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Database: UniProt
Entry: G5EFX6
LinkDB: G5EFX6
Original site: G5EFX6 
ID   SLIT1_CAEEL             Reviewed;        1410 AA.
AC   G5EFX6;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   16-JAN-2019, entry version 62.
DE   RecName: Full=Slit homolog 1 protein;
DE            Short=Slt-1;
DE   Flags: Precursor;
GN   Name=slt-1; ORFNames=F40E10.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=11604136; DOI=10.1016/S0896-6273(01)00448-2;
RA   Hao J.C., Yu T.W., Fujisawa K., Culotti J.G., Gengyo-Ando K.,
RA   Mitani S., Moulder G., Barstead R., Tessier-Lavigne M., Bargmann C.I.;
RT   "C. elegans slit acts in midline, dorsal-ventral, and anterior-
RT   posterior guidance via the SAX-3/Robo receptor.";
RL   Neuron 32:25-38(2001).
RN   [3]
RP   INTERACTION WITH EVA-1.
RX   PubMed=25122090; DOI=10.1371/journal.pgen.1004521;
RA   Chan K.K., Seetharaman A., Bagg R., Selman G., Zhang Y., Kim J.,
RA   Roy P.J.;
RT   "EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the
RT   MADD-4 guidance cue in Caenorhabditis elegans.";
RL   PLoS Genet. 10:E1004521-E1004521(2014).
CC   -!- FUNCTION: Functions as a ligand for sax-3 receptor during larval
CC       development. Acts via the sax-3/Robo receptor to direct ventral
CC       axon guidance and guidance at the midline during embryonic
CC       development. {ECO:0000269|PubMed:11604136}.
CC   -!- SUBUNIT: Interacts with eva-1. {ECO:0000269|PubMed:25122090}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
DR   EMBL; Z69792; CAA93668.3; -; Genomic_DNA.
DR   EMBL; AL022270; CAA93668.3; JOINED; Genomic_DNA.
DR   PIR; D89711; D89711.
DR   PIR; T22025; T22025.
DR   RefSeq; NP_510437.2; NM_078036.5.
DR   UniGene; Cel.16941; -.
DR   ProteinModelPortal; G5EFX6; -.
DR   BioGrid; 46459; 1.
DR   STRING; 6239.F40E10.4; -.
DR   EPD; G5EFX6; -.
DR   PaxDb; G5EFX6; -.
DR   PRIDE; G5EFX6; -.
DR   EnsemblMetazoa; F40E10.4; F40E10.4; WBGene00004854.
DR   GeneID; 181562; -.
DR   KEGG; cel:CELE_F40E10.4; -.
DR   CTD; 181562; -.
DR   WormBase; F40E10.4; CE32412; WBGene00004854; slt-1.
DR   eggNOG; KOG4237; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   GeneTree; ENSGT00940000167217; -.
DR   InParanoid; G5EFX6; -.
DR   KO; K06839; -.
DR   OMA; IRCKHGK; -.
DR   OrthoDB; 28488at2759; -.
DR   PhylomeDB; G5EFX6; -.
DR   Reactome; R-CEL-376176; Signaling by ROBO receptors.
DR   Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR   Reactome; R-CEL-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-CEL-8985586; SLIT2:ROBO1 increases RHOA activity.
DR   PRO; PR:G5EFX6; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00004854; Expressed in 4 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005576; C:extracellular region; ISS:WormBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:WormBase.
DR   GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR   GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:WormBase.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IGI:WormBase.
DR   GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR   GO; GO:1905489; P:regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR   GO; GO:0097374; P:sensory neuron axon guidance; IMP:UniProtKB.
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; 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; 3.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF13855; LRR_8; 5.
DR   Pfam; PF01462; LRRNT; 2.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00369; LRR_TYP; 15.
DR   SMART; SM00082; LRRCT; 4.
DR   SMART; SM00013; LRRNT; 4.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 7.
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   Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; Leucine-rich repeat; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17   1410       Slit homolog 1 protein.
FT                                /FTId=PRO_0000420958.
FT   DOMAIN       17     43       LRRNT 1.
FT   REPEAT       22     42       LRR 1.
FT   REPEAT       43     66       LRR 2.
FT   REPEAT       67     90       LRR 3.
FT   REPEAT       91    114       LRR 4.
FT   REPEAT      116    138       LRR 5.
FT   REPEAT      140    162       LRR 6.
FT   REPEAT      163    186       LRR 7.
FT   DOMAIN      195    243       LRRCT 1.
FT   REPEAT      219    242       LRR 8.
FT   DOMAIN      259    286       LRRNT 2.
FT   REPEAT      286    309       LRR 9.
FT   REPEAT      310    333       LRR 10.
FT   REPEAT      335    357       LRR 11.
FT   REPEAT      358    381       LRR 12.
FT   REPEAT      383    405       LRR 13.
FT   REPEAT      407    430       LRR 14.
FT   DOMAIN      417    466       LRRCT 2.
FT   REPEAT      442    465       LRR 15.
FT   DOMAIN      484    511       LRRNT 3.
FT   REPEAT      489    510       LRR 16.
FT   REPEAT      511    535       LRR 17.
FT   REPEAT      536    559       LRR 18.
FT   REPEAT      561    583       LRR 19.
FT   REPEAT      585    607       LRR 20.
FT   DOMAIN      619    671       LRRCT 3.
FT   DOMAIN      677    703       LRRNT 4.
FT   REPEAT      681    703       LRR 21.
FT   REPEAT      704    726       LRR 22.
FT   REPEAT      727    750       LRR 23.
FT   REPEAT      752    774       LRR 24.
FT   REPEAT      775    798       LRR 25.
FT   REPEAT      800    823       LRR 26.
FT   DOMAIN      810    859       LRRCT 4.
FT   DOMAIN      871    906       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      908    945       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      947    983       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      985   1023       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1025   1061       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1072   1109       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1112   1285       Laminin G-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REPEAT     1197   1221       LRR 27.
FT   DOMAIN     1288   1326       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1332   1406       CTCK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00039}.
FT   DISULFID    873    884       {ECO:0000250}.
FT   DISULFID    878    894       {ECO:0000250}.
FT   DISULFID    896    905       {ECO:0000250}.
FT   DISULFID    912    923       {ECO:0000250}.
FT   DISULFID    917    933       {ECO:0000250}.
FT   DISULFID    935    944       {ECO:0000250}.
FT   DISULFID    951    962       {ECO:0000250}.
FT   DISULFID    956    971       {ECO:0000250}.
FT   DISULFID    973    982       {ECO:0000250}.
FT   DISULFID    989   1002       {ECO:0000250}.
FT   DISULFID    996   1011       {ECO:0000250}.
FT   DISULFID   1013   1022       {ECO:0000250}.
FT   DISULFID   1029   1040       {ECO:0000250}.
FT   DISULFID   1034   1049       {ECO:0000250}.
FT   DISULFID   1051   1060       {ECO:0000250}.
FT   DISULFID   1076   1086       {ECO:0000250}.
FT   DISULFID   1081   1097       {ECO:0000250}.
FT   DISULFID   1099   1108       {ECO:0000250}.
FT   DISULFID   1259   1285       {ECO:0000250}.
FT   DISULFID   1292   1302       {ECO:0000250}.
FT   DISULFID   1297   1314       {ECO:0000250}.
FT   DISULFID   1316   1325       {ECO:0000250}.
FT   DISULFID   1332   1368       {ECO:0000250}.
FT   DISULFID   1346   1382       {ECO:0000250}.
FT   DISULFID   1357   1398       {ECO:0000250}.
FT   DISULFID   1361   1400       {ECO:0000250}.
SQ   SEQUENCE   1410 AA;  158223 MW;  D33716A9C98EBA9D CRC64;
     MLICFIFILL IPESATCPAE CVCVDRTVSC VGQQLTEVPQ NIPNDTIRLD LQDNEITKIG
     PNDFSSLMNL KALQLMDNQI VTIHNQSFSS LVFLQKLRLS RNRIRHLPDN VFQNNLKLTH
     LDLSENDITV VSDAQLQGPE FLEVLNLDKN HIFCLENNVI SSWVSLEVLT LNGNRLTTFE
     EPSNARFRQL DLFNNPWNCD CRLRWMRKWL EKAEGQNKTV CATPLNLQGS SIEILQDKFM
     TCSGNRKRRY KKTCETAEIC PLPCTCTGTT VDCRDSGLTY VPTNLPPSTT EIRLEQNQIS
     SIPSHSFKNL KNLTRLDLSK NIITEIQPKA FLGLHNLHTL VLYGNNITDL KSDTFEGLGS
     LQLLLLNANQ LTCIRRGTFD HVPKLSMLSL YDNDIKSISE VTFQNLTSLS TLHLAKNPLI
     CDCNLQWLAQ INLQKNIETS GARCEQPKRL RKKKFATLPP NKFKCKGSES FVSMYADSCF
     IDSICPTQCD CYGTTVDCNK RGLNTIPTSI PRFATQLLLS GNNISTVDLN SNIHVLENLE
     VLDLSNNHIT FINDKSFEKL SKLRELRLND NKLHHFSSMV LDEQSNLEIL DLSGNNIQCF
     SSIFFNKATR IREIKVIGND LLCDCRILPL MSWLRSNSSH SIDIPPCQQF QYSDNESDKQ
     RCAAFPEETC SDDSNLCPPK CSCLDRVVRC SNKNLTSFPS RIPFDTTELY LDANYINEIP
     AHDLNRLYSL TKLDLSHNRL ISLENNTFSN LTRLSTLIIS YNKLRCLQPL AFNGLNALRI
     LSLHGNDISF LPQSAFSNLT SITHIAVGSN SLYCDCNMAW FSKWIKSKFI EAGIARCEYP
     NTVSNQLLLT AQPYQFTCDS KVPTKLATKC DLCLNSPCKN NAICETTSSR KYTCNCTPGF
     YGVHCENQID ACYGSPCLNN ATCKVAQAGR FNCYCNKGFE GDYCEKNIDD CVNSKCENGG
     KCVDLINSYR CDCPMEYEGK HCEDKLEYCT KKLNPCENNG KCIPINGSYS CMCSPGFTGN
     NCETNIDDCK NVECQNGGSC VDGILSYDCL CRPGYAGQYC EIPPMMDMEY QKTDACQQSA
     CGQGECVASQ NSSDFTCKCH EGFSGPSCDR QMSVGFKNPG AYLALDPLAS DGTITMTLRT
     TSKIGILLYY GDDHFVSAEL YDGRVKLVYY IGNFPASHMY SSVKVNDGLP HRISIRTSER
     KCFLQIDKNP VQIVENSGKS DQLITKGKEM LYIGGLPIEK SQDAKRRFHV KNSESLKGCI
     SSITINEVPI NLQQALENVN TEQSCSATVN FCAGIDCGNG KCTNNALSPK GYMCQCDSHF
     SGEHCDEKRI KCDKQKFRRH HIENECRSVD RIKIAECNGY CGGEQNCCTA VKKKQRKVKM
     ICKNGTTKIS TVHIIRQCQC EPTKSVLSEK
//
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