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Protein

Slit homolog 2 protein

Gene

Slit2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 chord 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 chord 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 similarity

GO - Molecular functioni

GO - Biological processi

  • axon extension involved in axon guidance Source: GO_Central
  • brain development Source: RGD
  • central nervous system projection neuron axonogenesis Source: GO_Central
  • negative regulation of cell growth Source: GO_Central
  • negative regulation of inflammatory response Source: RGD
  • negative regulation of monocyte chemotaxis Source: BHF-UCL
  • regulation of axonogenesis Source: GO_Central
  • response to nutrient levels Source: RGD
  • retinal ganglion cell axon guidance Source: GO_Central
  • Roundabout signaling pathway Source: GO_Central
  • spinal cord development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Chemotaxis, Differentiation, Neurogenesis

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Slit homolog 2 protein
Short name:
Slit-2
Gene namesi
Name:Slit2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69310. Slit2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 766736Slit homolog 2 proteinPRO_0000007731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi281 ↔ 290By similarity
Disulfide bondi438 ↔ 461By similarity
Disulfide bondi440 ↔ 482By similarity
Disulfide bondi502 ↔ 508By similarity
Disulfide bondi506 ↔ 515By similarity
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence analysis
Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi664 ↔ 687By similarity
Disulfide bondi666 ↔ 708By similarity
Disulfide bondi723 ↔ 729By similarity
Disulfide bondi727 ↔ 736By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9WVC1.
PRIDEiQ9WVC1.

Expressioni

Developmental stagei

Detected at E20, between P0 and P10, and in adult in anterior olfactory nuclei, in cortex entorhinal region, hippocampal C3 and dentate gyrus, basal telencephalon septum, hypothalamus ventromedial and preoptic nuclei and dorsal thalamus medial habenula. Detected at E20 in cortex cortical plate. Detected between P0 and P10, and in adult basal telencephalon amygdaloid complex, and diencephalon pretectum optic tract nuclei.1 Publication

Interactioni

Subunit structurei

Homodimer. Binds ROBO1 and ROBO2 with high affinity (By similarity). Interacts with GREM1.By similarity1 Publication

GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: RGD
  • Roundabout binding Source: GO_Central

Protein-protein interaction databases

IntActiQ9WVC1. 1 interaction.
STRINGi10116.ENSRNOP00000005477.

Structurei

3D structure databases

ProteinModelPortaliQ9WVC1.
SMRiQ9WVC1. Positions 275-482, 501-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 5525LRRNTAdd
BLAST
Repeati56 – 7722LRR 1Add
BLAST
Repeati80 – 10122LRR 2Add
BLAST
Repeati104 – 12522LRR 3Add
BLAST
Repeati128 – 14922LRR 4Add
BLAST
Repeati152 – 17322LRR 5Add
BLAST
Repeati176 – 19722LRR 6Add
BLAST
Domaini209 – 25951LRRCT 1Add
BLAST
Domaini268 – 30437LRRNT 2Add
BLAST
Repeati305 – 32622LRR 7Add
BLAST
Repeati329 – 35022LRR 8Add
BLAST
Repeati353 – 37422LRR 9Add
BLAST
Repeati377 – 39822LRR 10Add
BLAST
Repeati401 – 42222LRR 11Add
BLAST
Domaini434 – 48451LRRCT 2Add
BLAST
Domaini493 – 52937LRRNT 3Add
BLAST
Repeati530 – 55122LRR 12Add
BLAST
Repeati555 – 57622LRR 13Add
BLAST
Repeati579 – 60022LRR 14Add
BLAST
Repeati603 – 62422LRR 15Add
BLAST
Repeati627 – 64822LRR 16Add
BLAST
Domaini660 – 71051LRRCT 3Add
BLAST
Domaini714 – 75037LRRNT 4Add
BLAST

Sequence similaritiesi

Contains at least 16 LRR (leucine-rich) repeats.Curated
Contains at least 3 LRRCT domains.Curated
Contains 4 LRRNT domains.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000170672.
HOVERGENiHBG057959.
InParanoidiQ9WVC1.
PhylomeDBiQ9WVC1.

Family and domain databases

Gene3Di3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR002272. FSH_rcpt.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 6 hits.
PF01463. LRRCT. 3 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
PRINTSiPR01143. FSHRECEPTOR.
SMARTiSM00369. LRR_TYP. 14 hits.
SM00082. LRRCT. 3 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 4 hits.
PROSITEiPS51450. LRR. 16 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

Q9WVC1-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:766
Mass (Da):86,049
Last modified:March 15, 2004 - v3
Checksum:iA380ACCE0A810FE1
GO

Sequence cautioni

The sequence AAD38940 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei766 – 7661

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141386 mRNA. Translation: AAD38940.2. Different termination.
UniGeneiRn.146652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF141386 mRNA. Translation: AAD38940.2. Different termination.
UniGeneiRn.146652.

3D structure databases

ProteinModelPortaliQ9WVC1.
SMRiQ9WVC1. Positions 275-482, 501-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVC1. 1 interaction.
STRINGi10116.ENSRNOP00000005477.

Proteomic databases

PaxDbiQ9WVC1.
PRIDEiQ9WVC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi69310. Slit2.

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000170672.
HOVERGENiHBG057959.
InParanoidiQ9WVC1.
PhylomeDBiQ9WVC1.

Family and domain databases

Gene3Di3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR002272. FSH_rcpt.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 6 hits.
PF01463. LRRCT. 3 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
PRINTSiPR01143. FSHRECEPTOR.
SMARTiSM00369. LRR_TYP. 14 hits.
SM00082. LRRCT. 3 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 4 hits.
PROSITEiPS51450. LRR. 16 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLIT2_RAT
AccessioniPrimary (citable) accession number: Q9WVC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: July 6, 2016
This is version 113 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.