CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020701
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Vasorin 
Protein Synonyms/Alias
 Protein slit-like 2 
Gene Name
 Vasn 
Gene Synonyms/Alias
 Slitl2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
628PLELEGVKAPLEPGSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 May act as an inhibitor of TGF-beta signaling (By similarity). 
Sequence Annotation
 DOMAIN 25 53 LRRNT.
 REPEAT 54 75 LRR 1.
 REPEAT 78 99 LRR 2.
 REPEAT 102 123 LRR 3.
 REPEAT 126 147 LRR 4.
 REPEAT 150 170 LRR 5.
 REPEAT 171 192 LRR 6.
 REPEAT 194 215 LRR 7.
 REPEAT 218 239 LRR 8.
 REPEAT 241 265 LRR 9.
 REPEAT 266 288 LRR 10.
 DOMAIN 299 352 LRRCT.
 DOMAIN 406 443 EGF-like.
 DOMAIN 459 556 Fibronectin type-III.
 CARBOHYD 102 102 N-linked (GlcNAc...) (Potential).
 CARBOHYD 118 118 N-linked (GlcNAc...) (Potential).
 CARBOHYD 274 274 N-linked (GlcNAc...) (Potential).
 CARBOHYD 501 501 N-linked (GlcNAc...) (Potential).
 CARBOHYD 529 529 N-linked (GlcNAc...) (Potential).
 CARBOHYD 555 555 N-linked (GlcNAc...) (Potential).
 DISULFID 410 421 By similarity.
 DISULFID 415 431 By similarity.
 DISULFID 433 442 By similarity.  
Keyword
 Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 673 AA 
Protein Sequence
MHSRSCLPPL LLLLLVLLGS GVQGCPSGCQ CNQPQTVFCT ARQGTTVPRD VPPDTVGLYI 60
FENGITTLDV GCFAGLPGLQ LLDLSQNQIT SLPGGIFQPL VNLSNLDLTA NKLHEISNET 120
FRGLRRLERL YLGKNRIRHI QPGAFDALDR LLELKLPDNE LRVLPPLHLP RLLLLDLSHN 180
SIPALEAGIL DTANVEALRL AGLGLRQLDE GLFGRLLNLH DLDVSDNQLE HMPSVIQGLR 240
GLTRLRLAGN TRIAQIRPED LAGLTALQEL DVSNLSLQAL PSDLSSLFPR LRLLAAARNP 300
FNCLCPLSWF GPWVRENHVV LASPEETRCH FPPKNAGRLL LDLDYADFGC PVTTTTATVP 360
TIRSTIREPT LSTSSQAPTW PSLTEPTTQA STVLSTAPPT MRPAPQPQDC PASICLNGGS 420
CRLGARHHWE CLCPEGFIGL YCESPVEQGM KPSSIPDTPR PPPLLPLSIE PVSPTSLRVK 480
LQRYLQGNTV QLRSLRLTYR NLSGPDKRLV TLRLPASLAE YTVTQLRPNA TYSICVTPLG 540
AGRTPEGEEA CGEANTSQAV RSNHAPVTQA REGNLPLLIA PALAAVLLAV LAAAGAAYCV 600
RRARATSTAQ DKGQVGPGTG PLELEGVKAP LEPGSKATEG GGEALSGGPE CEVPLMGYPG 660
PSLQGVLPAK HYI 673 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005886; C:plasma membrane; IDA:MGI.
 GO:0071456; P:cellular response to hypoxia; IMP:MGI.
 GO:0071461; P:cellular response to redox state; IMP:MGI. 
Interpro
 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. 
Pfam
 PF00008; EGF
 PF00041; fn3
 PF00560; LRR_1 
SMART
 SM00181; EGF
 SM00060; FN3
 SM00369; LRR_TYP
 SM00082; LRRCT
 SM00013; LRRNT 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS50853; FN3
 PS51450; LRR 
PRINTS