P29788 (VTNC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vitronectin
Short name=VN

Alternative name(s):
S-protein
Serum-spreading factor

Gene names

Name:

Vtn

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	478 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	Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
Subunit structure	Interacts with SERPINE1/PAI1, insulin and C1QBP By similarity.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Plasma.
Domain	The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin By similarity.
Post-translational modification	Sulfated on 2 tyrosine residues By similarity. N- and O-glycosylated By similarity. It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
Sequence similarities	Contains 4 hemopexin-like domains. Contains 1 SMB (somatomedin-B) domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-matrix adhesion Inferred from direct assay PubMed 15728191. Source: MGI extracellular matrix organization Inferred from direct assay PubMed 18757743. Source: MGI immune response Inferred from electronic annotation. Source: InterPro positive regulation of cell-substrate adhesion Inferred from direct assay PubMed 18757743. Source: MGI
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from direct assay PubMed 15728191. Source: MGI
Molecular_function	extracellular matrix binding Inferred from direct assay PubMed 18757743. Source: MGI heparin binding Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide binding Inferred from electronic annotation. Source: InterPro scavenger receptor 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 – 19	19	Ref.9
	Chain	20 – 478	459	Vitronectin		PRO_0000036398
Regions
	Domain	20 – 63	44	SMB
	Domain	160 – 203	44	Hemopexin-like 1
	Domain	205 – 251	47	Hemopexin-like 2
	Domain	253 – 303	51	Hemopexin-like 3
	Domain	426 – 473	48	Hemopexin-like 4
	Region	366 – 399	34	Heparin-binding By similarity
	Motif	64 – 66	3	Cell attachment site
Amino acid modifications
	Modified residue	69	1	Phosphothreonine By similarity
	Modified residue	75	1	Sulfotyrosine Potential
	Modified residue	78	1	Sulfotyrosine Potential
	Modified residue	80	1	Sulfotyrosine Potential
	Modified residue	278	1	Sulfotyrosine Potential
	Modified residue	281	1	Sulfotyrosine Potential
	Modified residue	311	1	Phosphoserine By similarity
	Modified residue	398	1	Phosphoserine; by PKA By similarity
	Modified residue	416	1	Sulfotyrosine Potential
	Modified residue	419	1	Sulfotyrosine Potential
	Modified residue	421	1	Sulfotyrosine Potential
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	168	1	N-linked (GlcNAc...) Potential
	Glycosylation	241	1	N-linked (GlcNAc...) Ref.10
	Disulfide bond	24 ↔ 40		Alternate By similarity
	Disulfide bond	24 ↔ 28		Alternate By similarity
	Disulfide bond	28 ↔ 58		Alternate By similarity
	Disulfide bond	38 ↔ 51		Alternate By similarity
	Disulfide bond	38 ↔ 40		Alternate By similarity
	Disulfide bond	44 ↔ 50		By similarity
	Disulfide bond	51 ↔ 58		Alternate By similarity
	Disulfide bond	292 ↔ 431		By similarity
Experimental info
	Sequence conflict	179 – 180	2	CY → RC in AAL34534. Ref.4
	Sequence conflict	186	1	A → T in AAH12690. Ref.8
	Sequence conflict	281	1	Y → H in AAL34534. Ref.4
	Sequence conflict	348	1	A → T in BAB27809. Ref.5
	Sequence conflict	369	1	K → P in AAL34534. Ref.4
	Sequence conflict	383 – 384	2	Missing in AAA40558. Ref.2
	Sequence conflict	416	1	Y → K in AAA40558. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29788 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: EB0C772F8BD6A166	FASTA	478	54,849
	10 20 30 40 50 60 MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC CADYMEQCKP 70 80 90 100 110 120 QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP GDLNPRTDGT LKPTAFLDPE 130 140 150 160 170 180 EQPSTPAPKV EQQEEILRPD TTDQGTPEFP EEELCSGKPF DAFTDLKNGS LFAFRGQYCY 190 200 210 220 230 240 ELDETAVRPG YPKLIQDVWG IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR 250 260 270 280 290 300 NISEGFSGIP DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV 310 320 330 340 350 360 FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA GRIYVTGSLS 370 380 390 400 410 420 HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS IWFSLFSSEE SGLGTYNNYD 430 440 450 460 470 YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL RTRRVDSVNP PYPRSIAQYW LGCPTSEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of the gene encoding mouse vitronectin." Seiffert D., Poenninger J., Binder B.R. Gene 134:303-304(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Liver.
[2]	"Detection of vitronectin mRNA in tissues and cells of the mouse." Seiffert D., Keeton M., Eguchi Y., Sawdey M., Loskutoff D.J. Proc. Natl. Acad. Sci. U.S.A. 88:9402-9406(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Primary structure of vitronectins and homology with other proteins." Ehrlich H.J., Richter B., von der Ahe D., Preissner K.T. (In) Preissner K.T., Rosenblatt S., Kost C., Wegerhoff J., Mosher D.F. (eds.); Biology of vitronectins, pp.1-1, Elsevier, Amsterdam (1996) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[4]	"Construction of a robust CHO cell-line for biopharmaceutical production." Lai D.-Z. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[5]	"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: Embryo and Gall bladder.
[6]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[7]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: Salivary gland.
[9]	"Vitronectin diversity in evolution but uniformity in ligand binding and size of the core polypeptide." Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H., Matsumoto I., Seno N., Hayashi M. Biochim. Biophys. Acta 1120:1-10(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-44.
[10]	"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-241, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X72091 Genomic DNA. Translation: CAA50981.1. M77123 mRNA. Translation: AAA40558.1. X63003 mRNA. Translation: CAA44732.1. AF440693 mRNA. Translation: AAL34534.1. AK011736 mRNA. Translation: BAB27809.1. AK090325 mRNA. Translation: BAC41171.1. AL591177 Genomic DNA. Translation: CAI25547.1. CH466556 Genomic DNA. Translation: EDL15582.1. BC012690 mRNA. Translation: AAH12690.1.
IPI	IPI00129240.
PIR	SGMSV. S19894.
RefSeq	NP_035837.1. NM_011707.2.
UniGene	Mm.3667.
3D structure databases
ProteinModelPortal	P29788.
SMR	P29788. Positions 20-70, 154-281.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000017488.
PTM databases
PhosphoSite	P29788.
Proteomic databases
PaxDb	P29788.
PRIDE	P29788.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017488; ENSMUSP00000017488; ENSMUSG00000017344.
GeneID	22370.
KEGG	mmu:22370.
UCSC	uc007kjk.2. mouse.
Organism-specific databases
CTD	7448.
MGI	MGI:98940. Vtn.
Phylogenomic databases
eggNOG	NOG245064.
GeneTree	ENSGT00530000063751.
HOGENOM	HOG000133161.
HOVERGEN	HBG002902.
InParanoid	Q91X32.
KO	K06251.
OMA	ECEGSSL.
OrthoDB	EOG4JT065.
Gene expression databases
Bgee	P29788.
CleanEx	MM_VTN.
Genevestigator	P29788.
GermOnline	ENSMUSG00000017344. Mus musculus.
Family and domain databases
Gene3D	2.110.10.10. 3 hits.
InterPro	IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR018486. Hemopexin_CS. IPR020436. Somatomedin_B_chordata. IPR001212. Somatomedin_B_dom. [Graphical view]
Pfam	PF00045. Hemopexin. 4 hits. PF01033. Somatomedin_B. 1 hit. [Graphical view]
PRINTS	PR00022. SOMATOMEDINB.
SMART	SM00120. HX. 4 hits. SM00201. SO. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit.
PROSITE	PS00024. HEMOPEXIN. 2 hits. PS00524. SMB_1. 1 hit. PS50958. SMB_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	VTN. mouse.
NextBio	302703.
SOURCE	Search...

Entry information

Entry name

VTNC_MOUSE

Accession

Primary (citable) accession number: P29788
Secondary accession number(s): Q5SYG4 , Q8VII4, Q91X32, Q9D080

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program