GenomeNet

Database: UniProt
Entry: Q9WVB4
LinkDB: Q9WVB4
Original site: Q9WVB4 
ID   SLIT3_MOUSE             Reviewed;        1523 AA.
AC   Q9WVB4; B1ATW4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-FEB-2019, entry version 157.
DE   RecName: Full=Slit homolog 3 protein;
DE            Short=Slit-3;
DE            Short=Slit3;
DE   Flags: Precursor;
GN   Name=Slit3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=ICR X Swiss Webster;
RX   PubMed=10433822; DOI=10.1006/dbio.1999.9371;
RA   Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.;
RT   "The mouse SLIT family: secreted ligands for ROBO expressed in
RT   patterns that suggest a role in morphogenesis and axon guidance.";
RL   Dev. Biol. 212:290-306(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: May act as molecular guidance cue in cellular migration,
CC       and function may be mediated by interaction with roundabout
CC       homolog receptors.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Detected as early as 8.25 dpc in the ventral
CC       neural tube. From 9.5 dpc to 11.5 dpc is expressed in the floor
CC       plate and motor columns. This pattern of expression continued
CC       until at least 17.5 dpc and remained weak. Rostrally, at 8.25 dpc
CC       is expressed in the ventral midline of the neural groove and in
CC       the neural fold prior to closure of the neural tube. Between 8.5
CC       dpc and 9.5 dpc, expression is observed in the ventral side of the
CC       mesencephalon and metencephalon and in the commissural plate after
CC       closure of the neural tube. After 13.5 dpc, the expression of
CC       SLIT3 is weak in the developing CNS. At 9.5 dpc, SLIT3 is detected
CC       in the otic vesicle and in the clefts between the first and the
CC       second branchial arches. Between 10.5 dpc and 11.5 dpc is
CC       prominently expressed in the otic vesicle but decreased in the
CC       branchial clefts. From 13.5 dpc to 17.5 dpc, expression is
CC       observed in the cochlea, in the pigment layer of the retina, and
CC       in the olfactory epithelium. At 13.5 dpc expression is observed in
CC       the whisker follicle surrounding the bulb and shaft. In the
CC       developing limb is first detected at 10.5 dpc in distal limb bud
CC       mesenchyme. At this stage, is also observed in lateral ridge
CC       tissue flanking the limb bud. This pattern persisted through 11.5
CC       dpc but unlike with SLIT2, expression is not observed in the
CC       inter-limb bud lateral ridge tissue. At 11.5 dpc, expression in
CC       both the fore- and the hindlimb is most intense in the distal
CC       anterior mesenchyme and in the proximal posterior cleft between
CC       the limb bud and the lateral ridge. At 13.5 dpc could be detected
CC       in the wrist and weakly in palm and proximal part of the digits
CC       excluding the tips of the digits. {ECO:0000269|PubMed:10433822}.
DR   EMBL; AF144629; AAD44760.1; -; mRNA.
DR   EMBL; AL669839; CAI24241.1; -; Genomic_DNA.
DR   EMBL; AL669856; CAI24241.1; JOINED; Genomic_DNA.
DR   EMBL; AL731688; CAI24241.1; JOINED; Genomic_DNA.
DR   EMBL; AL732401; CAI24241.1; JOINED; Genomic_DNA.
DR   EMBL; AL732630; CAI24241.1; JOINED; Genomic_DNA.
DR   EMBL; AL731688; CAI24974.1; -; Genomic_DNA.
DR   EMBL; AL669839; CAI24974.1; JOINED; Genomic_DNA.
DR   EMBL; AL669856; CAI24974.1; JOINED; Genomic_DNA.
DR   EMBL; AL732401; CAI24974.1; JOINED; Genomic_DNA.
DR   EMBL; AL732630; CAI24974.1; JOINED; Genomic_DNA.
DR   EMBL; AL732630; CAI25087.1; -; Genomic_DNA.
DR   EMBL; AL669839; CAI25087.1; JOINED; Genomic_DNA.
DR   EMBL; AL669856; CAI25087.1; JOINED; Genomic_DNA.
DR   EMBL; AL731688; CAI25087.1; JOINED; Genomic_DNA.
DR   EMBL; AL732401; CAI25087.1; JOINED; Genomic_DNA.
DR   EMBL; AL732401; CAI25608.1; -; Genomic_DNA.
DR   EMBL; AL669839; CAI25608.1; JOINED; Genomic_DNA.
DR   EMBL; AL669856; CAI25608.1; JOINED; Genomic_DNA.
DR   EMBL; AL731688; CAI25608.1; JOINED; Genomic_DNA.
DR   EMBL; AL732630; CAI25608.1; JOINED; Genomic_DNA.
DR   EMBL; AL669856; CAI25804.1; -; Genomic_DNA.
DR   EMBL; AL669839; CAI25804.1; JOINED; Genomic_DNA.
DR   EMBL; AL731688; CAI25804.1; JOINED; Genomic_DNA.
DR   EMBL; AL732401; CAI25804.1; JOINED; Genomic_DNA.
DR   EMBL; AL732630; CAI25804.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS24542.1; -.
DR   RefSeq; NP_035542.2; NM_011412.3.
DR   UniGene; Mm.478604; -.
DR   ProteinModelPortal; Q9WVB4; -.
DR   BioGrid; 203329; 3.
DR   STRING; 10090.ENSMUSP00000066857; -.
DR   PhosphoSitePlus; Q9WVB4; -.
DR   MaxQB; Q9WVB4; -.
DR   PaxDb; Q9WVB4; -.
DR   PRIDE; Q9WVB4; -.
DR   Ensembl; ENSMUST00000069837; ENSMUSP00000066857; ENSMUSG00000056427.
DR   GeneID; 20564; -.
DR   KEGG; mmu:20564; -.
DR   UCSC; uc007ild.2; mouse.
DR   CTD; 6586; -.
DR   MGI; MGI:1315202; Slit3.
DR   eggNOG; KOG4237; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   GeneTree; ENSGT00940000159322; -.
DR   HOGENOM; HOG000116120; -.
DR   HOVERGEN; HBG057959; -.
DR   InParanoid; Q9WVB4; -.
DR   KO; K06850; -.
DR   OMA; ELYQGHI; -.
DR   OrthoDB; 28488at2759; -.
DR   TreeFam; TF332887; -.
DR   Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR   ChiTaRS; Slit3; mouse.
DR   PRO; PR:Q9WVB4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000056427; Expressed in 239 organ(s), highest expression level in dorsal pancreas.
DR   Genevisible; Q9WVB4; MM.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048495; F:Roundabout binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0061364; P:apoptotic process involved in luteolysis; IEA:Ensembl.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
DR   GO; GO:0051414; P:response to cortisol; IEA:Ensembl.
DR   GO; GO:0035385; P:Roundabout signaling pathway; ISO:MGI.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP: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; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF02210; Laminin_G_2; 1.
DR   Pfam; PF13855; LRR_8; 5.
DR   Pfam; PF01463; LRRCT; 4.
DR   Pfam; PF01462; LRRNT; 3.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 9.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00369; LRR_TYP; 18.
DR   SMART; SM00082; LRRCT; 4.
DR   SMART; SM00013; LRRNT; 4.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
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   2: Evidence at transcript level;
KW   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW   Neurogenesis; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34   1523       Slit homolog 3 protein.
FT                                /FTId=PRO_0000007733.
FT   DOMAIN       34     61       LRRNT.
FT   REPEAT       62     83       LRR 1.
FT   REPEAT       86    107       LRR 2.
FT   REPEAT      110    131       LRR 3.
FT   REPEAT      134    155       LRR 4.
FT   REPEAT      158    179       LRR 5.
FT   REPEAT      182    203       LRR 6.
FT   DOMAIN      215    265       LRRCT 1.
FT   DOMAIN      271    307       LRRNT 2.
FT   REPEAT      308    329       LRR 7.
FT   REPEAT      332    353       LRR 8.
FT   REPEAT      356    377       LRR 9.
FT   REPEAT      380    401       LRR 10.
FT   REPEAT      404    425       LRR 11.
FT   DOMAIN      437    487       LRRCT 2.
FT   DOMAIN      496    532       LRRNT 3.
FT   REPEAT      533    554       LRR 12.
FT   REPEAT      558    579       LRR 13.
FT   REPEAT      582    603       LRR 14.
FT   REPEAT      606    627       LRR 15.
FT   REPEAT      630    651       LRR 16.
FT   DOMAIN      663    713       LRRCT 3.
FT   DOMAIN      716    752       LRRNT 4.
FT   REPEAT      753    774       LRR 17.
FT   REPEAT      776    797       LRR 18.
FT   REPEAT      800    821       LRR 19.
FT   REPEAT      824    845       LRR 20.
FT   DOMAIN      857    907       LRRCT 4.
FT   DOMAIN      918    953       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      955    994       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      996   1032       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1034   1072       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1074   1110       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1119   1155       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1158   1332       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1340   1365       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1368   1403       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1408   1444       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1449   1523       CTCK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00039}.
FT   CARBOHYD     72     72       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    192    192       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    563    563       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    622    622       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    784    784       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    792    792       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    797    797       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    928    928       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1025   1025       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1181   1181       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1247   1247       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1406   1406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    284    293       {ECO:0000250}.
FT   DISULFID    441    464       {ECO:0000250}.
FT   DISULFID    443    485       {ECO:0000250}.
FT   DISULFID    505    511       {ECO:0000250}.
FT   DISULFID    509    518       {ECO:0000250}.
FT   DISULFID    667    690       {ECO:0000250}.
FT   DISULFID    669    711       {ECO:0000250}.
FT   DISULFID    920    931       {ECO:0000250}.
FT   DISULFID    925    941       {ECO:0000250}.
FT   DISULFID    943    952       {ECO:0000250}.
FT   DISULFID    959    970       {ECO:0000250}.
FT   DISULFID    964    982       {ECO:0000250}.
FT   DISULFID    984    993       {ECO:0000250}.
FT   DISULFID   1000   1011       {ECO:0000250}.
FT   DISULFID   1005   1020       {ECO:0000250}.
FT   DISULFID   1022   1031       {ECO:0000250}.
FT   DISULFID   1038   1051       {ECO:0000250}.
FT   DISULFID   1045   1060       {ECO:0000250}.
FT   DISULFID   1062   1071       {ECO:0000250}.
FT   DISULFID   1078   1089       {ECO:0000250}.
FT   DISULFID   1083   1098       {ECO:0000250}.
FT   DISULFID   1100   1109       {ECO:0000250}.
FT   DISULFID   1123   1134       {ECO:0000250}.
FT   DISULFID   1128   1143       {ECO:0000250}.
FT   DISULFID   1145   1154       {ECO:0000250}.
FT   DISULFID   1305   1332       {ECO:0000250}.
FT   DISULFID   1355   1364       {ECO:0000250}.
FT   DISULFID   1372   1382       {ECO:0000250}.
FT   DISULFID   1377   1391       {ECO:0000250}.
FT   DISULFID   1393   1402       {ECO:0000250}.
FT   DISULFID   1412   1422       {ECO:0000250}.
FT   DISULFID   1417   1432       {ECO:0000250}.
FT   DISULFID   1434   1443       {ECO:0000250}.
FT   DISULFID   1449   1487       {ECO:0000250}.
FT   DISULFID   1467   1501       {ECO:0000250}.
FT   DISULFID   1478   1517       {ECO:0000250}.
FT   DISULFID   1482   1519       {ECO:0000250}.
FT   CONFLICT    582    582       G -> S (in Ref. 1; AAD44760).
FT                                {ECO:0000305}.
FT   CONFLICT    606    606       S -> G (in Ref. 1; AAD44760).
FT                                {ECO:0000305}.
FT   CONFLICT    729    729       C -> F (in Ref. 1; AAD44760).
FT                                {ECO:0000305}.
FT   CONFLICT    999    999       D -> G (in Ref. 1; AAD44760).
FT                                {ECO:0000305}.
FT   CONFLICT   1242   1242       E -> K (in Ref. 1; AAD44760).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1523 AA;  167727 MW;  95C4E98E58B9C8EA CRC64;
     MALGRTGAGA AVRARLALGL ALASILSGPP AAACPTKCTC SAASVDCHGL GLRAVPRGIP
     RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSII ERGAFQDLKQ LERLRLNKNK
     LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGVTGVK NLQLDNNHIS CIEDGAFRAL
     RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTIGQFT
     LCMAPVHLRG FSVADVQKKE YVCPGPHSEA PACNANSLSC PSACSCSNNI VDCRGKGLTE
     IPANLPEGIV EIRLEQNSIK SIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
     VLYGNKITEI PKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
     GLFVPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
     KKFRCSGSED YRNRFSSECF MDLVCPEKCR CEGTIVDCSN QKLARIPSHL PEYTTDLRLN
     DNDISVLEAT GIFKKLPNLR KINLSNNRIK EVREGAFDGA AGVQELMLTG NQLETMHGRM
     FRGLSSLKTL MLRSNLISCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
     LSNPFNCNCH MAWLGRWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNEESSCQ
     LSPRCPEQCT CVETVVRCSN RGLHALPKGM PKDVTELYLE GNHLTAVPKE LSAFRQLTLI
     DLSNNSISML TNHTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
     GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPESM ADRLLLTTPT
     HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CSQDPVEQYR CTCPYSYKGK DCTVPINTCV
     QNPCEHGGTC HLSENLRDGF SCSCPLGFEG QRCEINPDDC EDNDCENSAT CVDGINNYAC
     LCPPNYTGEL CDEVIDYCVP EMNLCQHEAK CISLDKGFRC ECVPGYSGKL CETNNDDCVA
     HKCRHGAQCV DEVNGYTCIC PQGFSGLFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
     PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
     NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVMLNQTL NLVVDKGAPK
     SLGKLQKQPA VGSNSPLYLG GIPTSTGLSA LRQGADRPLG GFHGCIHEVR INNELQDFKA
     LPPQSLGVSP GCKSCTVCRH GLCRSVEKDS VVCECHPGWT GPLCDQEARD PCLGHSCRHG
     TCMATGDSYV CKCAEGYGGA LCDQKNDSAS ACSAFKCHHG QCHISDRGEP YCLCQPGFSG
     HHCEQENPCM GEIVREAIRR QKDYASCATA SKVPIMECRG GCGSQCCQPI RSKRRKYVFQ
     CTDGSSFVEE VERHLECGCR ACS
//
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