GenomeNet

Database: UniProt
Entry: O94813
LinkDB: O94813
Original site: O94813 
ID   SLIT2_HUMAN             Reviewed;        1529 AA.
AC   O94813; A0A0A6YYB8; B7ZLR5; O95710; Q17RU3; Q9Y5Q7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   13-FEB-2019, entry version 191.
DE   RecName: Full=Slit homolog 2 protein;
DE            Short=Slit-2;
DE   Contains:
DE     RecName: Full=Slit homolog 2 protein N-product;
DE   Contains:
DE     RecName: Full=Slit homolog 2 protein C-product;
DE   Flags: Precursor;
GN   Name=SLIT2; Synonyms=SLIL3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000312|EMBL:BAA35185.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   VARIANTS PRO-636 AND PHE-1277.
RC   TISSUE=Fetal lung;
RX   PubMed=9813312; DOI=10.1016/S0169-328X(98)00224-1;
RA   Itoh A., Miyabayashi T., Ohno M., Sakano S.;
RT   "Cloning and expressions of three mammalian homologues of Drosophila
RT   slit suggest possible roles for Slit in the formation and maintenance
RT   of the nervous system.";
RL   Brain Res. Mol. Brain Res. 62:175-186(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain, and Fetal kidney;
RX   PubMed=10349621; DOI=10.1016/S0925-4773(98)00174-9;
RA   Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
RA   Little M.H.;
RT   "Distinct but overlapping expression patterns of two vertebrate slit
RT   homologs implies functional roles in CNS development and
RT   organogenesis.";
RL   Mech. Dev. 79:57-72(1998).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1122-1129,
RP   FUNCTION, INTERACTION WITH ROBO1 AND ROBO2, AND SUBCELLULAR LOCATION.
RC   TISSUE=Fetal brain;
RX   PubMed=10102268; DOI=10.1016/S0092-8674(00)80590-5;
RA   Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA   Tessier-Lavigne M., Kidd T.;
RT   "Slit proteins bind Robo receptors and have an evolutionarily
RT   conserved role in repulsive axon guidance.";
RL   Cell 96:795-806(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=10975526; DOI=10.1016/S0092-8674(00)00041-6;
RA   Zou Y., Stoeckli E., Chen H., Tessier-Lavigne M.;
RT   "Squeezing axons out of the gray matter: a role for slit and
RT   semaphorin proteins from midline and ventral spinal cord.";
RL   Cell 102:363-375(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=10864954;
RA   Niclou S.P., Jia L., Raper J.A.;
RT   "Slit2 is a repellent for retinal ganglion cell axons.";
RL   J. Neurosci. 20:4962-4974(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=11309622; DOI=10.1038/35073616;
RA   Wu J.Y., Feng L., Park H.T., Havlioglu N., Wen L., Tang H.,
RA   Bacon K.B., Jiang Z.H., Zhang X.C., Rao Y.;
RT   "The neuronal repellent Slit inhibits leukocyte chemotaxis induced by
RT   chemotactic factors.";
RL   Nature 410:948-952(2001).
RN   [10]
RP   DOMAIN.
RX   PubMed=11222645;
RA   Chen J.H., Wen L., Dupuis S., Wu J.Y., Rao Y.;
RT   "The N-terminal leucine-rich regions in Slit are sufficient to repel
RT   olfactory bulb axons and subventricular zone neurons.";
RL   J. Neurosci. 21:1548-1556(2001).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH ROBO1 AND ROBO2.
RX   PubMed=11404413;
RA   Nguyen-Ba-Charvet K.T., Brose K., Ma L., Wang K.H., Marillat V.,
RA   Sotelo C., Tessier-Lavigne M., Chedotal A.;
RT   "Diversity and specificity of actions of Slit2 proteolytic fragments
RT   in axon guidance.";
RL   J. Neurosci. 21:4281-4289(2001).
RN   [12]
RP   FUNCTION.
RX   PubMed=11239147; DOI=10.1126/science.1058445;
RA   Stein E., Tessier-Lavigne M.;
RT   "Hierarchical organization of guidance receptors: silencing of netrin
RT   attraction by slit through a Robo/DCC receptor complex.";
RL   Science 291:1928-1938(2001).
RN   [13]
RP   REVIEW.
RX   PubMed=12200164; DOI=10.1016/S0959-437X(02)00343-X;
RA   Wong K., Park H.T., Wu J.Y., Rao Y.;
RT   "Slit proteins: molecular guidance cues for cells ranging from neurons
RT   to leukocytes.";
RL   Curr. Opin. Genet. Dev. 12:583-591(2002).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 504-716, AND DISULFIDE
RP   BONDS.
RX   PubMed=17704564; DOI=10.1107/S0907444907035470;
RA   Morlot C., Hemrika W., Romijn R.A., Gros P., Cusack S., McCarthy A.A.;
RT   "Production of Slit2 LRR domains in mammalian cells for structural
RT   studies and the structure of human Slit2 domain 3.";
RL   Acta Crystallogr. D 63:961-968(2007).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-480 IN COMPLEX WITH
RP   ROBO1, AND DISULFIDE BONDS.
RX   PubMed=17848514; DOI=10.1073/pnas.0705310104;
RA   Morlot C., Thielens N.M., Ravelli R.B., Hemrika W., Romijn R.A.,
RA   Gros P., Cusack S., McCarthy A.A.;
RT   "Structural insights into the Slit-Robo complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14923-14928(2007).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 726-907, SUBUNIT, DISULFIDE
RP   BONDS, AND HEPARIN-BINDING.
RX   PubMed=19498462; DOI=10.1038/embor.2009.95;
RA   Seiradake E., von Philipsborn A.C., Henry M., Fritz M.,
RA   Lortat-Jacob H., Jamin M., Hemrika W., Bastmeyer M., Cusack S.,
RA   McCarthy A.A.;
RT   "Structure and functional relevance of the Slit2 homodimerization
RT   domain.";
RL   EMBO Rep. 10:736-741(2009).
CC   -!- FUNCTION: Thought to act as molecular guidance cue in cellular
CC       migration, and function appears to be mediated by interaction with
CC       roundabout homolog receptors. During neural development involved
CC       in axonal navigation at the ventral midline of the neural tube and
CC       projection of axons to different regions. SLIT1 and SLIT2 seem to
CC       be essential for midline guidance in the forebrain by acting as
CC       repulsive signal preventing inappropriate midline crossing by
CC       axons projecting from the olfactory bulb. In spinal chord
CC       development may play a role in guiding commissural axons once they
CC       reached the floor plate by modulating the response to netrin. In
CC       vitro, silences the attractive effect of NTN1 but not its growth-
CC       stimulatory effect and silencing requires the formation of a
CC       ROBO1-DCC complex. May be implicated in spinal chord midline post-
CC       crossing axon repulsion. In vitro, only commissural axons that
CC       crossed the midline responded to SLIT2. In the developing visual
CC       system appears to function as repellent for retinal ganglion axons
CC       by providing a repulsion that directs these axons along their
CC       appropriate paths prior to, and after passage through, the optic
CC       chiasm. In vitro, collapses and repels retinal ganglion cell
CC       growth cones. Seems to play a role in branching and arborization
CC       of CNS sensory axons, and in neuronal cell migration. In vitro,
CC       Slit homolog 2 protein N-product, but not Slit homolog 2 protein
CC       C-product, repels olfactory bulb (OB) but not dorsal root ganglia
CC       (DRG) axons, induces OB growth cones collapse and induces
CC       branching of DRG axons. Seems to be involved in regulating
CC       leukocyte migration. {ECO:0000269|PubMed:10102268,
CC       ECO:0000269|PubMed:10864954, ECO:0000269|PubMed:10975526,
CC       ECO:0000269|PubMed:11239147, ECO:0000269|PubMed:11309622,
CC       ECO:0000269|PubMed:11404413}.
CC   -!- SUBUNIT: Interacts with GREM1 (By similarity). Homodimer. Binds
CC       ROBO1 and ROBO2 with high affinity. {ECO:0000250,
CC       ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:11404413,
CC       ECO:0000269|PubMed:17848514, ECO:0000269|PubMed:19498462}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-1236865, EBI-1236865;
CC       Q9Y6N7:ROBO1; NbExp=2; IntAct=EBI-1236865, EBI-399762;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10102268}.
CC       Note=The C-terminal cleavage protein is more diffusible than the
CC       larger N-terminal protein that is more tightly cell associated.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000305};
CC         IsoId=O94813-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=O94813-2; Sequence=VSP_050035, VSP_050036;
CC       Name=3 {ECO:0000305};
CC         IsoId=O94813-3; Sequence=VSP_050036;
CC   -!- TISSUE SPECIFICITY: Fetal lung and kidney, and adult spinal cord.
CC       Weak expression in adult adrenal gland, thyroid, trachea and other
CC       tissues examined. {ECO:0000269|PubMed:10349621,
CC       ECO:0000269|PubMed:9813312}.
CC   -!- DOMAIN: The leucine-rich repeat domain is sufficient for guiding
CC       both axon projection and neuronal migration, in vitro.
CC       {ECO:0000269|PubMed:11222645}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SLIT2ID42328ch4p15.html";
DR   EMBL; AB017168; BAA35185.1; -; mRNA.
DR   EMBL; AF055585; AAD04309.1; -; mRNA.
DR   EMBL; AF133270; AAD25539.1; -; mRNA.
DR   EMBL; AC021118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471069; EAW92793.1; -; Genomic_DNA.
DR   EMBL; BC117190; AAI17191.1; -; mRNA.
DR   EMBL; BC143978; AAI43979.1; -; mRNA.
DR   CCDS; CCDS3426.1; -. [O94813-1]
DR   CCDS; CCDS75110.1; -. [O94813-2]
DR   CCDS; CCDS75111.1; -. [O94813-3]
DR   RefSeq; NP_001276064.1; NM_001289135.2. [O94813-2]
DR   RefSeq; NP_001276065.1; NM_001289136.2. [O94813-3]
DR   RefSeq; NP_004778.1; NM_004787.3. [O94813-1]
DR   UniGene; Hs.29802; -.
DR   PDB; 2V70; X-ray; 3.01 A; A/B/C/D=504-714.
DR   PDB; 2V9S; X-ray; 2.00 A; A/B/C/D=271-480.
DR   PDB; 2V9T; X-ray; 1.70 A; B=271-479.
DR   PDB; 2WFH; X-ray; 1.80 A; A/B=726-907.
DR   PDBsum; 2V70; -.
DR   PDBsum; 2V9S; -.
DR   PDBsum; 2V9T; -.
DR   PDBsum; 2WFH; -.
DR   ProteinModelPortal; O94813; -.
DR   SMR; O94813; -.
DR   BioGrid; 114756; 18.
DR   DIP; DIP-38198N; -.
DR   IntAct; O94813; 10.
DR   MINT; O94813; -.
DR   STRING; 9606.ENSP00000422591; -.
DR   iPTMnet; O94813; -.
DR   PhosphoSitePlus; O94813; -.
DR   BioMuta; SLIT2; -.
DR   EPD; O94813; -.
DR   jPOST; O94813; -.
DR   MaxQB; O94813; -.
DR   PaxDb; O94813; -.
DR   PeptideAtlas; O94813; -.
DR   PRIDE; O94813; -.
DR   ProteomicsDB; 50454; -.
DR   ProteomicsDB; 50455; -. [O94813-2]
DR   ProteomicsDB; 50456; -. [O94813-3]
DR   Ensembl; ENST00000503823; ENSP00000427548; ENSG00000145147. [O94813-3]
DR   Ensembl; ENST00000503837; ENSP00000422261; ENSG00000145147. [O94813-2]
DR   Ensembl; ENST00000504154; ENSP00000422591; ENSG00000145147. [O94813-1]
DR   GeneID; 9353; -.
DR   KEGG; hsa:9353; -.
DR   UCSC; uc003gpr.3; human. [O94813-1]
DR   CTD; 9353; -.
DR   DisGeNET; 9353; -.
DR   EuPathDB; HostDB:ENSG00000145147.19; -.
DR   GeneCards; SLIT2; -.
DR   HGNC; HGNC:11086; SLIT2.
DR   HPA; CAB007590; -.
DR   HPA; HPA019511; -.
DR   HPA; HPA023088; -.
DR   MIM; 603746; gene.
DR   neXtProt; NX_O94813; -.
DR   OpenTargets; ENSG00000145147; -.
DR   PharmGKB; PA35939; -.
DR   eggNOG; KOG4237; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   GeneTree; ENSGT00940000158402; -.
DR   HOGENOM; HOG000116120; -.
DR   HOVERGEN; HBG057959; -.
DR   InParanoid; O94813; -.
DR   KO; K06839; -.
DR   OrthoDB; 28488at2759; -.
DR   PhylomeDB; O94813; -.
DR   TreeFam; TF332887; -.
DR   Reactome; R-HSA-373752; Netrin-1 signaling.
DR   Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR   Reactome; R-HSA-428540; Activation of RAC1.
DR   Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR   Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
DR   Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-HSA-8985586; SLIT2:ROBO1 increases RHOA activity.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   SIGNOR; O94813; -.
DR   ChiTaRS; SLIT2; human.
DR   EvolutionaryTrace; O94813; -.
DR   GeneWiki; SLIT2; -.
DR   GenomeRNAi; 9353; -.
DR   PRO; PR:O94813; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000145147; Expressed in 230 organ(s), highest expression level in upper lobe of lung.
DR   ExpressionAtlas; O94813; baseline and differential.
DR   Genevisible; O94813; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0043237; F:laminin-1 binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0043394; F:proteoglycan binding; IPI:UniProtKB.
DR   GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
DR   GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IDA:UniProtKB.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0071504; P:cellular response to heparin; IDA:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
DR   GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; IDA:UniProtKB.
DR   GO; GO:0021972; P:corticospinal neuron axon guidance through spinal cord; IMP:BHF-UCL.
DR   GO; GO:0050929; P:induction of negative chemotaxis; IDA:UniProtKB.
DR   GO; GO:0008045; P:motor neuron axon guidance; IDA:UniProtKB.
DR   GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0090288; P:negative regulation of cellular response to growth factor stimulus; IDA:BHF-UCL.
DR   GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:UniProtKB.
DR   GO; GO:0010593; P:negative regulation of lamellipodium assembly; IDA:UniProtKB.
DR   GO; GO:0002689; P:negative regulation of leukocyte chemotaxis; IDA:UniProtKB.
DR   GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:BHF-UCL.
DR   GO; GO:0071676; P:negative regulation of mononuclear cell migration; IDA:BHF-UCL.
DR   GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0090260; P:negative regulation of retinal ganglion cell axon guidance; IDA:UniProtKB.
DR   GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IDA:UniProtKB.
DR   GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; TAS:UniProtKB.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0051414; P:response to cortisol; IEP:UniProtKB.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:UniProtKB.
DR   GO; GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR   Gene3D; 3.80.10.10; -; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   Pfam; PF00008; EGF; 5.
DR   Pfam; PF12661; hEGF; 2.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF13855; LRR_8; 7.
DR   Pfam; PF01463; LRRCT; 4.
DR   Pfam; PF01462; LRRNT; 4.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM00274; FOLN; 3.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00369; LRR_TYP; 17.
DR   SMART; SM00082; LRRCT; 4.
DR   SMART; SM00013; LRRNT; 4.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 9.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR   PROSITE; PS51450; LRR; 20.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chemotaxis; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Heparin-binding;
KW   Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     30       {ECO:0000255}.
FT   CHAIN        31   1529       Slit homolog 2 protein.
FT                                /FTId=PRO_0000007725.
FT   CHAIN        31   1121       Slit homolog 2 protein N-product.
FT                                /FTId=PRO_0000007726.
FT   CHAIN      1122   1529       Slit homolog 2 protein C-product.
FT                                /FTId=PRO_0000007727.
FT   DOMAIN       31     55       LRRNT.
FT   REPEAT       56     77       LRR 1.
FT   REPEAT       80    101       LRR 2.
FT   REPEAT      104    125       LRR 3.
FT   REPEAT      128    149       LRR 4.
FT   REPEAT      152    173       LRR 5.
FT   REPEAT      176    197       LRR 6.
FT   DOMAIN      209    259       LRRCT 1.
FT   DOMAIN      264    300       LRRNT 2.
FT   REPEAT      301    322       LRR 7.
FT   REPEAT      325    346       LRR 8.
FT   REPEAT      349    370       LRR 9.
FT   REPEAT      373    394       LRR 10.
FT   REPEAT      397    418       LRR 11.
FT   DOMAIN      430    480       LRRCT 2.
FT   DOMAIN      497    533       LRRNT 3.
FT   REPEAT      534    555       LRR 12.
FT   REPEAT      559    580       LRR 13.
FT   REPEAT      583    604       LRR 14.
FT   REPEAT      607    628       LRR 15.
FT   REPEAT      631    652       LRR 16.
FT   DOMAIN      664    714       LRRCT 3.
FT   DOMAIN      718    754       LRRNT 4.
FT   REPEAT      755    777       LRR 17.
FT   REPEAT      778    799       LRR 18.
FT   REPEAT      802    823       LRR 19.
FT   REPEAT      826    847       LRR 20.
FT   DOMAIN      859    909       LRRCT 4.
FT   DOMAIN      918    955       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      957    996       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      998   1034       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1036   1074       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1076   1112       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1121   1157       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1160   1333       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1332   1368       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1453   1528       CTCK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00039, ECO:0000305}.
FT   SITE       1121   1122       Cleavage.
FT   CARBOHYD     66     66       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    186    186       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    564    564       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    623    623       N-linked (GlcNAc...) asparagine.
FT   CARBOHYD    794    794       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    799    799       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1009   1009       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1010   1010       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1019   1019       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1183   1183       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1266   1266       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1300   1300       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    277    286
FT   DISULFID    434    457
FT   DISULFID    436    478
FT   DISULFID    506    512
FT   DISULFID    510    519
FT   DISULFID    668    691
FT   DISULFID    670    712
FT   DISULFID    727    733
FT   DISULFID    731    740
FT   DISULFID    863    886
FT   DISULFID    865    907
FT   DISULFID    922    933       {ECO:0000250}.
FT   DISULFID    927    943       {ECO:0000250}.
FT   DISULFID    945    954       {ECO:0000250}.
FT   DISULFID    961    972       {ECO:0000250}.
FT   DISULFID    966    984       {ECO:0000250}.
FT   DISULFID    986    995       {ECO:0000250}.
FT   DISULFID   1002   1013       {ECO:0000250}.
FT   DISULFID   1007   1022       {ECO:0000250}.
FT   DISULFID   1024   1033       {ECO:0000250}.
FT   DISULFID   1040   1053       {ECO:0000250}.
FT   DISULFID   1047   1062       {ECO:0000250}.
FT   DISULFID   1064   1073       {ECO:0000250}.
FT   DISULFID   1080   1091       {ECO:0000250}.
FT   DISULFID   1085   1100       {ECO:0000250}.
FT   DISULFID   1102   1111       {ECO:0000250}.
FT   DISULFID   1125   1136       {ECO:0000250}.
FT   DISULFID   1130   1145       {ECO:0000250}.
FT   DISULFID   1147   1156       {ECO:0000250}.
FT   DISULFID   1307   1333       {ECO:0000250}.
FT   DISULFID   1336   1346       {ECO:0000250}.
FT   DISULFID   1341   1356       {ECO:0000250}.
FT   DISULFID   1358   1367       {ECO:0000250}.
FT   DISULFID   1375   1385       {ECO:0000250}.
FT   DISULFID   1380   1395       {ECO:0000250}.
FT   DISULFID   1397   1406       {ECO:0000250}.
FT   DISULFID   1416   1426       {ECO:0000250}.
FT   DISULFID   1421   1436       {ECO:0000250}.
FT   DISULFID   1438   1447       {ECO:0000250}.
FT   DISULFID   1453   1492       {ECO:0000250}.
FT   DISULFID   1471   1506       {ECO:0000250}.
FT   DISULFID   1482   1522       {ECO:0000250}.
FT   DISULFID   1486   1524       {ECO:0000250}.
FT   VAR_SEQ     258    258       S -> SDEEE (in isoform 2).
FT                                {ECO:0000303|PubMed:10102268,
FT                                ECO:0000303|PubMed:9813312}.
FT                                /FTId=VSP_050035.
FT   VAR_SEQ     480    487       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:10102268,
FT                                ECO:0000303|PubMed:10349621,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9813312}.
FT                                /FTId=VSP_050036.
FT   VARIANT     636    636       S -> P. {ECO:0000269|PubMed:9813312}.
FT                                /FTId=VAR_018098.
FT   VARIANT    1277   1277       S -> F (in dbSNP:rs771375896).
FT                                {ECO:0000269|PubMed:9813312}.
FT                                /FTId=VAR_018099.
FT   CONFLICT    226    226       Q -> K (in Ref. 2; AAD25539).
FT                                {ECO:0000305}.
FT   CONFLICT    607    610       SLKT -> KPQN (in Ref. 3; AAD04309).
FT                                {ECO:0000305}.
FT   CONFLICT    634    634       L -> M (in Ref. 3; AAD04309).
FT                                {ECO:0000305}.
FT   STRAND      277    280       {ECO:0000244|PDB:2V9T}.
FT   STRAND      283    285       {ECO:0000244|PDB:2V9T}.
FT   STRAND      304    306       {ECO:0000244|PDB:2V9T}.
FT   TURN        317    322       {ECO:0000244|PDB:2V9S}.
FT   STRAND      328    330       {ECO:0000244|PDB:2V9T}.
FT   TURN        341    346       {ECO:0000244|PDB:2V9T}.
FT   STRAND      352    354       {ECO:0000244|PDB:2V9T}.
FT   TURN        365    370       {ECO:0000244|PDB:2V9T}.
FT   STRAND      376    378       {ECO:0000244|PDB:2V9T}.
FT   TURN        389    394       {ECO:0000244|PDB:2V9T}.
FT   STRAND      400    402       {ECO:0000244|PDB:2V9T}.
FT   TURN        413    418       {ECO:0000244|PDB:2V9T}.
FT   STRAND      424    426       {ECO:0000244|PDB:2V9T}.
FT   HELIX       436    438       {ECO:0000244|PDB:2V9T}.
FT   HELIX       439    447       {ECO:0000244|PDB:2V9T}.
FT   STRAND      456    460       {ECO:0000244|PDB:2V9T}.
FT   HELIX       461    463       {ECO:0000244|PDB:2V9T}.
FT   HELIX       468    470       {ECO:0000244|PDB:2V9T}.
FT   HELIX       473    475       {ECO:0000244|PDB:2V9T}.
FT   STRAND      511    513       {ECO:0000244|PDB:2V70}.
FT   STRAND      516    518       {ECO:0000244|PDB:2V70}.
FT   STRAND      536    539       {ECO:0000244|PDB:2V70}.
FT   HELIX       554    556       {ECO:0000244|PDB:2V70}.
FT   STRAND      562    564       {ECO:0000244|PDB:2V70}.
FT   TURN        575    580       {ECO:0000244|PDB:2V70}.
FT   STRAND      586    588       {ECO:0000244|PDB:2V70}.
FT   HELIX       599    602       {ECO:0000244|PDB:2V70}.
FT   STRAND      610    612       {ECO:0000244|PDB:2V70}.
FT   STRAND      633    636       {ECO:0000244|PDB:2V70}.
FT   TURN        647    652       {ECO:0000244|PDB:2V70}.
FT   STRAND      658    660       {ECO:0000244|PDB:2V70}.
FT   HELIX       670    672       {ECO:0000244|PDB:2V70}.
FT   HELIX       673    681       {ECO:0000244|PDB:2V70}.
FT   STRAND      690    694       {ECO:0000244|PDB:2V70}.
FT   HELIX       695    697       {ECO:0000244|PDB:2V70}.
FT   HELIX       702    704       {ECO:0000244|PDB:2V70}.
FT   HELIX       707    709       {ECO:0000244|PDB:2V70}.
FT   STRAND      732    734       {ECO:0000244|PDB:2WFH}.
FT   STRAND      737    739       {ECO:0000244|PDB:2WFH}.
FT   STRAND      758    760       {ECO:0000244|PDB:2WFH}.
FT   HELIX       771    775       {ECO:0000244|PDB:2WFH}.
FT   STRAND      781    783       {ECO:0000244|PDB:2WFH}.
FT   TURN        794    799       {ECO:0000244|PDB:2WFH}.
FT   STRAND      805    807       {ECO:0000244|PDB:2WFH}.
FT   TURN        818    823       {ECO:0000244|PDB:2WFH}.
FT   STRAND      829    831       {ECO:0000244|PDB:2WFH}.
FT   TURN        842    847       {ECO:0000244|PDB:2WFH}.
FT   STRAND      853    855       {ECO:0000244|PDB:2WFH}.
FT   HELIX       865    867       {ECO:0000244|PDB:2WFH}.
FT   HELIX       868    876       {ECO:0000244|PDB:2WFH}.
FT   STRAND      885    889       {ECO:0000244|PDB:2WFH}.
FT   HELIX       890    892       {ECO:0000244|PDB:2WFH}.
FT   TURN        897    899       {ECO:0000244|PDB:2WFH}.
FT   HELIX       902    904       {ECO:0000244|PDB:2WFH}.
SQ   SEQUENCE   1529 AA;  169870 MW;  5D19CC5E7FD461BA CRC64;
     MRGVGWQMLS LSLGLVLAIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP RNIPRNTERL
     DLNGNNITRI TKTDFAGLRH LRVLQLMENK ISTIERGAFQ DLKELERLRL NRNHLQLFPE
     LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA VDIKNLQLDY NQISCIEDGA FRALRDLEVL
     TLNNNNITRL SVASFNHMPK LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS
     HLRGHNVAEV QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE
     TITEIRLEQN TIKVIPPGAF SPYKKLRRID LSNNQISELA PDAFQGLRSL NSLVLYGNKI
     TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL LSLYDNKLQT IAKGTFSPLR
     AIQTMHLAQN PFICDCHLKW LADYLHTNPI ETSGARCTSP RRLANKRIGQ IKSKKFRCSA
     KEQYFIPGTE DYRSKLSGDC FADLACPEKC RCEGTTVDCS NQKLNKIPEH IPQYTAELRL
     NNNEFTVLEA TGIFKKLPQL RKINFSNNKI TDIEEGAFEG ASGVNEILLT SNRLENVQHK
     MFKGLESLKT LMLRSNRITC VGNDSFIGLS SVRLLSLYDN QITTVAPGAF DTLHSLSTLN
     LLANPFNCNC YLAWLGEWLR KKRIVTGNPR CQKPYFLKEI PIQDVAIQDF TCDDGNDDNS
     CSPLSRCPTE CTCLDTVVRC SNKGLKVLPK GIPRDVTELY LDGNQFTLVP KELSNYKHLT
     LIDLSNNRIS TLSNQSFSNM TQLLTLILSY NRLRCIPPRT FDGLKSLRLL SLHGNDISVV
     PEGAFNDLSA LSHLAIGANP LYCDCNMQWL SDWVKSEYKE PGIARCAGPG EMADKLLLTT
     PSKKFTCQGP VDVNILAKCN PCLSNPCKND GTCNSDPVDF YRCTCPYGFK GQDCDVPIHA
     CISNPCKHGG TCHLKEGEED GFWCICADGF EGENCEVNVD DCEDNDCENN STCVDGINNY
     TCLCPPEYTG ELCEEKLDFC AQDLNPCQHD SKCILTPKGF KCDCTPGYVG EHCDIDFDDC
     QDNKCKNGAH CTDAVNGYTC ICPEGYSGLF CEFSPPMVLP RTSPCDNFDC QNGAQCIVRI
     NEPICQCLPG YQGEKCEKLV SVNFINKESY LQIPSAKVRP QTNITLQIAT DEDSGILLYK
     GDKDHIAVEL YRGRVRASYD TGSHPASAIY SVETINDGNF HIVELLALDQ SLSLSVDGGN
     PKIITNLSKQ STLNFDSPLY VGGMPGKSNV ASLRQAPGQN GTSFHGCIRN LYINSELQDF
     QKVPMQTGIL PGCEPCHKKV CAHGTCQPSS QAGFTCECQE GWMGPLCDQR TNDPCLGNKC
     VHGTCLPINA FSYSCKCLEG HGGVLCDEEE DLFNPCQAIK CKHGKCRLSG LGQPYCECSS
     GYTGDSCDRE ISCRGERIRD YYQKQQGYAA CQTTKKVSRL ECRGGCAGGQ CCGPLRSKRR
     KYSFECTDGS SFVDEVEKVV KCGCTRCVS
//
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