SLIT3_MOUSE
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 03-AUG-2022, entry version 174.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 patterns
RT 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May act as molecular guidance cue in cellular migration, and
CC function may be mediated by interaction with roundabout homolog
CC 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 plate
CC and motor columns. This pattern of expression continued until at least
CC 17.5 dpc and remained weak. Rostrally, at 8.25 dpc is expressed in the
CC ventral midline of the neural groove and in the neural fold prior to
CC closure of the neural tube. Between 8.5 dpc and 9.5 dpc, expression is
CC observed in the ventral side of the mesencephalon and metencephalon and
CC in the commissural plate after closure of the neural tube. After 13.5
CC dpc, the expression of SLIT3 is weak in the developing CNS. At 9.5 dpc,
CC SLIT3 is detected in the otic vesicle and in the clefts between the
CC first and the 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 observed in
CC the cochlea, in the pigment layer of the retina, and in the olfactory
CC epithelium. At 13.5 dpc expression is observed in the whisker follicle
CC surrounding the bulb and shaft. In the developing limb is first
CC detected at 10.5 dpc in distal limb bud mesenchyme. At this stage, is
CC also observed in lateral ridge tissue flanking the limb bud. This
CC pattern persisted through 11.5 dpc but unlike with SLIT2, expression is
CC not observed in the inter-limb bud lateral ridge tissue. At 11.5 dpc,
CC expression in both the fore- and the hindlimb is most intense in the
CC distal anterior mesenchyme and in the proximal posterior cleft between
CC the limb bud and the lateral ridge. At 13.5 dpc could be detected in
CC the wrist and weakly in palm and proximal part of the digits excluding
CC the tips of the digits. {ECO:0000269|PubMed:10433822}.
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DR EMBL; AF144629; AAD44760.1; -; mRNA.
DR EMBL; AL669839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24542.1; -.
DR RefSeq; NP_035542.2; NM_011412.3.
DR AlphaFoldDB; Q9WVB4; -.
DR SMR; Q9WVB4; -.
DR BioGRID; 203329; 4.
DR STRING; 10090.ENSMUSP00000066857; -.
DR GlyConnect; 2717; 1 N-Linked glycan (3 sites).
DR GlyGen; Q9WVB4; 12 sites, 1 N-linked glycan (3 sites).
DR PhosphoSitePlus; Q9WVB4; -.
DR MaxQB; Q9WVB4; -.
DR PaxDb; Q9WVB4; -.
DR PRIDE; Q9WVB4; -.
DR ProteomicsDB; 261421; -.
DR Antibodypedia; 16807; 245 antibodies from 31 providers.
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 VEuPathDB; HostDB:ENSMUSG00000056427; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000159322; -.
DR HOGENOM; CLU_001431_2_0_1; -.
DR InParanoid; Q9WVB4; -.
DR OMA; PACNANS; -.
DR OrthoDB; 28488at2759; -.
DR PhylomeDB; Q9WVB4; -.
DR TreeFam; TF332887; -.
DR Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR BioGRID-ORCS; 20564; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Slit3; mouse.
DR PRO; PR:Q9WVB4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WVB4; protein.
DR Bgee; ENSMUSG00000056427; Expressed in dorsal pancreas and 203 other tissues.
DR Genevisible; Q9WVB4; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
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 CDD; cd00110; LamG; 1.
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 Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Leucine-rich repeat; Neurogenesis; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1523
FT /note="Slit homolog 3 protein"
FT /id="PRO_0000007733"
FT DOMAIN 34..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 86..107
FT /note="LRR 2"
FT REPEAT 110..131
FT /note="LRR 3"
FT REPEAT 134..155
FT /note="LRR 4"
FT REPEAT 158..179
FT /note="LRR 5"
FT REPEAT 182..203
FT /note="LRR 6"
FT DOMAIN 215..265
FT /note="LRRCT 1"
FT DOMAIN 271..307
FT /note="LRRNT 2"
FT REPEAT 308..329
FT /note="LRR 7"
FT REPEAT 332..353
FT /note="LRR 8"
FT REPEAT 356..377
FT /note="LRR 9"
FT REPEAT 380..401
FT /note="LRR 10"
FT REPEAT 404..425
FT /note="LRR 11"
FT DOMAIN 437..487
FT /note="LRRCT 2"
FT DOMAIN 496..532
FT /note="LRRNT 3"
FT REPEAT 533..554
FT /note="LRR 12"
FT REPEAT 558..579
FT /note="LRR 13"
FT REPEAT 582..603
FT /note="LRR 14"
FT REPEAT 606..627
FT /note="LRR 15"
FT REPEAT 630..651
FT /note="LRR 16"
FT DOMAIN 663..713
FT /note="LRRCT 3"
FT DOMAIN 716..752
FT /note="LRRNT 4"
FT REPEAT 753..774
FT /note="LRR 17"
FT REPEAT 776..797
FT /note="LRR 18"
FT REPEAT 800..821
FT /note="LRR 19"
FT REPEAT 824..845
FT /note="LRR 20"
FT DOMAIN 857..907
FT /note="LRRCT 4"
FT DOMAIN 918..953
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 955..994
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 996..1032
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1034..1072
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1074..1110
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1119..1155
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1158..1332
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1340..1365
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1368..1403
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1408..1444
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1449..1523
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 284..293
FT /evidence="ECO:0000250"
FT DISULFID 441..464
FT /evidence="ECO:0000250"
FT DISULFID 443..485
FT /evidence="ECO:0000250"
FT DISULFID 505..511
FT /evidence="ECO:0000250"
FT DISULFID 509..518
FT /evidence="ECO:0000250"
FT DISULFID 667..690
FT /evidence="ECO:0000250"
FT DISULFID 669..711
FT /evidence="ECO:0000250"
FT DISULFID 920..931
FT /evidence="ECO:0000250"
FT DISULFID 925..941
FT /evidence="ECO:0000250"
FT DISULFID 943..952
FT /evidence="ECO:0000250"
FT DISULFID 959..970
FT /evidence="ECO:0000250"
FT DISULFID 964..982
FT /evidence="ECO:0000250"
FT DISULFID 984..993
FT /evidence="ECO:0000250"
FT DISULFID 1000..1011
FT /evidence="ECO:0000250"
FT DISULFID 1005..1020
FT /evidence="ECO:0000250"
FT DISULFID 1022..1031
FT /evidence="ECO:0000250"
FT DISULFID 1038..1051
FT /evidence="ECO:0000250"
FT DISULFID 1045..1060
FT /evidence="ECO:0000250"
FT DISULFID 1062..1071
FT /evidence="ECO:0000250"
FT DISULFID 1078..1089
FT /evidence="ECO:0000250"
FT DISULFID 1083..1098
FT /evidence="ECO:0000250"
FT DISULFID 1100..1109
FT /evidence="ECO:0000250"
FT DISULFID 1123..1134
FT /evidence="ECO:0000250"
FT DISULFID 1128..1143
FT /evidence="ECO:0000250"
FT DISULFID 1145..1154
FT /evidence="ECO:0000250"
FT DISULFID 1305..1332
FT /evidence="ECO:0000250"
FT DISULFID 1355..1364
FT /evidence="ECO:0000250"
FT DISULFID 1372..1382
FT /evidence="ECO:0000250"
FT DISULFID 1377..1391
FT /evidence="ECO:0000250"
FT DISULFID 1393..1402
FT /evidence="ECO:0000250"
FT DISULFID 1412..1422
FT /evidence="ECO:0000250"
FT DISULFID 1417..1432
FT /evidence="ECO:0000250"
FT DISULFID 1434..1443
FT /evidence="ECO:0000250"
FT DISULFID 1449..1487
FT /evidence="ECO:0000250"
FT DISULFID 1467..1501
FT /evidence="ECO:0000250"
FT DISULFID 1478..1517
FT /evidence="ECO:0000250"
FT DISULFID 1482..1519
FT /evidence="ECO:0000250"
FT CONFLICT 582
FT /note="G -> S (in Ref. 1; AAD44760)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="S -> G (in Ref. 1; AAD44760)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="C -> F (in Ref. 1; AAD44760)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="D -> G (in Ref. 1; AAD44760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1242
FT /note="E -> K (in Ref. 1; AAD44760)"
FT /evidence="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
