SLIT3_RAT
ID SLIT3_RAT Reviewed; 1523 AA.
AC O88280;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Slit homolog 3 protein;
DE Short=Slit-3;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 5;
DE Short=Multiple EGF-like domains protein 5;
DE Flags: Precursor;
GN Name=Slit3; Synonyms=Megf5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=11754167; DOI=10.1002/cne.10068;
RA Marillat V., Cases O., Nguyen-Ba-Charvet K.T., Tessier-Lavigne M.,
RA Sotelo C., Chedotal A.;
RT "Spatiotemporal expression patterns of slit and robo genes in the rat
RT brain.";
RL J. Comp. Neurol. 442:130-155(2002).
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 at E20, and between P0 and P5 in
CC olfactory mitral cells. Detected between E18 and E20, between P0 and
CC P10, and in adult in anterior olfactor, hypothalamus ventromedial
CC nuclei. Detected at E15 in cortex marginal zone. Detected between E15
CC and E20, between P0 and P10, and in adult in cortex entorhinal and
CC periform region, hippocampal regions, basal telencephalon bed stria
CC terminalis nuclei. Detected at E20, between P0 and P10, and in adult in
CC cortex induseum griseum and tenia tecta, and basal telencephalon
CC olfactory tubercle. Detected between P0 and P10, and in adult in
CC ventral thalamus zona incerta. Detected between P5 and P10, and in
CC adult in ventral thalamus reticular nuclei. Detected between P0 and
CC P10, and in adult in dorsal thalamus regions.
CC {ECO:0000269|PubMed:11754167}.
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DR EMBL; AB011531; BAA32461.1; -; mRNA.
DR PIR; T13953; T13953.
DR RefSeq; NP_112611.1; NM_031321.1.
DR AlphaFoldDB; O88280; -.
DR SMR; O88280; -.
DR BioGRID; 249708; 1.
DR IntAct; O88280; 2.
DR STRING; 10116.ENSRNOP00000009714; -.
DR CarbonylDB; O88280; -.
DR GlyGen; O88280; 12 sites.
DR PaxDb; O88280; -.
DR PRIDE; O88280; -.
DR GeneID; 83467; -.
DR KEGG; rno:83467; -.
DR UCSC; RGD:69311; rat.
DR CTD; 6586; -.
DR RGD; 69311; Slit3.
DR eggNOG; KOG4237; Eukaryota.
DR InParanoid; O88280; -.
DR OrthoDB; 28488at2759; -.
DR PhylomeDB; O88280; -.
DR PRO; PR:O88280; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
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:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0061364; P:apoptotic process involved in luteolysis; ISO:RGD.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISO:RGD.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0051414; P:response to cortisol; ISO:RGD.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISO:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
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; 6.
DR Pfam; PF12661; hEGF; 1.
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_0000007734"
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"
SQ SEQUENCE 1523 AA; 167768 MW; 6CE1B7AF9244478E CRC64;
MAPGRTGAGA AVRARLALAL ALASILSGPP AAACPTKCTC SAASVDCHGL GLRAVPRGIP
RNAERLDLDR NNITRITKMD FTGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGVTGVK NLQLDNNHIS CIEDGAFRAL
RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTIGQFT
LCMAPVHLRG FSVADVQKKE YVCPGPHSEA PACNANSLSC PSACSCSNNI VDCRGKGLTE
IPANLPEGIV EIRLEQNSIK SIPAGAFIQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
VLYGNKITEI PKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
KKFRCSGSED YRNRFSSECF MDLVCPEKCR CEGTIVDCSN QKLSRIPSHL PEYTTDLRLN
DNDIAVLEAT GIFKKLPNLR KINLSNNRIK EVREGAFDGA AGVQELMLTG NQLETMHGRM
FRGLSGLKTL MLRSNLISCV NNDTFAGLSS VRLLSLYDNR ITTISPGAFT TLVSLSTINL
LSNPFNCNCH MAWLGRWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CEGNEENSCQ
LSPRCPEQCT CVETVVRCSN RGLHTLPKGM PKDVTELYLE GNHLTAVPKE LSTFRQLTLI
DLSNNSISML TNHTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
GSFNDLTSLS HLALGINPLH CDCSLRWLSE WIKAGYKEPG IARCSSPESM ADRLLLTTPT
HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CSQDPVEQYR CTCPYSYKGK DCTVPINTCV
QNPCQHGGTC HLSESHRDGF SCSCPLGFEG QRCEINPDDC EDNDCENSAT CVDGINNYAC
VCPPNYTGEL CDEVIDYCVP EMNLCQHEAK CISLDKGFRC ECVPGYSGKL CETDNDDCVA
HKCRHGAQCV DAVNGYTCIC PQGFSGLFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVMLNQTL NLVVDKGAPK
SLGKLQKQPA VGINSPLYLG GIPTSTGLSA LRQGADRPLG GFHGCIHEVR INNELQDFKA
LPPQSLGVSP GCKSCTVCRH GLCRSVEKDS VVCECHPGWT GPLCDQEAQD PCLGHSCSHG
TCVATGNSYV CKCAEGYEGP LCDQKNDSAN ACSAFKCHHG QCHISDRGEP YCLCQPGFSG
NHCEQENPCL GEIVREAIRR QKDYASCATA SKVPIMVCRG GCGSQCCQPI RSKRRKYVFQ
CTDGSSFVEE VERHLECGCR ECS
