mmu:14473; -.
DR UCSC; uc008yam.2; mouse.
DR CTD; 2638; -.
DR MGI; MGI:95669; Gc.
DR VEuPathDB; HostDB:ENSMUSG00000035540; -.
DR eggNOG; ENOG502QTPW; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR HOGENOM; CLU_045992_0_0_1; -.
DR InParanoid; P21614; -.
DR OMA; MVSTCCI; -.
DR OrthoDB; 514529at2759; -.
DR PhylomeDB; P21614; -.
DR TreeFam; TF335561; -.
DR Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
DR BioGRID-ORCS; 14473; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gc; mouse.
DR PRO; PR:P21614; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P21614; protein.
DR Bgee; ENSMUSG00000035540; Expressed in left lobe of liver and 66 other tissues.
DR ExpressionAtlas; P21614; baseline and differential.
DR Genevisible; P21614; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:1902118; F:calcidiol binding; ISO:MGI.
DR GO; GO:0005499; F:vitamin D binding; ISO:MGI.
DR GO; GO:0090482; F:vitamin transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042359; P:vitamin D metabolic process; IDA:MGI.
DR CDD; cd00015; ALBUMIN; 1.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR InterPro; IPR000213; VitD-bd.
DR InterPro; IPR015247; VitD-bind_III.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR PANTHER; PTHR11385:SF11; PTHR11385:SF11; 1.
DR Pfam; PF00273; Serum_albumin; 2.
DR Pfam; PF09164; VitD-bind_III; 1.
DR PRINTS; PR00802; SERUMALBUMIN.
DR PRINTS; PR00804; VITAMNDBNDNG.
DR SMART; SM00103; ALBUMIN; 2.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 1.
DR PROSITE; PS51438; ALBUMIN_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Transport;
KW Vitamin D.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:10052453,
FT ECO:0000269|PubMed:3243374"
FT CHAIN 17..476
FT /note="Vitamin D-binding protein"
FT /id="PRO_0000001103"
FT DOMAIN 17..208
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 209..394
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 395..476
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04276"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 29..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 74..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 96..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 111..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 145..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 189..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 220..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 265..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 286..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 299..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 335..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 407..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 452..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 247
FT /note="N -> K (in Ref. 1; BAB27297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53600 MW; 633B0CE183CD43FD CRC64;
MKRVLVLLLA LAFGHALERG RDYEKDKVCN ELAMLGKEDF RSLSLILYSR KFSSSTFEQV
NQLVKEVVSL TEECCAEGAD PTCYDTRTSE LSVKSCESDA PFPVHPGTPE CCTKEGLERK
LCMAALSHQP QEFPTYVEPT NDEICEAFRR DPKGFADQFL YEYSSNYGQA PLPLLVAYTK
NYLSMVGSCC TSANPTVCFV KERLQMKHLS LLTTMSNRVC SQYAAYGKEK SRLSHLIKLA
QKVPTANLEN VLPLAEDFTE ILSRCCESTS EDCMASELPE HTIKICQNLS KKNSKFEECC
QENTPMNIFM CTYFMPAAEP LQLPAIKLPT GKDLCGQSTT QAMDQYTFEL SRRTQVPEVF
LSKVLEPTLK TLRECCDTQD SVACFSTQSP LLKRQLTSFI EKGQEMCADY SENTFTEYKK
KLAERLRTKT PNTSPAELKD MVEKHSDFAS KCCSINSPPL YCSSQIDAEM IDTLQS
