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P24014 (SLIT_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein slit

Short name=dSlit

Cleaved into the following 2 chains:

  1. Protein slit N-product
  2. Protein slit C-product
Gene names
Name:sli
ORF Names:CG43758
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.5 Ref.6

Subunit structure

Interacts with robo. Ref.6

Subcellular location

Secreted Ref.1 Ref.5.

Tissue specificity

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. Ref.1 Ref.2 Ref.5

Disruption phenotype

Flies lacking sli exhibit disruption of the developing midline cells and the commissural axon pathways. Ref.5

Sequence similarities

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 7 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 19 LRR (leucine-rich) repeats.

Contains 4 LRRCT domains.

Contains 4 LRRNT domains.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Leucine-rich repeat
Repeat
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRoundabout signaling pathway

Inferred from genetic interaction Ref.2. Source: FlyBase

axon guidance

Inferred from mutant phenotype Ref.2PubMed 11404414PubMed 12040052. Source: FlyBase

axon midline choice point recognition

Inferred from mutant phenotype PubMed 12973825PubMed 15147761PubMed 17049509PubMed 17121810PubMed 17409115. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 18817767. Source: FlyBase

digestive tract mesoderm development

Inferred from mutant phenotype PubMed 21377458. Source: FlyBase

embryonic heart tube development

Inferred from mutant phenotype PubMed 16360689PubMed 16516189PubMed 16888037. Source: FlyBase

epithelial cell migration, open tracheal system

Inferred from mutant phenotype PubMed 15229181. Source: FlyBase

glial cell migration

Inferred from mutant phenotype Ref.1. Source: UniProtKB

gonad development

Inferred from mutant phenotype PubMed 21377458. Source: FlyBase

induction of negative chemotaxis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

mesoderm migration involved in gastrulation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

mesodermal cell migration

Inferred from mutant phenotype Ref.2. Source: FlyBase

neuron differentiation

Inferred from mutant phenotype PubMed 11688564. Source: FlyBase

neuron migration

Inferred from mutant phenotype PubMed 15296748. Source: FlyBase

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 18250318. Source: FlyBase

positive regulation of cell-cell adhesion

Inferred from mutant phenotype PubMed 16888037. Source: FlyBase

regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 12397103. Source: FlyBase

regulation of epithelial cell migration, open tracheal system

Inferred from mutant phenotype PubMed 12397103. Source: FlyBase

salivary gland boundary specification

Inferred from mutant phenotype PubMed 15950216. Source: FlyBase

   Cellular_componentSlit-Robo signaling complex

Inferred from direct assay PubMed 17062560. Source: FlyBase

extracellular matrix

Inferred from direct assay Ref.1. Source: FlyBase

extracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Traceable author statement PubMed 7760738. Source: FlyBase

   Molecular_functionRoundabout binding

Inferred from physical interaction PubMed 17062560. Source: FlyBase

calcium ion binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay PubMed 17062560. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 18359766. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: P24014-1)

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.
Isoform A (identifier: P24014-2)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     152-175: Missing.
Isoform B (identifier: P24014-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636
Chain37 – 15041468Protein slit
PRO_0000007719
Chain37 – 11351099Protein slit N-product By similarity
PRO_0000007720
Chain1136 – 1504369Protein slit C-product By similarity
PRO_0000007721

Regions

Domain64 – 10037LRRNT 1
Repeat101 – 12222LRR 1
Repeat125 – 14622LRR 2
Repeat149 – 17022LRR 3
Repeat173 – 19422LRR 4
Repeat197 – 21822LRR 5
Repeat221 – 24222LRR 6
Domain254 – 30451LRRCT 1
Domain310 – 34637LRRNT 2
Repeat347 – 36822LRR 7
Repeat371 – 39222LRR 8
Repeat395 – 41622LRR 9
Repeat419 – 44022LRR 10
Repeat443 – 46422LRR 11
Domain476 – 52651LRRCT 2
Domain534 – 57037LRRNT 3
Repeat571 – 59222LRR 12
Repeat596 – 61722LRR 13
Repeat620 – 64122LRR 14
Repeat644 – 66522LRR 15
Domain677 – 72751LRRCT 3
Domain730 – 76637LRRNT 4
Repeat767 – 78822LRR 16
Repeat791 – 81222LRR 17
Repeat815 – 83622LRR 18
Repeat839 – 86022LRR 19
Domain872 – 92251LRRCT 4
Domain931 – 96838EGF-like 1
Domain970 – 100738EGF-like 2
Domain1009 – 104638EGF-like 3; calcium-binding Potential
Domain1048 – 108639EGF-like 4
Domain1088 – 112437EGF-like 5; calcium-binding Potential
Domain1135 – 117339EGF-like 6
Domain1176 – 1349174Laminin G-like
Domain1377 – 141640EGF-like 7
Domain1433 – 150472CTCK

Sites

Site1135 – 11362Cleavage By similarity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4591N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential
Glycosylation8121N-linked (GlcNAc...) Potential
Glycosylation9821N-linked (GlcNAc...) Potential
Glycosylation10221N-linked (GlcNAc...) Potential
Glycosylation10841N-linked (GlcNAc...) Potential
Glycosylation11831N-linked (GlcNAc...) Potential
Glycosylation11991N-linked (GlcNAc...) Potential
Glycosylation12671N-linked (GlcNAc...) Potential
Glycosylation13161N-linked (GlcNAc...) Potential
Disulfide bond543 ↔ 549 Ref.7
Disulfide bond547 ↔ 556 Ref.7
Disulfide bond657 ↔ 733 Ref.7
Disulfide bond681 ↔ 704 Ref.7
Disulfide bond683 ↔ 725 Ref.7
Disulfide bond935 ↔ 946 By similarity
Disulfide bond940 ↔ 956 By similarity
Disulfide bond958 ↔ 967 By similarity
Disulfide bond974 ↔ 985 By similarity
Disulfide bond979 ↔ 995 By similarity
Disulfide bond997 ↔ 1006 By similarity
Disulfide bond1013 ↔ 1025 By similarity
Disulfide bond1019 ↔ 1034 By similarity
Disulfide bond1036 ↔ 1045 By similarity
Disulfide bond1052 ↔ 1065 By similarity
Disulfide bond1059 ↔ 1074 By similarity
Disulfide bond1076 ↔ 1085 By similarity
Disulfide bond1092 ↔ 1103 By similarity
Disulfide bond1097 ↔ 1112 By similarity
Disulfide bond1114 ↔ 1123 By similarity
Disulfide bond1139 ↔ 1149 By similarity
Disulfide bond1144 ↔ 1161 By similarity
Disulfide bond1163 ↔ 1172 By similarity
Disulfide bond1323 ↔ 1349 By similarity
Disulfide bond1381 ↔ 1392 By similarity
Disulfide bond1386 ↔ 1404 By similarity
Disulfide bond1406 ↔ 1415 By similarity
Disulfide bond1433 ↔ 1467 By similarity
Disulfide bond1447 ↔ 1481 By similarity
Disulfide bond1458 ↔ 1497 By similarity
Disulfide bond1462 ↔ 1499 By similarity

Natural variations

Alternative sequence152 – 17524Missing in isoform A and isoform B.
VSP_001408
Alternative sequence1418 – 142811Missing in isoform B.
VSP_001409

Experimental info

Sequence conflict350 – 3512EL → DV in CAA37910. Ref.1
Sequence conflict350 – 3512EL → DV in AAD26567. Ref.2
Sequence conflict4211Q → R in CAA37910. Ref.1
Sequence conflict4681I → M in CAA37910. Ref.1
Sequence conflict5271D → G in CAA37910. Ref.1
Sequence conflict5601G → R in CAA37910. Ref.1
Sequence conflict691 – 6922WL → CV in CAA37910. Ref.1
Sequence conflict7511R → A in CAA37910. Ref.1
Sequence conflict8431L → V in CAA37910. Ref.1
Sequence conflict1207 – 12082AE → G in AAA72722. Ref.5
Sequence conflict1429 – 14357AASTCRK → GTYIYHA in AAA72722. Ref.5

Secondary structure

................................ 1504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform C (E) [UniParc].

Last modified February 28, 2003. Version 2.
Checksum: 836A3F5022BF234F

FASTA1,504168,599
        10         20         30         40         50         60 
MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI 

        70         80         90        100        110        120 
PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF 

       130        140        150        160        170        180 
QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLRLNNNRL KAIPENFVTS SASLLRLDIS 

       190        200        210        220        230        240 
NNVITTVGRR VFKGAQSLRS LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF 

       250        260        270        280        290        300 
GGLGRLRALR LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF 

       310        320        330        340        350        360 
KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE LRLEQNFITE 

       370        380        390        400        410        420 
LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV LYGNKIKDLP SGVFKGLGSL 

       430        440        450        460        470        480 
QLLLLNANEI SCIRKDAFRD LHSLSLLSLY DNNIQSLANG TFDAMKSIKT VHLAKNPFIC 

       490        500        510        520        530        540 
DCNLRWLADY LHKNPIETSG ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD 

       550        560        570        580        590        600 
SDCPAMCHCE GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL 

       610        620        630        640        650        660 
ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL YDNQISCVMP 

       670        680        690        700        710        720 
GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG AARCGAPSKV RDVQIKDLPH 

       730        740        750        760        770        780 
SEFKCSSENS EGCLGDGYCP PSCTCTGTVV RCSRNQLKEI PRGIPAETSE LYLESNEIEQ 

       790        800        810        820        830        840 
IHYERIRHLR SLTRLDLSNN QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL 

       850        860        870        880        890        900 
RVLSLHGNRI SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA 

       910        920        930        940        950        960 
EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP QREYQCLCQP 

       970        980        990       1000       1010       1020 
GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG YTGARCETNI DDCLGEIKCQ 

      1030       1040       1050       1060       1070       1080 
NNATCIDGVE SYKCECQPGF SGEFCDTKIQ FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF 

      1090       1100       1110       1120       1130       1140 
HGTNCTDNID DCQNHMCQNG GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ 

      1150       1160       1170       1180       1190       1200 
NHECKHGVCF QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV 

      1210       1220       1230       1240       1250       1260 
TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM VADGKYHAVE 

      1270       1280       1290       1300       1310       1320 
LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL PVDPAQQAYK NWQIRNLTSF 

      1330       1340       1350       1360       1370       1380 
KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA LLEGEQQEEE DDEQDFMDET PHIKEEPVDP 

      1390       1400       1410       1420       1430       1440 
CLENKCRRGS RCVPNSNARD GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE 

      1450       1460       1470       1480       1490       1500 
YYTENDCRSR QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT 


KKCY 

« Hide

Isoform A (D) [UniParc].

Checksum: F456BC617D8453ED
Show »

FASTA1,480165,890
Isoform B [UniParc].

Checksum: 14DBA99CE1DAEAC4
Show »

FASTA1,469164,834

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA36665.
B36665.
RefSeqNP_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]
UniGeneDm.4729.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W8AX-ray2.80A542-733[»]
ProteinModelPortalP24014.
SMRP24014. Positions 73-921, 933-1433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62473. 14 interactions.
IntActP24014. 3 interactions.

Proteomic databases

PaxDbP24014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0330731; FBpp0303575; FBgn0264089. [P24014-1]
FBtr0330733; FBpp0303577; FBgn0264089. [P24014-1]
GeneID36746.
KEGGdme:Dmel_CG43758.

Organism-specific databases

CTD36746.
FlyBaseFBgn0264089. sli.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00750000117236.
InParanoidP24014.
KOK06839.
PhylomeDBP24014.

Enzyme and pathway databases

ReactomeREACT_227403. Developmental Biology.

Gene expression databases

BgeeP24014.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. 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]
PfamPF00008. 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]
SMARTSM00041. 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]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP24014.
GenomeRNAi36746.
NextBio800151.

Entry information

Entry nameSLIT_DROME
AccessionPrimary (citable) accession number: P24014
Secondary accession number(s): A8DYF5 expand/collapse secondary AC list , A8DYF6, Q24526, Q8MLB9, Q9V7F8, Q9V7F9, Q9XYV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 28, 2003
Last modified: July 9, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase