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O94813

- SLIT2_HUMAN

UniProt

O94813 - SLIT2_HUMAN

Protein

Slit homolog 2 protein

Gene

SLIT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1121 – 11222Cleavage

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. chemorepellent activity Source: Ensembl
    3. GTPase inhibitor activity Source: UniProtKB
    4. heparin binding Source: UniProtKB
    5. identical protein binding Source: IntAct
    6. laminin-1 binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein homodimerization activity Source: UniProtKB
    9. proteoglycan binding Source: UniProtKB
    10. Roundabout binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process involved in luteolysis Source: UniProtKB
    2. axon extension involved in axon guidance Source: UniProtKB
    3. axon guidance Source: UniProtKB
    4. branching morphogenesis of an epithelial tube Source: UniProtKB
    5. cell migration involved in sprouting angiogenesis Source: BHF-UCL
    6. cellular response to heparin Source: UniProtKB
    7. cellular response to hormone stimulus Source: UniProtKB
    8. chemorepulsion involved in postnatal olfactory bulb interneuron migration Source: UniProtKB
    9. corticospinal neuron axon guidance through spinal cord Source: BHF-UCL
    10. dorsal/ventral axon guidance Source: Ensembl
    11. induction of negative chemotaxis Source: UniProtKB
    12. in utero embryonic development Source: Ensembl
    13. mammary duct terminal end bud growth Source: Ensembl
    14. metanephros development Source: Ensembl
    15. motor neuron axon guidance Source: UniProtKB
    16. negative chemotaxis Source: UniProtKB
    17. negative regulation of actin filament polymerization Source: UniProtKB
    18. negative regulation of catalytic activity Source: GOC
    19. negative regulation of cell growth Source: BHF-UCL
    20. negative regulation of cell migration Source: UniProtKB
    21. negative regulation of cell proliferation Source: Ensembl
    22. negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
    23. negative regulation of chemokine-mediated signaling pathway Source: BHF-UCL
    24. negative regulation of endothelial cell migration Source: UniProtKB
    25. negative regulation of gene expression Source: Ensembl
    26. negative regulation of lamellipodium assembly Source: UniProtKB
    27. negative regulation of leukocyte chemotaxis Source: UniProtKB
    28. negative regulation of monocyte chemotaxis Source: BHF-UCL
    29. negative regulation of mononuclear cell migration Source: BHF-UCL
    30. negative regulation of neutrophil chemotaxis Source: UniProtKB
    31. negative regulation of protein phosphorylation Source: UniProtKB
    32. negative regulation of retinal ganglion cell axon guidance Source: UniProtKB
    33. negative regulation of small GTPase mediated signal transduction Source: UniProtKB
    34. negative regulation of smooth muscle cell chemotaxis Source: BHF-UCL
    35. negative regulation of smooth muscle cell migration Source: BHF-UCL
    36. negative regulation of vascular permeability Source: UniProtKB
    37. positive regulation of apoptotic process Source: UniProtKB
    38. positive regulation of axonogenesis Source: UniProtKB
    39. response to cortisol Source: UniProtKB
    40. retinal ganglion cell axon guidance Source: UniProtKB
    41. Roundabout signaling pathway Source: BHF-UCL
    42. single organismal cell-cell adhesion Source: Ensembl
    43. ureteric bud development Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Chemotaxis, Differentiation, Neurogenesis

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_19226. Activation of Rac.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_19342. Inactivation of Cdc42 and Rac.
    REACT_19351. Signaling by Robo receptor.
    REACT_19376. Regulation of Commissural axon pathfinding by Slit and Robo.
    REACT_22237. Netrin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Slit homolog 2 protein
    Short name:
    Slit-2
    Cleaved into the following 2 chains:
    Gene namesi
    Name:SLIT2
    Synonyms:SLIL3
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11086. SLIT2.

    Subcellular locationi

    Secreted 1 Publication
    Note: The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 15291499Slit homolog 2 proteinPRO_0000007725Add
    BLAST
    Chaini31 – 11211091Slit homolog 2 protein N-productPRO_0000007726Add
    BLAST
    Chaini1122 – 1529408Slit homolog 2 protein C-productPRO_0000007727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi277 ↔ 286
    Disulfide bondi434 ↔ 457
    Disulfide bondi436 ↔ 478
    Disulfide bondi506 ↔ 512
    Disulfide bondi510 ↔ 519
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi623 – 6231N-linked (GlcNAc...)
    Disulfide bondi668 ↔ 691
    Disulfide bondi670 ↔ 712
    Disulfide bondi727 ↔ 733
    Disulfide bondi731 ↔ 740
    Glycosylationi794 – 7941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi799 – 7991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi863 ↔ 886
    Disulfide bondi865 ↔ 907
    Disulfide bondi922 ↔ 933By similarity
    Disulfide bondi927 ↔ 943By similarity
    Disulfide bondi945 ↔ 954By similarity
    Disulfide bondi961 ↔ 972By similarity
    Disulfide bondi966 ↔ 984By similarity
    Disulfide bondi986 ↔ 995By similarity
    Disulfide bondi1002 ↔ 1013By similarity
    Disulfide bondi1007 ↔ 1022By similarity
    Glycosylationi1009 – 10091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1010 – 10101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1019 – 10191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1024 ↔ 1033By similarity
    Disulfide bondi1040 ↔ 1053By similarity
    Disulfide bondi1047 ↔ 1062By similarity
    Disulfide bondi1064 ↔ 1073By similarity
    Disulfide bondi1080 ↔ 1091By similarity
    Disulfide bondi1085 ↔ 1100By similarity
    Disulfide bondi1102 ↔ 1111By similarity
    Disulfide bondi1125 ↔ 1136By similarity
    Disulfide bondi1130 ↔ 1145By similarity
    Disulfide bondi1147 ↔ 1156By similarity
    Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1266 – 12661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1300 – 13001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1307 ↔ 1333By similarity
    Disulfide bondi1336 ↔ 1346By similarity
    Disulfide bondi1341 ↔ 1356By similarity
    Disulfide bondi1358 ↔ 1367By similarity
    Disulfide bondi1375 ↔ 1385By similarity
    Disulfide bondi1380 ↔ 1395By similarity
    Disulfide bondi1397 ↔ 1406By similarity
    Disulfide bondi1416 ↔ 1426By similarity
    Disulfide bondi1421 ↔ 1436By similarity
    Disulfide bondi1438 ↔ 1447By similarity
    Disulfide bondi1453 ↔ 1492By similarity
    Disulfide bondi1471 ↔ 1506By similarity
    Disulfide bondi1482 ↔ 1522By similarity
    Disulfide bondi1486 ↔ 1524By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO94813.
    PaxDbiO94813.
    PRIDEiO94813.

    PTM databases

    PhosphoSiteiO94813.

    Expressioni

    Tissue specificityi

    Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined.2 Publications

    Gene expression databases

    ArrayExpressiO94813.
    BgeeiO94813.
    CleanExiHS_SLIT2.
    GenevestigatoriO94813.

    Organism-specific databases

    HPAiCAB007590.
    HPA019511.
    HPA023088.

    Interactioni

    Subunit structurei

    Interacts with GREM1 By similarity. Homodimer. Binds ROBO1 and ROBO2 with high affinity.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1236865,EBI-1236865

    Protein-protein interaction databases

    BioGridi114756. 5 interactions.
    DIPiDIP-38198N.
    IntActiO94813. 7 interactions.
    MINTiMINT-6768470.
    STRINGi9606.ENSP00000273739.

    Structurei

    Secondary structure

    1
    1529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi277 – 2804
    Beta strandi283 – 2853
    Beta strandi304 – 3063
    Turni317 – 3226
    Beta strandi328 – 3303
    Turni341 – 3466
    Beta strandi352 – 3543
    Turni365 – 3706
    Beta strandi376 – 3783
    Turni389 – 3946
    Beta strandi400 – 4023
    Turni413 – 4186
    Beta strandi424 – 4263
    Helixi436 – 4383
    Helixi439 – 4479
    Beta strandi456 – 4605
    Helixi461 – 4633
    Helixi468 – 4703
    Helixi473 – 4753
    Beta strandi511 – 5133
    Beta strandi516 – 5183
    Beta strandi536 – 5394
    Helixi554 – 5563
    Beta strandi562 – 5643
    Turni575 – 5806
    Beta strandi586 – 5883
    Helixi599 – 6024
    Beta strandi610 – 6123
    Beta strandi633 – 6364
    Turni647 – 6526
    Beta strandi658 – 6603
    Helixi670 – 6723
    Helixi673 – 6819
    Beta strandi690 – 6945
    Helixi695 – 6973
    Helixi702 – 7043
    Helixi707 – 7093
    Beta strandi732 – 7343
    Beta strandi737 – 7393
    Beta strandi758 – 7603
    Helixi771 – 7755
    Beta strandi781 – 7833
    Turni794 – 7996
    Beta strandi805 – 8073
    Turni818 – 8236
    Beta strandi829 – 8313
    Turni842 – 8476
    Beta strandi853 – 8553
    Helixi865 – 8673
    Helixi868 – 8769
    Beta strandi885 – 8895
    Helixi890 – 8923
    Turni897 – 8993
    Helixi902 – 9043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V70X-ray3.01A/B/C/D504-714[»]
    2V9SX-ray2.00A/B/C/D271-480[»]
    2V9TX-ray1.70B271-479[»]
    2WFHX-ray1.80A/B726-907[»]
    ProteinModelPortaliO94813.
    SMRiO94813. Positions 25-1528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94813.

    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
    Domaini264 – 30037LRRNT 2Add
    BLAST
    Repeati301 – 32222LRR 7Add
    BLAST
    Repeati325 – 34622LRR 8Add
    BLAST
    Repeati349 – 37022LRR 9Add
    BLAST
    Repeati373 – 39422LRR 10Add
    BLAST
    Repeati397 – 41822LRR 11Add
    BLAST
    Domaini430 – 48051LRRCT 2Add
    BLAST
    Domaini497 – 53337LRRNT 3Add
    BLAST
    Repeati534 – 55522LRR 12Add
    BLAST
    Repeati559 – 58022LRR 13Add
    BLAST
    Repeati583 – 60422LRR 14Add
    BLAST
    Repeati607 – 62822LRR 15Add
    BLAST
    Repeati631 – 65222LRR 16Add
    BLAST
    Domaini664 – 71451LRRCT 3Add
    BLAST
    Domaini718 – 75437LRRNT 4Add
    BLAST
    Repeati755 – 77723LRR 17Add
    BLAST
    Repeati778 – 79922LRR 18Add
    BLAST
    Repeati802 – 82322LRR 19Add
    BLAST
    Repeati826 – 84722LRR 20Add
    BLAST
    Domaini859 – 90951LRRCT 4Add
    BLAST
    Domaini918 – 95538EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini957 – 99640EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 103437EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1036 – 107439EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1076 – 111237EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1121 – 115737EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1160 – 1333174Laminin G-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1332 – 136837EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1453 – 152876CTCKCuratedPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro.1 Publication

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 7 EGF-like domains.CuratedPROSITE-ProRule annotation
    Contains 1 laminin G-like domain.PROSITE-ProRule annotation
    Contains 20 LRR (leucine-rich) repeats.Curated
    Contains 4 LRRCT domains.Curated
    Contains 4 LRRNT domains.Curated

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000116120.
    HOVERGENiHBG057959.
    InParanoidiO94813.
    KOiK06839.
    OrthoDBiEOG78WKQW.
    PhylomeDBiO94813.
    TreeFamiTF332887.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000483. Cys-rich_flank_reg_C.
    IPR006207. Cys_knot_C.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR003645. Fol_N.
    IPR001791. Laminin_G.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF00008. EGF. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 7 hits.
    PF01463. LRRCT. 4 hits.
    PF01462. LRRNT. 4 hits.
    [Graphical view]
    SMARTiSM00041. CT. 1 hit.
    SM00181. EGF. 7 hits.
    SM00179. EGF_CA. 2 hits.
    SM00274. FOLN. 3 hits.
    SM00282. LamG. 1 hit.
    SM00369. LRR_TYP. 8 hits.
    SM00082. LRRCT. 4 hits.
    SM00013. LRRNT. 4 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 9 hits.
    PS01187. EGF_CA. 2 hits.
    PS50025. LAM_G_DOMAIN. 1 hit.
    PS51450. LRR. 20 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1Curated (identifier: O94813-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRGVGWQMLS LSLGLVLAIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP     50
    RNIPRNTERL DLNGNNITRI TKTDFAGLRH LRVLQLMENK ISTIERGAFQ 100
    DLKELERLRL NRNHLQLFPE LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA 150
    VDIKNLQLDY NQISCIEDGA FRALRDLEVL TLNNNNITRL SVASFNHMPK 200
    LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS HLRGHNVAEV 250
    QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE 300
    TITEIRLEQN TIKVIPPGAF SPYKKLRRID LSNNQISELA PDAFQGLRSL 350
    NSLVLYGNKI TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL 400
    LSLYDNKLQT IAKGTFSPLR AIQTMHLAQN PFICDCHLKW LADYLHTNPI 450
    ETSGARCTSP RRLANKRIGQ IKSKKFRCSA KEQYFIPGTE DYRSKLSGDC 500
    FADLACPEKC RCEGTTVDCS NQKLNKIPEH IPQYTAELRL NNNEFTVLEA 550
    TGIFKKLPQL RKINFSNNKI TDIEEGAFEG ASGVNEILLT SNRLENVQHK 600
    MFKGLESLKT LMLRSNRITC VGNDSFIGLS SVRLLSLYDN QITTVAPGAF 650
    DTLHSLSTLN LLANPFNCNC YLAWLGEWLR KKRIVTGNPR CQKPYFLKEI 700
    PIQDVAIQDF TCDDGNDDNS CSPLSRCPTE CTCLDTVVRC SNKGLKVLPK 750
    GIPRDVTELY LDGNQFTLVP KELSNYKHLT LIDLSNNRIS TLSNQSFSNM 800
    TQLLTLILSY NRLRCIPPRT FDGLKSLRLL SLHGNDISVV PEGAFNDLSA 850
    LSHLAIGANP LYCDCNMQWL SDWVKSEYKE PGIARCAGPG EMADKLLLTT 900
    PSKKFTCQGP VDVNILAKCN PCLSNPCKND GTCNSDPVDF YRCTCPYGFK 950
    GQDCDVPIHA CISNPCKHGG TCHLKEGEED GFWCICADGF EGENCEVNVD 1000
    DCEDNDCENN STCVDGINNY TCLCPPEYTG ELCEEKLDFC AQDLNPCQHD 1050
    SKCILTPKGF KCDCTPGYVG EHCDIDFDDC QDNKCKNGAH CTDAVNGYTC 1100
    ICPEGYSGLF CEFSPPMVLP RTSPCDNFDC QNGAQCIVRI NEPICQCLPG 1150
    YQGEKCEKLV SVNFINKESY LQIPSAKVRP QTNITLQIAT DEDSGILLYK 1200
    GDKDHIAVEL YRGRVRASYD TGSHPASAIY SVETINDGNF HIVELLALDQ 1250
    SLSLSVDGGN PKIITNLSKQ STLNFDSPLY VGGMPGKSNV ASLRQAPGQN 1300
    GTSFHGCIRN LYINSELQDF QKVPMQTGIL PGCEPCHKKV CAHGTCQPSS 1350
    QAGFTCECQE GWMGPLCDQR TNDPCLGNKC VHGTCLPINA FSYSCKCLEG 1400
    HGGVLCDEEE DLFNPCQAIK CKHGKCRLSG LGQPYCECSS GYTGDSCDRE 1450
    ISCRGERIRD YYQKQQGYAA CQTTKKVSRL ECRGGCAGGQ CCGPLRSKRR 1500
    KYSFECTDGS SFVDEVEKVV KCGCTRCVS 1529
    Length:1,529
    Mass (Da):169,870
    Last modified:May 1, 1999 - v1
    Checksum:i5D19CC5E7FD461BA
    GO
    Isoform 2Curated (identifier: O94813-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         258-258: S → SDEEE
         480-487: Missing.

    Show »
    Length:1,525
    Mass (Da):169,395
    Checksum:i56DE2356BB2E5CAD
    GO
    Isoform 3Curated (identifier: O94813-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         480-487: Missing.

    Show »
    Length:1,521
    Mass (Da):168,893
    Checksum:i7620F3C96DD4E534
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261Q → K in AAD25539. (PubMed:10349621)Curated
    Sequence conflicti607 – 6104SLKT → KPQN in AAD04309. (PubMed:10102268)Curated
    Sequence conflicti634 – 6341L → M in AAD04309. (PubMed:10102268)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti636 – 6361S → P.1 Publication
    VAR_018098
    Natural varianti1277 – 12771S → F.1 Publication
    VAR_018099

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei258 – 2581S → SDEEE in isoform 2. 2 PublicationsVSP_050035
    Alternative sequencei480 – 4878Missing in isoform 2 and isoform 3. 4 PublicationsVSP_050036

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017168 mRNA. Translation: BAA35185.1.
    AF055585 mRNA. Translation: AAD04309.1.
    AF133270 mRNA. Translation: AAD25539.1.
    CH471069 Genomic DNA. Translation: EAW92793.1.
    BC117190 mRNA. Translation: AAI17191.1.
    BC143978 mRNA. Translation: AAI43979.1.
    CCDSiCCDS3426.1. [O94813-1]
    RefSeqiNP_001276064.1. NM_001289135.1. [O94813-2]
    NP_001276065.1. NM_001289136.1. [O94813-3]
    NP_004778.1. NM_004787.2. [O94813-1]
    UniGeneiHs.29802.

    Genome annotation databases

    EnsembliENST00000503823; ENSP00000427548; ENSG00000145147. [O94813-3]
    ENST00000503837; ENSP00000422261; ENSG00000145147. [O94813-2]
    ENST00000504154; ENSP00000422591; ENSG00000145147. [O94813-1]
    GeneIDi9353.
    KEGGihsa:9353.
    UCSCiuc003gpr.1. human. [O94813-1]
    uc003gps.1. human. [O94813-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017168 mRNA. Translation: BAA35185.1 .
    AF055585 mRNA. Translation: AAD04309.1 .
    AF133270 mRNA. Translation: AAD25539.1 .
    CH471069 Genomic DNA. Translation: EAW92793.1 .
    BC117190 mRNA. Translation: AAI17191.1 .
    BC143978 mRNA. Translation: AAI43979.1 .
    CCDSi CCDS3426.1. [O94813-1 ]
    RefSeqi NP_001276064.1. NM_001289135.1. [O94813-2 ]
    NP_001276065.1. NM_001289136.1. [O94813-3 ]
    NP_004778.1. NM_004787.2. [O94813-1 ]
    UniGenei Hs.29802.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V70 X-ray 3.01 A/B/C/D 504-714 [» ]
    2V9S X-ray 2.00 A/B/C/D 271-480 [» ]
    2V9T X-ray 1.70 B 271-479 [» ]
    2WFH X-ray 1.80 A/B 726-907 [» ]
    ProteinModelPortali O94813.
    SMRi O94813. Positions 25-1528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114756. 5 interactions.
    DIPi DIP-38198N.
    IntActi O94813. 7 interactions.
    MINTi MINT-6768470.
    STRINGi 9606.ENSP00000273739.

    PTM databases

    PhosphoSitei O94813.

    Proteomic databases

    MaxQBi O94813.
    PaxDbi O94813.
    PRIDEi O94813.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000503823 ; ENSP00000427548 ; ENSG00000145147 . [O94813-3 ]
    ENST00000503837 ; ENSP00000422261 ; ENSG00000145147 . [O94813-2 ]
    ENST00000504154 ; ENSP00000422591 ; ENSG00000145147 . [O94813-1 ]
    GeneIDi 9353.
    KEGGi hsa:9353.
    UCSCi uc003gpr.1. human. [O94813-1 ]
    uc003gps.1. human. [O94813-3 ]

    Organism-specific databases

    CTDi 9353.
    GeneCardsi GC04P020254.
    HGNCi HGNC:11086. SLIT2.
    HPAi CAB007590.
    HPA019511.
    HPA023088.
    MIMi 603746. gene.
    neXtProti NX_O94813.
    PharmGKBi PA35939.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000116120.
    HOVERGENi HBG057959.
    InParanoidi O94813.
    KOi K06839.
    OrthoDBi EOG78WKQW.
    PhylomeDBi O94813.
    TreeFami TF332887.

    Enzyme and pathway databases

    Reactomei REACT_19226. Activation of Rac.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_19342. Inactivation of Cdc42 and Rac.
    REACT_19351. Signaling by Robo receptor.
    REACT_19376. Regulation of Commissural axon pathfinding by Slit and Robo.
    REACT_22237. Netrin-1 signaling.

    Miscellaneous databases

    EvolutionaryTracei O94813.
    GeneWikii SLIT2.
    GenomeRNAii 9353.
    NextBioi 35025.
    PROi O94813.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94813.
    Bgeei O94813.
    CleanExi HS_SLIT2.
    Genevestigatori O94813.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000483. Cys-rich_flank_reg_C.
    IPR006207. Cys_knot_C.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR003645. Fol_N.
    IPR001791. Laminin_G.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF00008. EGF. 6 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 7 hits.
    PF01463. LRRCT. 4 hits.
    PF01462. LRRNT. 4 hits.
    [Graphical view ]
    SMARTi SM00041. CT. 1 hit.
    SM00181. EGF. 7 hits.
    SM00179. EGF_CA. 2 hits.
    SM00274. FOLN. 3 hits.
    SM00282. LamG. 1 hit.
    SM00369. LRR_TYP. 8 hits.
    SM00082. LRRCT. 4 hits.
    SM00013. LRRNT. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 7 hits.
    PS50026. EGF_3. 9 hits.
    PS01187. EGF_CA. 2 hits.
    PS50025. LAM_G_DOMAIN. 1 hit.
    PS51450. LRR. 20 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation and maintenance of the nervous system."
      Itoh A., Miyabayashi T., Ohno M., Sakano S.
      Brain Res. Mol. Brain Res. 62:175-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANTS PRO-636 AND PHE-1277.
      Tissue: Fetal lung.
    2. "Distinct but overlapping expression patterns of two vertebrate slit homologs implies functional roles in CNS development and organogenesis."
      Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T., Little M.H.
      Mech. Dev. 79:57-72(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Fetal brain and Fetal kidney.
    3. "Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance."
      Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S., Tessier-Lavigne M., Kidd T.
      Cell 96:795-806(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1122-1129, FUNCTION, INTERACTION WITH ROBO1 AND ROBO2, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 3).
    6. "Squeezing axons out of the gray matter: a role for slit and semaphorin proteins from midline and ventral spinal cord."
      Zou Y., Stoeckli E., Chen H., Tessier-Lavigne M.
      Cell 102:363-375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Slit2 is a repellent for retinal ganglion cell axons."
      Niclou S.P., Jia L., Raper J.A.
      J. Neurosci. 20:4962-4974(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The neuronal repellent Slit inhibits leukocyte chemotaxis induced by chemotactic factors."
      Wu J.Y., Feng L., Park H.T., Havlioglu N., Wen L., Tang H., Bacon K.B., Jiang Z.H., Zhang X.C., Rao Y.
      Nature 410:948-952(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The N-terminal leucine-rich regions in Slit are sufficient to repel olfactory bulb axons and subventricular zone neurons."
      Chen J.H., Wen L., Dupuis S., Wu J.Y., Rao Y.
      J. Neurosci. 21:1548-1556(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    10. "Diversity and specificity of actions of Slit2 proteolytic fragments in axon guidance."
      Nguyen-Ba-Charvet K.T., Brose K., Ma L., Wang K.H., Marillat V., Sotelo C., Tessier-Lavigne M., Chedotal A.
      J. Neurosci. 21:4281-4289(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ROBO1 AND ROBO2.
    11. "Hierarchical organization of guidance receptors: silencing of netrin attraction by slit through a Robo/DCC receptor complex."
      Stein E., Tessier-Lavigne M.
      Science 291:1928-1938(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Slit proteins: molecular guidance cues for cells ranging from neurons to leukocytes."
      Wong K., Park H.T., Wu J.Y., Rao Y.
      Curr. Opin. Genet. Dev. 12:583-591(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "Production of Slit2 LRR domains in mammalian cells for structural studies and the structure of human Slit2 domain 3."
      Morlot C., Hemrika W., Romijn R.A., Gros P., Cusack S., McCarthy A.A.
      Acta Crystallogr. D 63:961-968(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 504-716, DISULFIDE BONDS.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-480 IN COMPLEX WITH ROBO1, DISULFIDE BONDS.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 726-907, SUBUNIT, DISULFIDE BONDS, HEPARIN-BINDING.

    Entry informationi

    Entry nameiSLIT2_HUMAN
    AccessioniPrimary (citable) accession number: O94813
    Secondary accession number(s): B7ZLR5
    , O95710, Q17RU3, Q9Y5Q7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3