UniProtKB - Q9WVC1 (SLIT2_RAT)
Slit homolog 2 protein
Slit2
Functioni
Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal cord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal cord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. Seems to be involved in regulating leukocyte migration (By similarity).
By similarityGO - Molecular functioni
- chemorepellent activity Source: RGD
- follicle-stimulating hormone receptor activity Source: InterPro
- GTPase inhibitor activity Source: RGD
- heparan sulfate proteoglycan binding Source: RGD
- heparin binding Source: RGD
- identical protein binding Source: RGD
- laminin-1 binding Source: RGD
- protein homodimerization activity Source: RGD
- proteoglycan binding Source: RGD
- Roundabout binding Source: RGD
GO - Biological processi
- aortic valve morphogenesis Source: RGD
- apoptotic process involved in luteolysis Source: RGD
- axon extension involved in axon guidance Source: RGD
- axon guidance Source: RGD
- axonogenesis Source: RGD
- brain development Source: RGD
- branching morphogenesis of an epithelial tube Source: RGD
- cell-cell adhesion Source: RGD
- cell migration involved in sprouting angiogenesis Source: RGD
- cellular response to heparin Source: RGD
- cellular response to hormone stimulus Source: RGD
- chemorepulsion involved in postnatal olfactory bulb interneuron migration Source: RGD
- corticospinal neuron axon guidance through spinal cord Source: RGD
- dorsal/ventral axon guidance Source: RGD
- induction of negative chemotaxis Source: RGD
- in utero embryonic development Source: RGD
- kidney development Source: RGD
- mammary duct terminal end bud growth Source: RGD
- mammary gland duct morphogenesis Source: RGD
- metanephros development Source: RGD
- motor neuron axon guidance Source: RGD
- negative chemotaxis Source: RGD
- negative regulation of actin filament polymerization Source: RGD
- negative regulation of axon extension Source: RGD
- negative regulation of cell growth Source: RGD
- negative regulation of cell migration Source: RGD
- negative regulation of cell population proliferation Source: RGD
- negative regulation of cellular response to growth factor stimulus Source: RGD
- negative regulation of chemokine-mediated signaling pathway Source: RGD
- negative regulation of endothelial cell migration Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of inflammatory response Source: RGD
- negative regulation of lamellipodium assembly Source: RGD
- negative regulation of leukocyte chemotaxis Source: RGD
- negative regulation of monocyte chemotaxis Source: BHF-UCL
- negative regulation of mononuclear cell migration Source: RGD
- negative regulation of neutrophil chemotaxis Source: RGD
- negative regulation of protein phosphorylation Source: RGD
- negative regulation of retinal ganglion cell axon guidance Source: RGD
- negative regulation of small GTPase mediated signal transduction Source: RGD
- negative regulation of smooth muscle cell chemotaxis Source: RGD
- negative regulation of smooth muscle cell migration Source: RGD
- negative regulation of vascular permeability Source: RGD
- neuron projection morphogenesis Source: RGD
- olfactory bulb development Source: RGD
- positive regulation of apoptotic process Source: RGD
- pulmonary valve morphogenesis Source: RGD
- response to cortisol Source: RGD
- response to nutrient levels Source: RGD
- retinal ganglion cell axon guidance Source: RGD
- Roundabout signaling pathway Source: RGD
- spinal cord development Source: RGD
- telencephalon cell migration Source: RGD
- ureteric bud development Source: RGD
- ventricular septum morphogenesis Source: RGD
Keywordsi
Molecular function | Developmental protein, Heparin-binding |
Biological process | Chemotaxis, Differentiation, Neurogenesis |
Names & Taxonomyi
Protein namesi | Recommended name: Slit homolog 2 proteinShort name: Slit-2 |
Gene namesi | Name:Slit2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 69310, Slit2 |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- extracellular space Source: RGD
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- cytoplasm Source: RGD
- integral component of membrane Source: InterPro
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 30 | Sequence analysisAdd BLAST | 30 | |
ChainiPRO_0000007731 | 31 – 766 | Slit homolog 2 proteinAdd BLAST | 736 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 66 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 186 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 281 ↔ 290 | By similarity | ||
Disulfide bondi | 438 ↔ 461 | By similarity | ||
Disulfide bondi | 440 ↔ 482 | By similarity | ||
Disulfide bondi | 502 ↔ 508 | By similarity | ||
Disulfide bondi | 506 ↔ 515 | By similarity | ||
Glycosylationi | 560 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 619 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 664 ↔ 687 | By similarity | ||
Disulfide bondi | 666 ↔ 708 | By similarity | ||
Disulfide bondi | 723 ↔ 729 | By similarity | ||
Disulfide bondi | 727 ↔ 736 | By similarity |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | Q9WVC1 |
PRIDEi | Q9WVC1 |
PTM databases
GlyGeni | Q9WVC1, 4 sites |
PhosphoSitePlusi | Q9WVC1 |
Expressioni
Developmental stagei
Interactioni
Subunit structurei
Homodimer. Binds ROBO1 and ROBO2 with high affinity (By similarity).
Interacts with GREM1.
By similarity1 PublicationGO - Molecular functioni
- chemorepellent activity Source: RGD
- heparan sulfate proteoglycan binding Source: RGD
- identical protein binding Source: RGD
- laminin-1 binding Source: RGD
- protein homodimerization activity Source: RGD
- proteoglycan binding Source: RGD
- Roundabout binding Source: RGD
Protein-protein interaction databases
IntActi | Q9WVC1, 1 interactor |
STRINGi | 10116.ENSRNOP00000005477 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 55 | LRRNTAdd BLAST | 25 | |
Repeati | 56 – 77 | LRR 1Add BLAST | 22 | |
Repeati | 80 – 101 | LRR 2Add BLAST | 22 | |
Repeati | 104 – 125 | LRR 3Add BLAST | 22 | |
Repeati | 128 – 149 | LRR 4Add BLAST | 22 | |
Repeati | 152 – 173 | LRR 5Add BLAST | 22 | |
Repeati | 176 – 197 | LRR 6Add BLAST | 22 | |
Domaini | 209 – 259 | LRRCT 1Add BLAST | 51 | |
Domaini | 268 – 304 | LRRNT 2Add BLAST | 37 | |
Repeati | 305 – 326 | LRR 7Add BLAST | 22 | |
Repeati | 329 – 350 | LRR 8Add BLAST | 22 | |
Repeati | 353 – 374 | LRR 9Add BLAST | 22 | |
Repeati | 377 – 398 | LRR 10Add BLAST | 22 | |
Repeati | 401 – 422 | LRR 11Add BLAST | 22 | |
Domaini | 434 – 484 | LRRCT 2Add BLAST | 51 | |
Domaini | 493 – 529 | LRRNT 3Add BLAST | 37 | |
Repeati | 530 – 551 | LRR 12Add BLAST | 22 | |
Repeati | 555 – 576 | LRR 13Add BLAST | 22 | |
Repeati | 579 – 600 | LRR 14Add BLAST | 22 | |
Repeati | 603 – 624 | LRR 15Add BLAST | 22 | |
Repeati | 627 – 648 | LRR 16Add BLAST | 22 | |
Domaini | 660 – 710 | LRRCT 3Add BLAST | 51 | |
Domaini | 714 – 750 | LRRNT 4Add BLAST | 37 |
Keywords - Domaini
Leucine-rich repeat, Repeat, SignalPhylogenomic databases
eggNOGi | KOG4237, Eukaryota |
InParanoidi | Q9WVC1 |
PhylomeDBi | Q9WVC1 |
Family and domain databases
Gene3Di | 3.80.10.10, 5 hits |
InterProi | View protein in InterPro IPR000483, Cys-rich_flank_reg_C IPR002272, FSH_rcpt IPR001611, Leu-rich_rpt IPR003591, Leu-rich_rpt_typical-subtyp IPR032675, LRR_dom_sf IPR000372, LRRNT |
Pfami | View protein in Pfam PF13855, LRR_8, 6 hits PF01463, LRRCT, 3 hits PF01462, LRRNT, 4 hits |
PRINTSi | PR01143, FSHRECEPTOR |
SMARTi | View protein in SMART SM00369, LRR_TYP, 14 hits SM00082, LRRCT, 3 hits SM00013, LRRNT, 4 hits |
PROSITEi | View protein in PROSITE PS51450, LRR, 16 hits |
(1+)i Sequence
Sequence statusi: Fragment.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MSGIGWQTLS LSLALVLSIL NKVAPHACPA QCSCSGSTVD CHGLALRIVP
60 70 80 90 100
RNIPRNTERL DLNGNNITRI TKTDFAGLRH LRILQLMENK ISTIERGAFH
110 120 130 140 150
DLKELERLRL NRNNLQLFPE LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA
160 170 180 190 200
VDIKNLQLDY NQISCIEDGA FRALRDLEVL TLNNNNITRL SVASFNHMPK
210 220 230 240 250
LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS HLRGHNVAEV
260 270 280 290 300
QKREFVCSDE EEGHQSFMAP SCSVLHCPIA CTCSNNIVDC RGKGLTEIPT
310 320 330 340 350
NLPETITEIR LEQNSIRVIP PGAFSPYKKL RRLDLSNNQI SELAPDAFQG
360 370 380 390 400
LRSLNSLVLY GNKITELPKS LFEGLFSLQL LLLNANKINC LRVDAFQDLH
410 420 430 440 450
NLNLLSLYDN KLQTVAKGTF SALRAIQTMH LAQNPFICDC HLKWLADYLH
460 470 480 490 500
TNPIETSGAR CTSPRRLANK RIGQIKSKKF RCSGTEDYRS KLSGDCFADL
510 520 530 540 550
ACPEKCRCEG TTVDCSNQKL NKIPDHIPQY TAELRLNNNE FTVLEATGIF
560 570 580 590 600
KKLPQLRKIN LSNNKITDIE EGAFEGASGV NEILLTSNRL ENVQHKMFKG
610 620 630 640 650
LESLKTLMLR SNRISCVGND SFTGLGSVRL LSLYDNQITT VAPGAFGTLH
660 670 680 690 700
SLSTLNLLAN PFNCNCHLAW LGEWLRRKRI VTGNPRCQKP YFLKEIPIQD
710 720 730 740 750
VAIQDFTCDD GNDDNSCSPL SRCPSECTCL DTVVRCSNKG LKVLPKGIPR
760
DVTELYLDGN QFTLVP
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1MA79 | F1MA79_RAT | Slit homolog 2 protein | Slit2 | 1,525 | Annotation score: | ||
A0A0G2KA49 | A0A0G2KA49_RAT | Slit homolog 2 protein | Slit2 | 1,533 | Annotation score: | ||
A0A8I6A6K5 | A0A8I6A6K5_RAT | Slit homolog 2 protein | Slit2 | 1,535 | Annotation score: | ||
A0A8I6AMD5 | A0A8I6AMD5_RAT | Slit homolog 2 protein | Slit2 | 1,542 | Annotation score: | ||
A0A8I6B4I9 | A0A8I6B4I9_RAT | Slit homolog 2 protein | Slit2 | 205 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 766 | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF141386 mRNA Translation: AAD38940.2 Different termination. |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF141386 mRNA Translation: AAD38940.2 Different termination. |
3D structure databases
AlphaFoldDBi | Q9WVC1 |
SMRi | Q9WVC1 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | Q9WVC1, 1 interactor |
STRINGi | 10116.ENSRNOP00000005477 |
PTM databases
GlyGeni | Q9WVC1, 4 sites |
PhosphoSitePlusi | Q9WVC1 |
Proteomic databases
PaxDbi | Q9WVC1 |
PRIDEi | Q9WVC1 |
Organism-specific databases
RGDi | 69310, Slit2 |
Phylogenomic databases
eggNOGi | KOG4237, Eukaryota |
InParanoidi | Q9WVC1 |
PhylomeDBi | Q9WVC1 |
Family and domain databases
Gene3Di | 3.80.10.10, 5 hits |
InterProi | View protein in InterPro IPR000483, Cys-rich_flank_reg_C IPR002272, FSH_rcpt IPR001611, Leu-rich_rpt IPR003591, Leu-rich_rpt_typical-subtyp IPR032675, LRR_dom_sf IPR000372, LRRNT |
Pfami | View protein in Pfam PF13855, LRR_8, 6 hits PF01463, LRRCT, 3 hits PF01462, LRRNT, 4 hits |
PRINTSi | PR01143, FSHRECEPTOR |
SMARTi | View protein in SMART SM00369, LRR_TYP, 14 hits SM00082, LRRCT, 3 hits SM00013, LRRNT, 4 hits |
PROSITEi | View protein in PROSITE PS51450, LRR, 16 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | SLIT2_RAT | |
Accessioni | Q9WVC1Primary (citable) accession number: Q9WVC1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 15, 2004 |
Last sequence update: | March 15, 2004 | |
Last modified: | May 25, 2022 | |
This is version 133 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |