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Q9CZT5 (VASN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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:
Vasorin
Alternative name(s):
Protein slit-like 2
Gene names
Name:Vasn
Synonyms:Slitl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May act as an inhibitor of TGF-beta signaling By similarity.

Subunit structure

Interacts with TGFB1, TGFB2 and TGFB3 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Developmental stage

Expression begins at E10.5 and increases as development progresses to E17.5. Expression rises in parallel with the differentiation of vascular smooth muscle cells (VSMCs) of the aorta. Ref.4

Induction

Upon retinoic acid-induced differentiation of smooth muscle cells in vitro. Ref.4

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Contains 1 EGF-like domain.

Contains 1 fibronectin type-III domain.

Contains 10 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 673649Vasorin
PRO_0000232631

Regions

Topological domain25 – 576552Extracellular Potential
Transmembrane577 – 59721Helical; Potential
Topological domain598 – 67376Cytoplasmic Potential
Domain25 – 5329LRRNT
Repeat54 – 7522LRR 1
Repeat78 – 9922LRR 2
Repeat102 – 12322LRR 3
Repeat126 – 14722LRR 4
Repeat150 – 17021LRR 5
Repeat171 – 19222LRR 6
Repeat194 – 21522LRR 7
Repeat218 – 23922LRR 8
Repeat241 – 26525LRR 9
Repeat266 – 28823LRR 10
Domain299 – 35254LRRCT
Domain406 – 44338EGF-like
Domain463 – 55997Fibronectin type-III

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5291N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Disulfide bond410 ↔ 421 By similarity
Disulfide bond415 ↔ 431 By similarity
Disulfide bond433 ↔ 442 By similarity

Experimental info

Sequence conflict2251S → Y in BAB28075. Ref.2
Sequence conflict3831L → H in BAC38992. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CZT5 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: AAB8DA82DA8E9D32

FASTA67372,261
        10         20         30         40         50         60 
MHSRSCLPPL LLLLLVLLGS GVQGCPSGCQ CNQPQTVFCT ARQGTTVPRD VPPDTVGLYI 

        70         80         90        100        110        120 
FENGITTLDV GCFAGLPGLQ LLDLSQNQIT SLPGGIFQPL VNLSNLDLTA NKLHEISNET 

       130        140        150        160        170        180 
FRGLRRLERL YLGKNRIRHI QPGAFDALDR LLELKLPDNE LRVLPPLHLP RLLLLDLSHN 

       190        200        210        220        230        240 
SIPALEAGIL DTANVEALRL AGLGLRQLDE GLFGRLLNLH DLDVSDNQLE HMPSVIQGLR 

       250        260        270        280        290        300 
GLTRLRLAGN TRIAQIRPED LAGLTALQEL DVSNLSLQAL PSDLSSLFPR LRLLAAARNP 

       310        320        330        340        350        360 
FNCLCPLSWF GPWVRENHVV LASPEETRCH FPPKNAGRLL LDLDYADFGC PVTTTTATVP 

       370        380        390        400        410        420 
TIRSTIREPT LSTSSQAPTW PSLTEPTTQA STVLSTAPPT MRPAPQPQDC PASICLNGGS 

       430        440        450        460        470        480 
CRLGARHHWE CLCPEGFIGL YCESPVEQGM KPSSIPDTPR PPPLLPLSIE PVSPTSLRVK 

       490        500        510        520        530        540 
LQRYLQGNTV QLRSLRLTYR NLSGPDKRLV TLRLPASLAE YTVTQLRPNA TYSICVTPLG 

       550        560        570        580        590        600 
AGRTPEGEEA CGEANTSQAV RSNHAPVTQA REGNLPLLIA PALAAVLLAV LAAAGAAYCV 

       610        620        630        640        650        660 
RRARATSTAQ DKGQVGPGTG PLELEGVKAP LEPGSKATEG GGEALSGGPE CEVPLMGYPG 

       670 
PSLQGVLPAK HYI 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression analysis of the mouse Slit-like 2 (Slitl2) gene."
Schrewe H., Kutejova E.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"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.
[3]"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.
[4]"Vasorin, a transforming growth factor beta-binding protein expressed in vascular smooth muscle cells, modulates the arterial response to injury in vivo."
Ikeda Y., Imai Y., Kumagai H., Nosaka T., Morikawa Y., Hisaoka T., Manabe I., Maemura K., Nakaoka T., Imamura T., Miyazono K., Komuro I., Nagai R., Kitamura T.
Proc. Natl. Acad. Sci. U.S.A. 101:10732-10737(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ458938 mRNA. Translation: CAD30331.1.
AK012169 mRNA. Translation: BAB28075.1.
AK083684 mRNA. Translation: BAC38992.1.
AK132325 mRNA. Translation: BAE21105.1.
BC050274 mRNA. Translation: AAH50274.1.
CCDSCCDS27921.1.
RefSeqNP_647468.2. NM_139307.3.
UniGeneMm.482140.

3D structure databases

ProteinModelPortalQ9CZT5.
SMRQ9CZT5. Positions 24-386, 464-543.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CZT5.

Proteomic databases

PaxDbQ9CZT5.
PRIDEQ9CZT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038770; ENSMUSP00000045162; ENSMUSG00000039646.
GeneID246154.
KEGGmmu:246154.
UCSCuc007xzz.2. mouse.

Organism-specific databases

CTD114990.
MGIMGI:2177651. Vasn.

Phylogenomic databases

eggNOGNOG273568.
GeneTreeENSGT00730000111167.
HOGENOMHOG000261606.
HOVERGENHBG084318.
InParanoidQ9CZT5.
OMAVTQLRPN.
OrthoDBEOG71ZP1F.
PhylomeDBQ9CZT5.
TreeFamTF351825.

Gene expression databases

BgeeQ9CZT5.
GenevestigatorQ9CZT5.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00041. fn3. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
[Graphical view]
SMARTSM00181. EGF. 1 hit.
SM00060. FN3. 1 hit.
SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50853. FN3. 1 hit.
PS51450. LRR. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio387103.
PROQ9CZT5.
SOURCESearch...

Entry information

Entry nameVASN_MOUSE
AccessionPrimary (citable) accession number: Q9CZT5
Secondary accession number(s): Q8BJJ0, Q8R2G5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: July 9, 2014
This is version 106 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