VASN_MOUSE
ID VASN_MOUSE Reviewed; 673 AA.
AC Q9CZT5; Q8BJJ0; Q8R2G5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Vasorin;
DE AltName: Full=Protein slit-like 2;
DE Flags: Precursor;
GN Name=Vasn; Synonyms=Slitl2;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Schrewe H., Kutejova E.;
RT "Structure and expression analysis of the mouse Slit-like 2 (Slitl2)
RT gene.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15247411; DOI=10.1073/pnas.0404117101;
RA Ikeda Y., Imai Y., Kumagai H., Nosaka T., Morikawa Y., Hisaoka T.,
RA Manabe I., Maemura K., Nakaoka T., Imamura T., Miyazono K., Komuro I.,
RA Nagai R., Kitamura T.;
RT "Vasorin, a transforming growth factor beta-binding protein expressed in
RT vascular smooth muscle cells, modulates the arterial response to injury in
RT vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10732-10737(2004).
CC -!- FUNCTION: May act as an inhibitor of TGF-beta signaling. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TGFB1, TGFB2 and TGFB3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at 10.5 dpc and increases as
CC development progresses to 17.5 dpc. Expression rises in parallel with
CC the differentiation of vascular smooth muscle cells (VSMCs) of the
CC aorta. {ECO:0000269|PubMed:15247411}.
CC -!- INDUCTION: Upon retinoic acid-induced differentiation of smooth muscle
CC cells in vitro. {ECO:0000269|PubMed:15247411}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AJ458938; CAD30331.1; -; mRNA.
DR EMBL; AK012169; BAB28075.1; -; mRNA.
DR EMBL; AK083684; BAC38992.1; -; mRNA.
DR EMBL; AK132325; BAE21105.1; -; mRNA.
DR EMBL; BC050274; AAH50274.1; -; mRNA.
DR CCDS; CCDS27921.1; -.
DR RefSeq; NP_647468.2; NM_139307.3.
DR AlphaFoldDB; Q9CZT5; -.
DR SMR; Q9CZT5; -.
DR BioGRID; 232880; 3.
DR STRING; 10090.ENSMUSP00000045162; -.
DR GlyConnect; 2817; 1 N-Linked glycan (1 site).
DR GlyGen; Q9CZT5; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9CZT5; -.
DR PhosphoSitePlus; Q9CZT5; -.
DR SwissPalm; Q9CZT5; -.
DR CPTAC; non-CPTAC-3511; -.
DR MaxQB; Q9CZT5; -.
DR PaxDb; Q9CZT5; -.
DR PeptideAtlas; Q9CZT5; -.
DR PRIDE; Q9CZT5; -.
DR ProteomicsDB; 300165; -.
DR Antibodypedia; 2203; 215 antibodies from 27 providers.
DR DNASU; 246154; -.
DR Ensembl; ENSMUST00000038770; ENSMUSP00000045162; ENSMUSG00000039646.
DR GeneID; 246154; -.
DR KEGG; mmu:246154; -.
DR UCSC; uc007xzz.2; mouse.
DR CTD; 114990; -.
DR MGI; MGI:2177651; Vasn.
DR VEuPathDB; HostDB:ENSMUSG00000039646; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159318; -.
DR HOGENOM; CLU_432517_0_0_1; -.
DR InParanoid; Q9CZT5; -.
DR OMA; CLENGGN; -.
DR OrthoDB; 397237at2759; -.
DR PhylomeDB; Q9CZT5; -.
DR TreeFam; TF351825; -.
DR BioGRID-ORCS; 246154; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Vasn; mouse.
DR PRO; PR:Q9CZT5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZT5; protein.
DR Bgee; ENSMUSG00000039646; Expressed in aorta tunica media and 249 other tissues.
DR Genevisible; Q9CZT5; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:MGI.
DR GO; GO:0071461; P:cellular response to redox state; IMP:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 8.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..673
FT /note="Vasorin"
FT /id="PRO_0000232631"
FT TOPO_DOM 25..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..53
FT /note="LRRNT"
FT REPEAT 54..75
FT /note="LRR 1"
FT REPEAT 78..99
FT /note="LRR 2"
FT REPEAT 102..123
FT /note="LRR 3"
FT REPEAT 126..147
FT /note="LRR 4"
FT REPEAT 150..170
FT /note="LRR 5"
FT REPEAT 171..192
FT /note="LRR 6"
FT REPEAT 194..215
FT /note="LRR 7"
FT REPEAT 218..239
FT /note="LRR 8"
FT REPEAT 241..265
FT /note="LRR 9"
FT REPEAT 266..288
FT /note="LRR 10"
FT DOMAIN 299..352
FT /note="LRRCT"
FT DOMAIN 406..443
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 463..559
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 369..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 410..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 415..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 225
FT /note="S -> Y (in Ref. 2; BAB28075)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> H (in Ref. 2; BAC38992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 72261 MW; AAB8DA82DA8E9D32 CRC64;
MHSRSCLPPL LLLLLVLLGS GVQGCPSGCQ CNQPQTVFCT ARQGTTVPRD VPPDTVGLYI
FENGITTLDV GCFAGLPGLQ LLDLSQNQIT SLPGGIFQPL VNLSNLDLTA NKLHEISNET
FRGLRRLERL YLGKNRIRHI QPGAFDALDR LLELKLPDNE LRVLPPLHLP RLLLLDLSHN
SIPALEAGIL DTANVEALRL AGLGLRQLDE GLFGRLLNLH DLDVSDNQLE HMPSVIQGLR
GLTRLRLAGN TRIAQIRPED LAGLTALQEL DVSNLSLQAL PSDLSSLFPR LRLLAAARNP
FNCLCPLSWF GPWVRENHVV LASPEETRCH FPPKNAGRLL LDLDYADFGC PVTTTTATVP
TIRSTIREPT LSTSSQAPTW PSLTEPTTQA STVLSTAPPT MRPAPQPQDC PASICLNGGS
CRLGARHHWE CLCPEGFIGL YCESPVEQGM KPSSIPDTPR PPPLLPLSIE PVSPTSLRVK
LQRYLQGNTV QLRSLRLTYR NLSGPDKRLV TLRLPASLAE YTVTQLRPNA TYSICVTPLG
AGRTPEGEEA CGEANTSQAV RSNHAPVTQA REGNLPLLIA PALAAVLLAV LAAAGAAYCV
RRARATSTAQ DKGQVGPGTG PLELEGVKAP LEPGSKATEG GGEALSGGPE CEVPLMGYPG
PSLQGVLPAK HYI
