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P24014

- SLIT_DROME

UniProt

P24014 - SLIT_DROME

Protein

Protein slit

Gene

sli

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 2 (28 Feb 2003)
      Previous versions | rss
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    Functioni

    A short-range repellent, controlling axon crossing of the midline and a long-range chemorepellent, controlling mesoderm migration and patterning away from the midline. May interact with extracellular matrix molecules. Repulsive ligand for the guidance receptor roundabout (robo) and prevents inappropriate midline crossing by Robo-expressing axons.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1135 – 11362CleavageBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. heparin binding Source: FlyBase
    3. protein binding Source: FlyBase
    4. Roundabout binding Source: FlyBase

    GO - Biological processi

    1. axon guidance Source: FlyBase
    2. axon midline choice point recognition Source: FlyBase
    3. dendrite morphogenesis Source: FlyBase
    4. digestive tract mesoderm development Source: FlyBase
    5. embryonic heart tube development Source: FlyBase
    6. epithelial cell migration, open tracheal system Source: FlyBase
    7. glial cell migration Source: UniProtKB
    8. gonad development Source: FlyBase
    9. induction of negative chemotaxis Source: UniProtKB
    10. lateral inhibition Source: FlyBase
    11. mesodermal cell migration Source: FlyBase
    12. mesoderm migration involved in gastrulation Source: UniProtKB
    13. neuron differentiation Source: FlyBase
    14. neuron migration Source: FlyBase
    15. outflow tract morphogenesis Source: FlyBase
    16. positive regulation of cell-cell adhesion Source: FlyBase
    17. regulation of epithelial cell migration Source: FlyBase
    18. regulation of epithelial cell migration, open tracheal system Source: FlyBase
    19. Roundabout signaling pathway Source: FlyBase
    20. salivary gland boundary specification Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein slit
    Short name:
    dSlit
    Cleaved into the following 2 chains:
    Gene namesi
    Name:sli
    ORF Names:CG43758
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0264089. sli.

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. extracellular matrix Source: FlyBase
    2. extracellular region Source: UniProtKB
    3. plasma membrane Source: Reactome
    4. proteinaceous extracellular matrix Source: FlyBase
    5. Slit-Robo signaling complex Source: FlyBase

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Flies lacking sli exhibit disruption of the developing midline cells and the commissural axon pathways.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3636Add
    BLAST
    Chaini37 – 15041468Protein slitPRO_0000007719Add
    BLAST
    Chaini37 – 11351099Protein slit N-productBy similarityPRO_0000007720Add
    BLAST
    Chaini1136 – 1504369Protein slit C-productBy similarityPRO_0000007721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi543 ↔ 5491 Publication
    Disulfide bondi547 ↔ 5561 Publication
    Disulfide bondi657 ↔ 7331 Publication
    Disulfide bondi681 ↔ 7041 Publication
    Disulfide bondi683 ↔ 7251 Publication
    Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi812 – 8121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi935 ↔ 946By similarity
    Disulfide bondi940 ↔ 956By similarity
    Disulfide bondi958 ↔ 967By similarity
    Disulfide bondi974 ↔ 985By similarity
    Disulfide bondi979 ↔ 995By similarity
    Glycosylationi982 – 9821N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi997 ↔ 1006By similarity
    Disulfide bondi1013 ↔ 1025By similarity
    Disulfide bondi1019 ↔ 1034By similarity
    Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1036 ↔ 1045By similarity
    Disulfide bondi1052 ↔ 1065By similarity
    Disulfide bondi1059 ↔ 1074By similarity
    Disulfide bondi1076 ↔ 1085By similarity
    Glycosylationi1084 – 10841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1092 ↔ 1103By similarity
    Disulfide bondi1097 ↔ 1112By similarity
    Disulfide bondi1114 ↔ 1123By similarity
    Disulfide bondi1139 ↔ 1149By similarity
    Disulfide bondi1144 ↔ 1161By similarity
    Disulfide bondi1163 ↔ 1172By similarity
    Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1199 – 11991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1316 – 13161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1323 ↔ 1349By similarity
    Disulfide bondi1381 ↔ 1392By similarity
    Disulfide bondi1386 ↔ 1404By similarity
    Disulfide bondi1406 ↔ 1415By similarity
    Disulfide bondi1433 ↔ 1467By similarity
    Disulfide bondi1447 ↔ 1481By similarity
    Disulfide bondi1458 ↔ 1497By similarity
    Disulfide bondi1462 ↔ 1499By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP24014.

    Expressioni

    Tissue specificityi

    In embryos, highest expression occurs around the midline glia and low expression is observed around CNS axons lateral to the midline. Expression can be seen on the commissural axons traversing the glial cells but it is absent from the cell bodies of these neurons.3 Publications

    Gene expression databases

    BgeeiP24014.

    Interactioni

    Subunit structurei

    Interacts with robo.1 Publication

    Protein-protein interaction databases

    BioGridi62473. 14 interactions.
    IntActiP24014. 3 interactions.

    Structurei

    Secondary structure

    1
    1504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi547 – 5504
    Beta strandi553 – 5553
    Beta strandi573 – 5764
    Helixi591 – 5933
    Beta strandi599 – 6013
    Turni612 – 6176
    Beta strandi623 – 6253
    Beta strandi636 – 6394
    Beta strandi647 – 6493
    Beta strandi671 – 6733
    Helixi683 – 6853
    Helixi686 – 69510
    Helixi699 – 7013
    Turni708 – 7125
    Helixi715 – 7173
    Turni720 – 7223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W8AX-ray2.80A542-733[»]
    ProteinModelPortaliP24014.
    SMRiP24014. Positions 73-921, 933-1433.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24014.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 10037LRRNT 1Add
    BLAST
    Repeati101 – 12222LRR 1Add
    BLAST
    Repeati125 – 14622LRR 2Add
    BLAST
    Repeati149 – 17022LRR 3Add
    BLAST
    Repeati173 – 19422LRR 4Add
    BLAST
    Repeati197 – 21822LRR 5Add
    BLAST
    Repeati221 – 24222LRR 6Add
    BLAST
    Domaini254 – 30451LRRCT 1Add
    BLAST
    Domaini310 – 34637LRRNT 2Add
    BLAST
    Repeati347 – 36822LRR 7Add
    BLAST
    Repeati371 – 39222LRR 8Add
    BLAST
    Repeati395 – 41622LRR 9Add
    BLAST
    Repeati419 – 44022LRR 10Add
    BLAST
    Repeati443 – 46422LRR 11Add
    BLAST
    Domaini476 – 52651LRRCT 2Add
    BLAST
    Domaini534 – 57037LRRNT 3Add
    BLAST
    Repeati571 – 59222LRR 12Add
    BLAST
    Repeati596 – 61722LRR 13Add
    BLAST
    Repeati620 – 64122LRR 14Add
    BLAST
    Repeati644 – 66522LRR 15Add
    BLAST
    Domaini677 – 72751LRRCT 3Add
    BLAST
    Domaini730 – 76637LRRNT 4Add
    BLAST
    Repeati767 – 78822LRR 16Add
    BLAST
    Repeati791 – 81222LRR 17Add
    BLAST
    Repeati815 – 83622LRR 18Add
    BLAST
    Repeati839 – 86022LRR 19Add
    BLAST
    Domaini872 – 92251LRRCT 4Add
    BLAST
    Domaini931 – 96838EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini970 – 100738EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1009 – 104638EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1048 – 108639EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1088 – 112437EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1135 – 117339EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1176 – 1349174Laminin G-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1377 – 141640EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1433 – 150472CTCKPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 7 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.PROSITE-ProRule annotation
    Contains 19 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.
    GeneTreeiENSGT00750000117236.
    InParanoidiP24014.
    KOiK06839.
    PhylomeDBiP24014.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001791. Laminin_G.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    [Graphical view]
    PfamiPF00008. EGF. 5 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF00560. LRR_1. 1 hit.
    PF13306. LRR_5. 1 hit.
    PF13855. LRR_8. 3 hits.
    PF01463. LRRCT. 4 hits.
    PF01462. LRRNT. 4 hits.
    [Graphical view]
    SMARTiSM00041. CT. 1 hit.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00282. LamG. 1 hit.
    SM00369. LRR_TYP. 9 hits.
    SM00082. LRRCT. 4 hits.
    SM00013. LRRNT. 4 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
    PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 7 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 C (identifier: P24014-1) [UniParc]FASTAAdd to Basket

    Also known as: E

    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

    MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS     50
    GGLGSVGIHI PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA 100
    DVERLELQGN NLTVIYETDF QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL 150
    ERLRLNNNRL KAIPENFVTS SASLLRLDIS NNVITTVGRR VFKGAQSLRS 200
    LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF GGLGRLRALR 250
    LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF 300
    KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE 350
    LRLEQNFITE LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV 400
    LYGNKIKDLP SGVFKGLGSL QLLLLNANEI SCIRKDAFRD LHSLSLLSLY 450
    DNNIQSLANG TFDAMKSIKT VHLAKNPFIC DCNLRWLADY LHKNPIETSG 500
    ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD SDCPAMCHCE 550
    GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL 600
    ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL 650
    YDNQISCVMP GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG 700
    AARCGAPSKV RDVQIKDLPH SEFKCSSENS EGCLGDGYCP PSCTCTGTVV 750
    RCSRNQLKEI PRGIPAETSE LYLESNEIEQ IHYERIRHLR SLTRLDLSNN 800
    QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL RVLSLHGNRI 850
    SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA 900
    EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP 950
    QREYQCLCQP GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG 1000
    YTGARCETNI DDCLGEIKCQ NNATCIDGVE SYKCECQPGF SGEFCDTKIQ 1050
    FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF HGTNCTDNID DCQNHMCQNG 1100
    GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ NHECKHGVCF 1150
    QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV 1200
    TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM 1250
    VADGKYHAVE LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL 1300
    PVDPAQQAYK NWQIRNLTSF KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA 1350
    LLEGEQQEEE DDEQDFMDET PHIKEEPVDP CLENKCRRGS RCVPNSNARD 1400
    GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE YYTENDCRSR 1450
    QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT 1500
    KKCY 1504
    Length:1,504
    Mass (Da):168,599
    Last modified:February 28, 2003 - v2
    Checksum:i836A3F5022BF234F
    GO
    Isoform A (identifier: P24014-2) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         152-175: Missing.

    Show »
    Length:1,480
    Mass (Da):165,890
    Checksum:iF456BC617D8453ED
    GO
    Isoform B (identifier: P24014-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         152-175: Missing.
         1418-1428: Missing.

    Show »
    Length:1,469
    Mass (Da):164,834
    Checksum:i14DBA99CE1DAEAC4
    GO

    Sequence cautioni

    The sequence AAA72722.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti350 – 3512EL → DV in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti350 – 3512EL → DV in AAD26567. (PubMed:10102267)Curated
    Sequence conflicti421 – 4211Q → R in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti468 – 4681I → M in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti527 – 5271D → G in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti560 – 5601G → R in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti691 – 6922WL → CV in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti751 – 7511R → A in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti843 – 8431L → V in CAA37910. (PubMed:2176636)Curated
    Sequence conflicti1207 – 12082AE → G in AAA72722. (PubMed:3144436)Curated
    Sequence conflicti1429 – 14357AASTCRK → GTYIYHA in AAA72722. (PubMed:3144436)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei152 – 17524Missing in isoform A and isoform B. 1 PublicationVSP_001408Add
    BLAST
    Alternative sequencei1418 – 142811Missing in isoform B. 1 PublicationVSP_001409Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53959 mRNA. Translation: CAA37910.1.
    AF126540 mRNA. Translation: AAD26567.1.
    AE013599 Genomic DNA. Translation: AAF58097.1.
    AE013599 Genomic DNA. Translation: AAF58098.1.
    AE013599 Genomic DNA. Translation: AAM70966.1.
    AE013599 Genomic DNA. Translation: ABV53816.1.
    AE013599 Genomic DNA. Translation: ABV53817.1.
    M23543 Genomic DNA. Translation: AAA72722.1. Different initiation.
    PIRiA36665.
    B36665.
    RefSeqiNP_001097333.1. NM_001103863.2. [P24014-2]
    NP_001097334.1. NM_001103864.2. [P24014-1]
    NP_476727.1. NM_057379.4. [P24014-1]
    NP_476728.1. NM_057380.4. [P24014-2]
    NP_476729.1. NM_057381.4. [P24014-3]
    UniGeneiDm.4729.

    Genome annotation databases

    EnsemblMetazoaiFBtr0330731; FBpp0303575; FBgn0264089. [P24014-1]
    FBtr0330733; FBpp0303577; FBgn0264089. [P24014-1]
    GeneIDi36746.
    KEGGidme:Dmel_CG43758.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53959 mRNA. Translation: CAA37910.1 .
    AF126540 mRNA. Translation: AAD26567.1 .
    AE013599 Genomic DNA. Translation: AAF58097.1 .
    AE013599 Genomic DNA. Translation: AAF58098.1 .
    AE013599 Genomic DNA. Translation: AAM70966.1 .
    AE013599 Genomic DNA. Translation: ABV53816.1 .
    AE013599 Genomic DNA. Translation: ABV53817.1 .
    M23543 Genomic DNA. Translation: AAA72722.1 . Different initiation.
    PIRi A36665.
    B36665.
    RefSeqi NP_001097333.1. NM_001103863.2. [P24014-2 ]
    NP_001097334.1. NM_001103864.2. [P24014-1 ]
    NP_476727.1. NM_057379.4. [P24014-1 ]
    NP_476728.1. NM_057380.4. [P24014-2 ]
    NP_476729.1. NM_057381.4. [P24014-3 ]
    UniGenei Dm.4729.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W8A X-ray 2.80 A 542-733 [» ]
    ProteinModelPortali P24014.
    SMRi P24014. Positions 73-921, 933-1433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62473. 14 interactions.
    IntActi P24014. 3 interactions.

    Proteomic databases

    PaxDbi P24014.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0330731 ; FBpp0303575 ; FBgn0264089 . [P24014-1 ]
    FBtr0330733 ; FBpp0303577 ; FBgn0264089 . [P24014-1 ]
    GeneIDi 36746.
    KEGGi dme:Dmel_CG43758.

    Organism-specific databases

    CTDi 36746.
    FlyBasei FBgn0264089. sli.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00750000117236.
    InParanoidi P24014.
    KOi K06839.
    PhylomeDBi P24014.

    Miscellaneous databases

    EvolutionaryTracei P24014.
    GenomeRNAii 36746.
    NextBioi 800151.

    Gene expression databases

    Bgeei P24014.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001791. Laminin_G.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    [Graphical view ]
    Pfami PF00008. EGF. 5 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF00560. LRR_1. 1 hit.
    PF13306. LRR_5. 1 hit.
    PF13855. LRR_8. 3 hits.
    PF01463. LRRCT. 4 hits.
    PF01462. LRRNT. 4 hits.
    [Graphical view ]
    SMARTi SM00041. CT. 1 hit.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00282. LamG. 1 hit.
    SM00369. LRR_TYP. 9 hits.
    SM00082. LRRCT. 4 hits.
    SM00013. LRRNT. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
    PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 5 hits.
    PS50026. EGF_3. 7 hits.
    PS01187. EGF_CA. 2 hits.
    PS50025. LAM_G_DOMAIN. 1 hit.
    PS51450. LRR. 20 hits.
    [Graphical view ]
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    Publicationsi

    1. "Slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains."
      Rothberg J.M., Jacobs J.R., Goodman C.S., Artavanis-Tsakonas S.
      Genes Dev. 4:2169-2187(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "Slit is the midline repellent for the robo receptor in Drosophila."
      Kidd T., Bland K.S., Goodman C.S.
      Cell 96:785-794(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. "slit: an EGF-homologous locus of D. melanogaster involved in the development of the embryonic central nervous system."
      Rothberg J.M., Hartley D.A., Walther Z., Artavanis-Tsakonas S.
      Cell 55:1047-1059(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 898-1435, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
      Strain: Canton-S.
    6. "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: FUNCTION, INTERACTION WITH ROBO, CLEAVAGE.
    7. "Binding site for Robo receptors revealed by dissection of the leucine-rich repeat region of Slit."
      Howitt J.A., Clout N.J., Hohenester E.
      EMBO J. 23:4406-4412(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 542-733, DISULFIDE BONDS IN THE LRR REGION.

    Entry informationi

    Entry nameiSLIT_DROME
    AccessioniPrimary (citable) accession number: P24014
    Secondary accession number(s): A8DYF5
    , A8DYF6, Q24526, Q8MLB9, Q9V7F8, Q9V7F9, Q9XYV4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: February 28, 2003
    Last modified: October 1, 2014
    This is version 165 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3