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P24014

- SLIT_DROME

UniProt

P24014 - SLIT_DROME

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Protein

Protein slit

Gene

sli

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 – 11362CleavageBy similarity

GO - Molecular functioni

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

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_236260. Netrin-1 signaling.
REACT_246260. Signaling by Robo receptor.
REACT_246981. Inactivation of Cdc42 and Rac.
REACT_256055. Role of Abl in Robo-Slit signaling.
REACT_263619. Activation of Rac.

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
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 – 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 – 5504Combined sources
Beta strandi553 – 5553Combined sources
Beta strandi573 – 5764Combined sources
Helixi591 – 5933Combined sources
Beta strandi599 – 6013Combined sources
Turni612 – 6176Combined sources
Beta strandi623 – 6253Combined sources
Beta strandi636 – 6394Combined sources
Beta strandi647 – 6493Combined sources
Beta strandi671 – 6733Combined sources
Helixi683 – 6853Combined sources
Helixi686 – 69510Combined sources
Helixi699 – 7013Combined sources
Turni708 – 7125Combined sources
Helixi715 – 7173Combined sources
Turni720 – 7223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W8AX-ray2.80A542-733[»]
ProteinModelPortaliP24014.
SMRiP24014. Positions 73-920, 933-1417.
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.
GeneTreeiENSGT00760000118786.
InParanoidiP24014.
KOiK06839.
PhylomeDBiP24014.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS
60 70 80 90 100
GGLGSVGIHI PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA
110 120 130 140 150
DVERLELQGN NLTVIYETDF QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL
160 170 180 190 200
ERLRLNNNRL KAIPENFVTS SASLLRLDIS NNVITTVGRR VFKGAQSLRS
210 220 230 240 250
LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF GGLGRLRALR
260 270 280 290 300
LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF
310 320 330 340 350
KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE
360 370 380 390 400
LRLEQNFITE LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV
410 420 430 440 450
LYGNKIKDLP SGVFKGLGSL QLLLLNANEI SCIRKDAFRD LHSLSLLSLY
460 470 480 490 500
DNNIQSLANG TFDAMKSIKT VHLAKNPFIC DCNLRWLADY LHKNPIETSG
510 520 530 540 550
ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD SDCPAMCHCE
560 570 580 590 600
GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL
610 620 630 640 650
ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL
660 670 680 690 700
YDNQISCVMP GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG
710 720 730 740 750
AARCGAPSKV RDVQIKDLPH SEFKCSSENS EGCLGDGYCP PSCTCTGTVV
760 770 780 790 800
RCSRNQLKEI PRGIPAETSE LYLESNEIEQ IHYERIRHLR SLTRLDLSNN
810 820 830 840 850
QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL RVLSLHGNRI
860 870 880 890 900
SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA
910 920 930 940 950
EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP
960 970 980 990 1000
QREYQCLCQP GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG
1010 1020 1030 1040 1050
YTGARCETNI DDCLGEIKCQ NNATCIDGVE SYKCECQPGF SGEFCDTKIQ
1060 1070 1080 1090 1100
FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF HGTNCTDNID DCQNHMCQNG
1110 1120 1130 1140 1150
GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ NHECKHGVCF
1160 1170 1180 1190 1200
QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV
1210 1220 1230 1240 1250
TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM
1260 1270 1280 1290 1300
VADGKYHAVE LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL
1310 1320 1330 1340 1350
PVDPAQQAYK NWQIRNLTSF KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA
1360 1370 1380 1390 1400
LLEGEQQEEE DDEQDFMDET PHIKEEPVDP CLENKCRRGS RCVPNSNARD
1410 1420 1430 1440 1450
GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE YYTENDCRSR
1460 1470 1480 1490 1500
QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT

KKCY
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.Curated

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:
EMBLi
GenBanki
DDBJi
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_001103863.3. [P24014-2]
NP_001097334.1. NM_001103864.3. [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:
EMBLi
GenBanki
DDBJi
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_001103863.3. [P24014-2 ]
NP_001097334.1. NM_001103864.3. [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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W8A X-ray 2.80 A 542-733 [» ]
ProteinModelPortali P24014.
SMRi P24014. Positions 73-920, 933-1417.
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 ENSGT00760000118786.
InParanoidi P24014.
KOi K06839.
PhylomeDBi P24014.

Enzyme and pathway databases

Reactomei REACT_236260. Netrin-1 signaling.
REACT_246260. Signaling by Robo receptor.
REACT_246981. Inactivation of Cdc42 and Rac.
REACT_256055. Role of Abl in Robo-Slit signaling.
REACT_263619. Activation of Rac.

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 IPR013320. ConA-like_dom.
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: November 26, 2014
This is version 167 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