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P24014

- SLIT_DROME

UniProt

P24014 - SLIT_DROME

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Protein
Protein slit
Gene
sli, CG43758
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 11362Cleavage By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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

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 – 3636
Add
BLAST
Chaini37 – 15041468Protein slit
PRO_0000007719Add
BLAST
Chaini37 – 11351099Protein slit N-product By similarity
PRO_0000007720Add
BLAST
Chaini1136 – 1504369Protein slit C-product By similarity
PRO_0000007721Add
BLAST

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP24014.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 7 EGF-like domains.
Contains 4 LRRCT domains.
Contains 4 LRRNT domains.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 17524Missing in isoform A and isoform B.
VSP_001408Add
BLAST
Alternative sequencei1418 – 142811Missing in isoform B.
VSP_001409Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3512EL → DV in CAA37910. 1 Publication
Sequence conflicti350 – 3512EL → DV in AAD26567. 1 Publication
Sequence conflicti421 – 4211Q → R in CAA37910. 1 Publication
Sequence conflicti468 – 4681I → M in CAA37910. 1 Publication
Sequence conflicti527 – 5271D → G in CAA37910. 1 Publication
Sequence conflicti560 – 5601G → R in CAA37910. 1 Publication
Sequence conflicti691 – 6922WL → CV in CAA37910. 1 Publication
Sequence conflicti751 – 7511R → A in CAA37910. 1 Publication
Sequence conflicti843 – 8431L → V in CAA37910. 1 Publication
Sequence conflicti1207 – 12082AE → G in AAA72722. 1 Publication
Sequence conflicti1429 – 14357AASTCRK → GTYIYHA in AAA72722. 1 Publication

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...

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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: September 3, 2014
This is version 164 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

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