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Q80TR4 (SLIT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Slit homolog 1 protein

Short name=Slit-1
Gene names
Name:Slit1
Synonyms:Kiaa0813
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions By similarity. SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. Ref.4 Ref.5

Subunit structure

Interacts with GREM1 By similarity and ROBO1. Ref.1

Subcellular location

Secreted By similarity.

Developmental stage

During retinal development, is expressed at E12.5 in the dorsocentral region of the retina, and at E17.5 is only very weakly expressed. In the developing optic chiasm is expressed at E12.5 around the junction of the optic nerve and the brain, with strongest expression dorsal to the site at which the optic stalk joins the diencephalon, and also weakly in a subset of the CD44/SSEA neurons. In the more dorsal region of the developing optic chiasm, is expressed in some distance posterior to the axons. However, more ventrally, is expressed in a region directly adjacent to the path taken by the RGC axons. By E17.5 is not longer be detected at the junction of the brain and optic nerve and is only weakly expressed by the CD44/SSEA neurons. Outside the developing brain detected at between E8.5 and E9.5 in the primordiun of the branchial arches, between E9.5 and 10.5 in the posterior dermamyotome. By E11.5 the expression pattern along somite boundaries was most prominent caudally. Weak expression was also observed in the nasal pit at E11.5. From E13.5 to E17.5 expression was observed in the trigeminal ganglion, in the olfactory epithelium, and in the neural layer of the retina in the developing eye (with strongest expression in the inner nuclear layer). Ref.1 Ref.6

Disruption phenotype

Mice show significant axon guidance errors in a variety of pathways, including corticofugal, callosal and thalamocortical tracts. Mice double-deficient in SLIT1 and SLIT2 show retinal axon guidance defects and a disorganized lateral olfactory tract (LOT). Ref.4

Sequence similarities

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

Contains 9 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 20 LRR (leucine-rich) repeats.

Contains 4 LRRCT domains.

Contains 4 LRRNT domains.

Sequence caution

The sequence BAC65658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentSecreted
   DomainEGF-like domain
Leucine-rich repeat
Repeat
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension involved in axon guidance

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from direct assay PubMed 12954717. Source: MGI

axonogenesis

Inferred from direct assay Ref.4. Source: MGI

dorsal/ventral axon guidance

Inferred from genetic interaction Ref.5. Source: MGI

establishment of nucleus localization

Inferred from direct assay PubMed 12051827. Source: MGI

motor neuron axon guidance

Inferred from electronic annotation. Source: Ensembl

negative chemotaxis

Inferred from mutant phenotype Ref.4. Source: MGI

negative regulation of axon extension involved in axon guidance

Inferred from electronic annotation. Source: Ensembl

negative regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection morphogenesis

Inferred from genetic interaction Ref.5. Source: MGI

olfactory bulb development

Inferred from genetic interaction Ref.4. Source: MGI

retinal ganglion cell axon guidance

Inferred from mutant phenotype PubMed 16828733PubMed 16885222. Source: MGI

spinal cord development

Inferred from electronic annotation. Source: Ensembl

tangential migration from the subventricular zone to the olfactory bulb

Inferred from mutant phenotype PubMed 14960623. Source: MGI

telencephalon cell migration

Inferred from genetic interaction PubMed 14960623. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 12954717. Source: MGI

   Molecular_functionRoundabout binding

Inferred from physical interaction Ref.1. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: InterPro

receptor binding

Traceable author statement PubMed 12954717. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 15311498Slit homolog 1 protein
PRO_0000007723

Regions

Domain34 – 6128LRRNT
Repeat62 – 8322LRR 1
Repeat86 – 10722LRR 2
Repeat110 – 13122LRR 3
Repeat134 – 15522LRR 4
Repeat158 – 17922LRR 5
Repeat182 – 20322LRR 6
Domain215 – 26551LRRCT 1
Domain273 – 30937LRRNT 23
Repeat310 – 33122LRR 7
Repeat334 – 35522LRR 8
Repeat358 – 37922LRR 9
Repeat382 – 40322LRR 10
Repeat406 – 42722LRR 11
Domain439 – 48951LRRCT 2
Domain504 – 54037LRRNT 3
Repeat541 – 56222LRR 12
Repeat566 – 58722LRR 13
Repeat590 – 61122LRR 14
Repeat614 – 63522LRR 15
Repeat638 – 65922LRR 16
Domain671 – 72151LRRCT 3
Domain725 – 76137LRRNT 4
Repeat762 – 78322LRR 17
Repeat785 – 80622LRR 18
Repeat809 – 83022LRR 19
Repeat833 – 85422LRR 20
Domain866 – 91651LRRCT 4
Domain927 – 96236EGF-like 1
Domain964 – 100340EGF-like 2
Domain1005 – 104137EGF-like 3
Domain1043 – 108139EGF-like 4
Domain1083 – 111937EGF-like 5
Domain1124 – 116037EGF-like 6
Domain1163 – 1336174Laminin G-like
Domain1337 – 137135EGF-like 7
Domain1374 – 141037EGF-like 8
Domain1415 – 145137EGF-like 9
Domain1456 – 153176CTCK

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation6301N-linked (GlcNAc...) Potential
Glycosylation7621N-linked (GlcNAc...) Potential
Glycosylation8011N-linked (GlcNAc...) Potential
Glycosylation8061N-linked (GlcNAc...) Potential
Glycosylation10261N-linked (GlcNAc...) Potential
Glycosylation10791N-linked (GlcNAc...) Potential
Glycosylation11861N-linked (GlcNAc...) Potential
Glycosylation12561N-linked (GlcNAc...) Potential
Glycosylation13031N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 295 By similarity
Disulfide bond443 ↔ 466 By similarity
Disulfide bond445 ↔ 487 By similarity
Disulfide bond513 ↔ 519 By similarity
Disulfide bond517 ↔ 526 By similarity
Disulfide bond675 ↔ 698 By similarity
Disulfide bond677 ↔ 719 By similarity
Disulfide bond929 ↔ 940 By similarity
Disulfide bond934 ↔ 950 By similarity
Disulfide bond952 ↔ 961 By similarity
Disulfide bond968 ↔ 979 By similarity
Disulfide bond973 ↔ 991 By similarity
Disulfide bond993 ↔ 1002 By similarity
Disulfide bond1009 ↔ 1020 By similarity
Disulfide bond1014 ↔ 1029 By similarity
Disulfide bond1031 ↔ 1040 By similarity
Disulfide bond1047 ↔ 1060 By similarity
Disulfide bond1054 ↔ 1069 By similarity
Disulfide bond1071 ↔ 1080 By similarity
Disulfide bond1087 ↔ 1098 By similarity
Disulfide bond1092 ↔ 1107 By similarity
Disulfide bond1109 ↔ 1118 By similarity
Disulfide bond1128 ↔ 1139 By similarity
Disulfide bond1133 ↔ 1148 By similarity
Disulfide bond1150 ↔ 1159 By similarity
Disulfide bond1310 ↔ 1336 By similarity
Disulfide bond1339 ↔ 1349 By similarity
Disulfide bond1344 ↔ 1359 By similarity
Disulfide bond1361 ↔ 1370 By similarity
Disulfide bond1378 ↔ 1388 By similarity
Disulfide bond1383 ↔ 1398 By similarity
Disulfide bond1400 ↔ 1409 By similarity
Disulfide bond1419 ↔ 1429 By similarity
Disulfide bond1424 ↔ 1439 By similarity
Disulfide bond1441 ↔ 1450 By similarity
Disulfide bond1456 ↔ 1495 By similarity
Disulfide bond1474 ↔ 1509 By similarity
Disulfide bond1485 ↔ 1525 By similarity
Disulfide bond1489 ↔ 1527 By similarity

Experimental info

Sequence conflict441Missing in AAH57131. Ref.3
Sequence conflict441Missing in AAH62091. Ref.3
Sequence conflict8301G → R in AAD44758. Ref.1
Sequence conflict15311A → V in AAD44758. Ref.1
Sequence conflict15311A → V in BAC65658. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q80TR4 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: C0F1C5A4E3DF6108

FASTA1,531167,420
        10         20         30         40         50         60 
MALTPQRGSS SGLSRPELWL LLWAAAWRLG ATACPALCTC TGTTVDCHGT GLQAIPKNIP 

        70         80         90        100        110        120 
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ 

       130        140        150        160        170        180 
LQVLPELLFQ NNQALSRLDL SENFLQAVPR KAFRGATDLK NLQLDKNRIS CIEEGAFRAL 

       190        200        210        220        230        240 
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT 

       250        260        270        280        290        300 
QCSGPASLRG LNVAEVQKGE FSCSGQGEAA GAPACTLSSG SCPAMCSCSS GIVDCRGKGL 

       310        320        330        340        350        360 
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN 

       370        380        390        400        410        420 
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL 

       430        440        450        460        470        480 
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TTGARCASPR RLANKRIGQI 

       490        500        510        520        530        540 
KSKKFRCSAK EQYFIPGTED YHLNSECTSD VACPHKCRCE ASVVECSSLK LSKIPERIPQ 

       550        560        570        580        590        600 
STTELRLNNN EISILEATGL FKKLSHLKKI NLSNNKVSEI EDGTFEGAAS VSELHLTANQ 

       610        620        630        640        650        660 
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNHIT TISPGAFDTL 

       670        680        690        700        710        720 
QALSTLNLLA NPFNCNCHLS WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE 

       730        740        750        760        770        780 
EGQEEVGCLP RPQCPQECAC LDTVVRCSNK HLQALPKGIP KNVTELYLDG NQFTLVPGQL 

       790        800        810        820        830        840 
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH 

       850        860        870        880        890        900 
GNDVSTLQEG IFADVTSLSH LAIGANPLYC DCRLRWLSSW VKTGYKEPGI ARCAGPPEME 

       910        920        930        940        950        960 
GKLLLTTPAK KFECQGPPSL AVQAKCDPCL SSPCQNQGTC HNDPLEVYRC TCPSGYKGRH 

       970        980        990       1000       1010       1020 
CEVSLDGCSS NPCGNGGTCH AQEGEDAGFT CSCPSGFEGP TCGVDTDDCV KHACVNGGVC 

      1030       1040       1050       1060       1070       1080 
VDGVGNYTCQ CPLQYTGRAC EQLVDFCSPD MNPCQHEAQC VGTPDGPRCE CMLGYTGDNC 

      1090       1100       1110       1120       1130       1140 
SENQDDCKDH KCQNGAQCVD EVNSYACLCV EGYSGQLCEI PPAPRSSCEG TECQNGANCV 

      1150       1160       1170       1180       1190       1200 
DQGSRPVCQC LPGFGGPECE KLLSVNFVDR DTYLQFTDLQ NWPRANITLQ VSTAEDNGIL 

      1210       1220       1230       1240       1250       1260 
LYNGDNDHIA VELYQGHVRV SYDPGSYPSS AIYSAETIND GQFHTVELVT FDQMVNLSID 

      1270       1280       1290       1300       1310       1320 
GGSPMTMDNF GKHYTLNSEA PLYVGGMPVD VNSAAFRLWQ ILNGTSFHGC IRNLYINNEL 

      1330       1340       1350       1360       1370       1380 
QDFTKTQMKP GVVPGCEPCR KLYCLHGICQ PNATPGPVCH CEAGWGGLHC DQPVDGPCHG 

      1390       1400       1410       1420       1430       1440 
HKCVHGKCVP LDALAYSCQC QDGYSGALCN QVGAVAEPCG GLQCLHGHCQ ASATKGAHCV 

      1450       1460       1470       1480       1490       1500 
CSPGFSGELC EQESECRGDP VRDFHRVQRG YAICQTTRPL SWVECRGACP GQGCCQGLRL 

      1510       1520       1530 
KRRKLTFECS DGTSFAEEVE KPTKCGCAQC A 

« Hide

References

« Hide 'large scale' references
[1]"The mouse SLIT family: secreted ligands for ROBO expressed in patterns that suggest a role in morphogenesis and axon guidance."
Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.
Dev. Biol. 212:290-306(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ROBO1, DEVELOPMENTAL STAGE.
Strain: ICR X Swiss Webster.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Slit1 and slit2 proteins control the development of the lateral olfactory tract."
Nguyen-Ba-Charvet K.T., Plump A.S., Tessier-Lavigne M., Chedotal A.
J. Neurosci. 22:5473-5480(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"Slit proteins prevent midline crossing and determine the dorsoventral position of major axonal pathways in the mammalian forebrain."
Bagri A., Marin O., Plump A.S., Mak J., Pleasure S.J., Rubenstein J.L., Tessier-Lavigne M.
Neuron 33:233-248(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Retinal ganglion cell axon guidance in the mouse optic chiasm: expression and function of robos and slits."
Erskine L., Williams S.E., Brose K., Kidd T., Rachel R.A., Goodman C.S., Tessier-Lavigne M., Mason C.A.
J. Neurosci. 20:4975-4982(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144627 mRNA. Translation: AAD44758.1.
AK122376 mRNA. Translation: BAC65658.1. Different initiation.
BC057131 mRNA. Translation: AAH57131.1.
BC062091 mRNA. Translation: AAH62091.1.
CCDSCCDS29812.1.
RefSeqNP_056563.2. NM_015748.3.
UniGeneMm.40322.

3D structure databases

ProteinModelPortalQ80TR4.
SMRQ80TR4. Positions 30-1451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203327. 1 interaction.
STRING10090.ENSMUSP00000025993.

PTM databases

PhosphoSiteQ80TR4.

Proteomic databases

PaxDbQ80TR4.
PRIDEQ80TR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025993; ENSMUSP00000025993; ENSMUSG00000025020.
GeneID20562.
KEGGmmu:20562.
UCSCuc008hmf.2. mouse.

Organism-specific databases

CTD6585.
MGIMGI:1315203. Slit1.
RougeSearch...

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00750000117236.
HOGENOMHOG000116120.
HOVERGENHBG057959.
InParanoidQ80TR4.
KOK06838.
OMAKCVHGKC.
PhylomeDBQ80TR4.
TreeFamTF332887.

Gene expression databases

BgeeQ80TR4.
CleanExMM_SLIT1.
GenevestigatorQ80TR4.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
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.
IPR003645. Fol_N.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00008. EGF. 4 hits.
PF12661. hEGF. 2 hits.
PF02210. Laminin_G_2. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 5 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
SMARTSM00041. CT. 1 hit.
SM00181. EGF. 7 hits.
SM00179. EGF_CA. 2 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 10 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 9 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 21 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio298853.
PROQ80TR4.
SOURCESearch...

Entry information

Entry nameSLIT1_MOUSE
AccessionPrimary (citable) accession number: Q80TR4
Secondary accession number(s): Q9WVB5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot