Q80TR4 · SLIT1_MOUSE
- ProteinSlit homolog 1 protein
- GeneSlit1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1531 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
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
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSlit homolog 1 protein
- Short namesSlit-1
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80TR4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
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).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 68 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MALTPQRGSSSGLSRPELWLLLWAAAWRLGATA | ||||||
Chain | PRO_0000007723 | 34-1531 | Slit homolog 1 protein | |||
Sequence: CPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLQVLPELLFQNNQALSRLDLSENFLQAVPRKAFRGATDLKNLQLDKNRISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKGEFSCSGQGEAAGAPACTLSSGSCPAMCSCSSGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYHLNSECTSDVACPHKCRCEASVVECSSLKLSKIPERIPQSTTELRLNNNEISILEATGLFKKLSHLKKINLSNNKVSEIEDGTFEGAASVSELHLTANQLESIRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNHITTISPGAFDTLQALSTLNLLANPFNCNCHLSWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDVSTLQEGIFADVTSLSHLAIGANPLYCDCRLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQGPPSLAVQAKCDPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRHCEVSLDGCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGPTCGVDTDDCVKHACVNGGVCVDGVGNYTCQCPLQYTGRACEQLVDFCSPDMNPCQHEAQCVGTPDGPRCECMLGYTGDNCSENQDDCKDHKCQNGAQCVDEVNSYACLCVEGYSGQLCEIPPAPRSSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCDQPVDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCNQVGAVAEPCGGLQCLHGHCQASATKGAHCVCSPGFSGELCEQESECRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAQCA | ||||||
Glycosylation | 72 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 192 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 286↔295 | |||||
Sequence: CSCSSGIVDC | ||||||
Glycosylation | 406 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 443↔466 | |||||
Sequence: CDCNLKWLADFLRTNPIETTGARC | ||||||
Disulfide bond | 445↔487 | |||||
Sequence: CNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRC | ||||||
Disulfide bond | 513↔519 | |||||
Sequence: CPHKCRC | ||||||
Disulfide bond | 517↔526 | |||||
Sequence: CRCEASVVEC | ||||||
Glycosylation | 571 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 630 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 675↔698 | |||||
Sequence: CNCHLSWLGDWLRKRKIVTGNPRC | ||||||
Disulfide bond | 677↔719 | |||||
Sequence: CHLSWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRC | ||||||
Glycosylation | 762 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 801 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 806 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 929↔940 | |||||
Sequence: CLSSPCQNQGTC | ||||||
Disulfide bond | 934↔950 | |||||
Sequence: CQNQGTCHNDPLEVYRC | ||||||
Disulfide bond | 952↔961 | |||||
Sequence: CPSGYKGRHC | ||||||
Disulfide bond | 968↔979 | |||||
Sequence: CSSNPCGNGGTC | ||||||
Disulfide bond | 973↔991 | |||||
Sequence: CGNGGTCHAQEGEDAGFTC | ||||||
Disulfide bond | 993↔1002 | |||||
Sequence: CPSGFEGPTC | ||||||
Disulfide bond | 1009↔1020 | |||||
Sequence: CVKHACVNGGVC | ||||||
Disulfide bond | 1014↔1029 | |||||
Sequence: CVNGGVCVDGVGNYTC | ||||||
Glycosylation | 1026 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1031↔1040 | |||||
Sequence: CPLQYTGRAC | ||||||
Disulfide bond | 1047↔1060 | |||||
Sequence: CSPDMNPCQHEAQC | ||||||
Disulfide bond | 1054↔1069 | |||||
Sequence: CQHEAQCVGTPDGPRC | ||||||
Disulfide bond | 1071↔1080 | |||||
Sequence: CMLGYTGDNC | ||||||
Glycosylation | 1079 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1087↔1098 | |||||
Sequence: CKDHKCQNGAQC | ||||||
Disulfide bond | 1092↔1107 | |||||
Sequence: CQNGAQCVDEVNSYAC | ||||||
Disulfide bond | 1109↔1118 | |||||
Sequence: CVEGYSGQLC | ||||||
Disulfide bond | 1128↔1139 | |||||
Sequence: CEGTECQNGANC | ||||||
Disulfide bond | 1133↔1148 | |||||
Sequence: CQNGANCVDQGSRPVC | ||||||
Disulfide bond | 1150↔1159 | |||||
Sequence: CLPGFGGPEC | ||||||
Glycosylation | 1186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1303 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1310↔1336 | |||||
Sequence: CIRNLYINNELQDFTKTQMKPGVVPGC | ||||||
Disulfide bond | 1339↔1349 | |||||
Sequence: CRKLYCLHGIC | ||||||
Disulfide bond | 1344↔1359 | |||||
Sequence: CLHGICQPNATPGPVC | ||||||
Disulfide bond | 1361↔1370 | |||||
Sequence: CEAGWGGLHC | ||||||
Disulfide bond | 1378↔1388 | |||||
Sequence: CHGHKCVHGKC | ||||||
Disulfide bond | 1383↔1398 | |||||
Sequence: CVHGKCVPLDALAYSC | ||||||
Disulfide bond | 1400↔1409 | |||||
Sequence: CQDGYSGALC | ||||||
Disulfide bond | 1419↔1429 | |||||
Sequence: CGGLQCLHGHC | ||||||
Disulfide bond | 1424↔1439 | |||||
Sequence: CLHGHCQASATKGAHC | ||||||
Disulfide bond | 1441↔1450 | |||||
Sequence: CSPGFSGELC | ||||||
Disulfide bond | 1456↔1495 | |||||
Sequence: CRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCC | ||||||
Disulfide bond | 1474↔1509 | |||||
Sequence: CQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFEC | ||||||
Disulfide bond | 1485↔1525 | |||||
Sequence: CRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKC | ||||||
Disulfide bond | 1489↔1527 | |||||
Sequence: CPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
During retinal development, is expressed at 12.5 dpc in the dorsocentral region of the retina, and at 17.5 dpc is only very weakly expressed. In the developing optic chiasm is expressed at 12.5 dpc 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 17.5 dpc 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 8.5 dpc and 9.5 dpc in the primordiun of the branchial arches, between 9.5 dpc and 10.5 dpc in the posterior dermamyotome. By 11.5 dpc the expression pattern along somite boundaries was most prominent caudally. Weak expression was also observed in the nasal pit at 11.5 dpc. From 13.5 dpc to 17.5 dpc 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).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-61 | LRRNT | ||||
Sequence: CPALCTCTGTTVDCHGTGLQAIPKNIPR | ||||||
Repeat | 62-83 | LRR 1 | ||||
Sequence: NTERLELNGNNITRIHKNDFAG | ||||||
Repeat | 86-107 | LRR 2 | ||||
Sequence: QLRVLQLMENQIGAVERGAFDD | ||||||
Repeat | 110-131 | LRR 3 | ||||
Sequence: ELERLRLNRNQLQVLPELLFQN | ||||||
Repeat | 134-155 | LRR 4 | ||||
Sequence: ALSRLDLSENFLQAVPRKAFRG | ||||||
Repeat | 158-179 | LRR 5 | ||||
Sequence: DLKNLQLDKNRISCIEEGAFRA | ||||||
Repeat | 182-203 | LRR 6 | ||||
Sequence: GLEVLTLNNNNITTIPVSSFNH | ||||||
Domain | 215-265 | LRRCT 1 | ||||
Sequence: NHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKGEFSCSG | ||||||
Domain | 273-309 | LRRNT 23 | ||||
Sequence: PACTLSSGSCPAMCSCSSGIVDCRGKGLTAIPANLPE | ||||||
Repeat | 310-331 | LRR 7 | ||||
Sequence: TMTEIRLELNGIKSIPPGAFSP | ||||||
Repeat | 334-355 | LRR 8 | ||||
Sequence: KLRRIDLSNNQIAEIAPDAFQG | ||||||
Repeat | 358-379 | LRR 9 | ||||
Sequence: SLNSLVLYGNKITDLPRGVFGG | ||||||
Repeat | 382-403 | LRR 10 | ||||
Sequence: TLQLLLLNANKINCIRPDAFQD | ||||||
Repeat | 406-427 | LRR 11 | ||||
Sequence: NLSLLSLYDNKIQSLAKGTFTS | ||||||
Domain | 439-489 | LRRCT 2 | ||||
Sequence: NPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSA | ||||||
Domain | 504-540 | LRRNT 3 | ||||
Sequence: NSECTSDVACPHKCRCEASVVECSSLKLSKIPERIPQ | ||||||
Repeat | 541-562 | LRR 12 | ||||
Sequence: STTELRLNNNEISILEATGLFK | ||||||
Repeat | 566-587 | LRR 13 | ||||
Sequence: HLKKINLSNNKVSEIEDGTFEG | ||||||
Repeat | 590-611 | LRR 14 | ||||
Sequence: SVSELHLTANQLESIRSGMFRG | ||||||
Repeat | 614-635 | LRR 15 | ||||
Sequence: GLRTLMLRNNRISCIHNDSFTG | ||||||
Repeat | 638-659 | LRR 16 | ||||
Sequence: NVRLLSLYDNHITTISPGAFDT | ||||||
Domain | 671-721 | LRRCT 3 | ||||
Sequence: NPFNCNCHLSWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEE | ||||||
Domain | 725-761 | LRRNT 4 | ||||
Sequence: EVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPK | ||||||
Repeat | 762-783 | LRR 17 | ||||
Sequence: NVTELYLDGNQFTLVPGQLSTF | ||||||
Repeat | 785-806 | LRR 18 | ||||
Sequence: YLQLVDLSNNKISSLSNSSFTN | ||||||
Repeat | 809-830 | LRR 19 | ||||
Sequence: QLTTLILSYNALQCIPPLAFQG | ||||||
Repeat | 833-854 | LRR 20 | ||||
Sequence: SLRLLSLHGNDVSTLQEGIFAD | ||||||
Domain | 866-916 | LRRCT 4 | ||||
Sequence: NPLYCDCRLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQG | ||||||
Domain | 927-962 | EGF-like 1 | ||||
Sequence: DPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRHCE | ||||||
Domain | 964-1003 | EGF-like 2 | ||||
Sequence: SLDGCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGPTCG | ||||||
Domain | 1005-1041 | EGF-like 3 | ||||
Sequence: DTDDCVKHACVNGGVCVDGVGNYTCQCPLQYTGRACE | ||||||
Domain | 1043-1081 | EGF-like 4 | ||||
Sequence: LVDFCSPDMNPCQHEAQCVGTPDGPRCECMLGYTGDNCS | ||||||
Domain | 1083-1119 | EGF-like 5 | ||||
Sequence: NQDDCKDHKCQNGAQCVDEVNSYACLCVEGYSGQLCE | ||||||
Domain | 1124-1160 | EGF-like 6 | ||||
Sequence: PRSSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECE | ||||||
Domain | 1163-1336 | Laminin G-like | ||||
Sequence: LSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGC | ||||||
Domain | 1337-1371 | EGF-like 7 | ||||
Sequence: EPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCD | ||||||
Domain | 1374-1410 | EGF-like 8 | ||||
Sequence: VDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCN | ||||||
Domain | 1415-1451 | EGF-like 9 | ||||
Sequence: VAEPCGGLQCLHGHCQASATKGAHCVCSPGFSGELCE | ||||||
Domain | 1456-1531 | CTCK | ||||
Sequence: CRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAQCA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,531
- Mass (Da)167,420
- Last updated2004-03-15 v2
- ChecksumC0F1C5A4E3DF6108
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 44 | in Ref. 3; AAH57131/AAH62091 | ||||
Sequence: Missing | ||||||
Sequence conflict | 830 | in Ref. 1; AAD44758 | ||||
Sequence: G → R | ||||||
Sequence conflict | 1531 | in Ref. 1; AAD44758 and 2; BAC65658 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF144627 EMBL· GenBank· DDBJ | AAD44758.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122376 EMBL· GenBank· DDBJ | BAC65658.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC057131 EMBL· GenBank· DDBJ | AAH57131.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062091 EMBL· GenBank· DDBJ | AAH62091.1 EMBL· GenBank· DDBJ | mRNA |