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Q9CZT5

- VASN_MOUSE

UniProt

Q9CZT5 - VASN_MOUSE

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Protein

Vasorin

Gene

Vasn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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

GO - Biological processi

  1. cellular response to hypoxia Source: MGI
  2. cellular response to redox state Source: MGI
  3. negative regulation of epithelial to mesenchymal transition Source: Ensembl
  4. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Vasorin
Alternative name(s):
Protein slit-like 2
Gene namesi
Name:Vasn
Synonyms:Slitl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:2177651. Vasn.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. lysosomal membrane Source: Ensembl
  6. mitochondrion Source: MGI
  7. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 673649VasorinPRO_0000232631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi410 ↔ 421PROSITE-ProRule annotation
Disulfide bondi415 ↔ 431PROSITE-ProRule annotation
Disulfide bondi433 ↔ 442PROSITE-ProRule annotation
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9CZT5.
PaxDbiQ9CZT5.
PRIDEiQ9CZT5.

PTM databases

PhosphoSiteiQ9CZT5.

Expressioni

Developmental stagei

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.1 Publication

Inductioni

Upon retinoic acid-induced differentiation of smooth muscle cells in vitro.1 Publication

Gene expression databases

BgeeiQ9CZT5.
GenevestigatoriQ9CZT5.

Interactioni

Subunit structurei

Interacts with TGFB1, TGFB2 and TGFB3.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9CZT5.
SMRiQ9CZT5. Positions 22-386, 461-541.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 576552ExtracellularSequence AnalysisAdd
BLAST
Topological domaini598 – 67376CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei577 – 59721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 5329LRRNTAdd
BLAST
Repeati54 – 7522LRR 1Add
BLAST
Repeati78 – 9922LRR 2Add
BLAST
Repeati102 – 12322LRR 3Add
BLAST
Repeati126 – 14722LRR 4Add
BLAST
Repeati150 – 17021LRR 5Add
BLAST
Repeati171 – 19222LRR 6Add
BLAST
Repeati194 – 21522LRR 7Add
BLAST
Repeati218 – 23922LRR 8Add
BLAST
Repeati241 – 26525LRR 9Add
BLAST
Repeati266 – 28823LRR 10Add
BLAST
Domaini299 – 35254LRRCTAdd
BLAST
Domaini406 – 44338EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini463 – 55997Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 10 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

EGF-like domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG273568.
GeneTreeiENSGT00730000111167.
HOGENOMiHOG000261606.
HOVERGENiHBG084318.
InParanoidiQ9CZT5.
OMAiVTQLRPN.
OrthoDBiEOG71ZP1F.
PhylomeDBiQ9CZT5.
TreeFamiTF351825.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR000483. 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]
PfamiPF00008. EGF. 1 hit.
PF00041. fn3. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
SM00060. FN3. 1 hit.
SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50853. FN3. 1 hit.
PS51450. LRR. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CZT5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHSRSCLPPL LLLLLVLLGS GVQGCPSGCQ CNQPQTVFCT ARQGTTVPRD
60 70 80 90 100
VPPDTVGLYI FENGITTLDV GCFAGLPGLQ LLDLSQNQIT SLPGGIFQPL
110 120 130 140 150
VNLSNLDLTA NKLHEISNET FRGLRRLERL YLGKNRIRHI QPGAFDALDR
160 170 180 190 200
LLELKLPDNE LRVLPPLHLP RLLLLDLSHN SIPALEAGIL DTANVEALRL
210 220 230 240 250
AGLGLRQLDE GLFGRLLNLH DLDVSDNQLE HMPSVIQGLR GLTRLRLAGN
260 270 280 290 300
TRIAQIRPED LAGLTALQEL DVSNLSLQAL PSDLSSLFPR LRLLAAARNP
310 320 330 340 350
FNCLCPLSWF GPWVRENHVV LASPEETRCH FPPKNAGRLL LDLDYADFGC
360 370 380 390 400
PVTTTTATVP TIRSTIREPT LSTSSQAPTW PSLTEPTTQA STVLSTAPPT
410 420 430 440 450
MRPAPQPQDC PASICLNGGS CRLGARHHWE CLCPEGFIGL YCESPVEQGM
460 470 480 490 500
KPSSIPDTPR PPPLLPLSIE PVSPTSLRVK LQRYLQGNTV QLRSLRLTYR
510 520 530 540 550
NLSGPDKRLV TLRLPASLAE YTVTQLRPNA TYSICVTPLG AGRTPEGEEA
560 570 580 590 600
CGEANTSQAV RSNHAPVTQA REGNLPLLIA PALAAVLLAV LAAAGAAYCV
610 620 630 640 650
RRARATSTAQ DKGQVGPGTG PLELEGVKAP LEPGSKATEG GGEALSGGPE
660 670
CEVPLMGYPG PSLQGVLPAK HYI
Length:673
Mass (Da):72,261
Last modified:April 18, 2006 - v2
Checksum:iAAB8DA82DA8E9D32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251S → Y in BAB28075. (PubMed:16141072)Curated
Sequence conflicti383 – 3831L → H in BAC38992. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS27921.1.
RefSeqiNP_647468.2. NM_139307.3.
UniGeneiMm.482140.

Genome annotation databases

EnsembliENSMUST00000038770; ENSMUSP00000045162; ENSMUSG00000039646.
GeneIDi246154.
KEGGimmu:246154.
UCSCiuc007xzz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS27921.1.
RefSeqi NP_647468.2. NM_139307.3.
UniGenei Mm.482140.

3D structure databases

ProteinModelPortali Q9CZT5.
SMRi Q9CZT5. Positions 22-386, 461-541.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CZT5.

Proteomic databases

MaxQBi Q9CZT5.
PaxDbi Q9CZT5.
PRIDEi Q9CZT5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038770 ; ENSMUSP00000045162 ; ENSMUSG00000039646 .
GeneIDi 246154.
KEGGi mmu:246154.
UCSCi uc007xzz.2. mouse.

Organism-specific databases

CTDi 114990.
MGIi MGI:2177651. Vasn.

Phylogenomic databases

eggNOGi NOG273568.
GeneTreei ENSGT00730000111167.
HOGENOMi HOG000261606.
HOVERGENi HBG084318.
InParanoidi Q9CZT5.
OMAi VTQLRPN.
OrthoDBi EOG71ZP1F.
PhylomeDBi Q9CZT5.
TreeFami TF351825.

Miscellaneous databases

NextBioi 387103.
PROi Q9CZT5.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZT5.
Genevestigatori Q9CZT5.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR000483. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00041. fn3. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
[Graphical view ]
SMARTi SM00181. EGF. 1 hit.
SM00060. FN3. 1 hit.
SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50853. FN3. 1 hit.
PS51450. LRR. 8 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiVASN_MOUSE
AccessioniPrimary (citable) accession number: Q9CZT5
Secondary accession number(s): Q8BJJ0, Q8R2G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: October 29, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3