SLIT1_CAEEL
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 03-AUG-2022, entry version 78.
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 investigating
RT 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., Mitani S.,
RA Moulder G., Barstead R., Tessier-Lavigne M., Bargmann C.I.;
RT "C. elegans slit acts in midline, dorsal-ventral, and anterior-posterior
RT 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., 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 axon
CC guidance and guidance at the midline during embryonic development.
CC {ECO:0000269|PubMed:11604136}.
CC -!- SUBUNIT: Interacts with eva-1. {ECO:0000269|PubMed:25122090}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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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 AlphaFoldDB; G5EFX6; -.
DR SMR; G5EFX6; -.
DR BioGRID; 46459; 7.
DR STRING; 6239.F40E10.4; -.
DR EPD; G5EFX6; -.
DR PaxDb; G5EFX6; -.
DR EnsemblMetazoa; F40E10.4.1; F40E10.4.1; 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 GeneTree; ENSGT00940000167217; -.
DR HOGENOM; CLU_001431_1_0_1; -.
DR InParanoid; G5EFX6; -.
DR OMA; ETKCQNN; -.
DR OrthoDB; 28488at2759; -.
DR PhylomeDB; G5EFX6; -.
DR Reactome; R-CEL-376176; Signaling by ROBO receptors.
DR Reactome; R-CEL-9010553; Regulation of expression of SLITs and ROBOs.
DR PRO; PR:G5EFX6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004854; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:WormBase.
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; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:WormBase.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
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 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; 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 Developmental protein; Disulfide bond; EGF-like domain;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1410
FT /note="Slit homolog 1 protein"
FT /id="PRO_0000420958"
FT DOMAIN 17..43
FT /note="LRRNT 1"
FT REPEAT 22..42
FT /note="LRR 1"
FT REPEAT 43..66
FT /note="LRR 2"
FT REPEAT 67..90
FT /note="LRR 3"
FT REPEAT 91..114
FT /note="LRR 4"
FT REPEAT 116..138
FT /note="LRR 5"
FT REPEAT 140..162
FT /note="LRR 6"
FT REPEAT 163..186
FT /note="LRR 7"
FT DOMAIN 195..243
FT /note="LRRCT 1"
FT REPEAT 219..242
FT /note="LRR 8"
FT DOMAIN 259..286
FT /note="LRRNT 2"
FT REPEAT 286..309
FT /note="LRR 9"
FT REPEAT 310..333
FT /note="LRR 10"
FT REPEAT 335..357
FT /note="LRR 11"
FT REPEAT 358..381
FT /note="LRR 12"
FT REPEAT 383..405
FT /note="LRR 13"
FT REPEAT 407..430
FT /note="LRR 14"
FT DOMAIN 417..466
FT /note="LRRCT 2"
FT REPEAT 442..465
FT /note="LRR 15"
FT DOMAIN 484..511
FT /note="LRRNT 3"
FT REPEAT 489..510
FT /note="LRR 16"
FT REPEAT 511..535
FT /note="LRR 17"
FT REPEAT 536..559
FT /note="LRR 18"
FT REPEAT 561..583
FT /note="LRR 19"
FT REPEAT 585..607
FT /note="LRR 20"
FT DOMAIN 619..671
FT /note="LRRCT 3"
FT DOMAIN 677..703
FT /note="LRRNT 4"
FT REPEAT 681..703
FT /note="LRR 21"
FT REPEAT 704..726
FT /note="LRR 22"
FT REPEAT 727..750
FT /note="LRR 23"
FT REPEAT 752..774
FT /note="LRR 24"
FT REPEAT 775..798
FT /note="LRR 25"
FT REPEAT 800..823
FT /note="LRR 26"
FT DOMAIN 810..859
FT /note="LRRCT 4"
FT DOMAIN 871..906
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 908..945
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 947..983
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 985..1023
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1025..1061
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1072..1109
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1112..1285
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REPEAT 1197..1221
FT /note="LRR 27"
FT DOMAIN 1288..1326
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1332..1406
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 873..884
FT /evidence="ECO:0000250"
FT DISULFID 878..894
FT /evidence="ECO:0000250"
FT DISULFID 896..905
FT /evidence="ECO:0000250"
FT DISULFID 912..923
FT /evidence="ECO:0000250"
FT DISULFID 917..933
FT /evidence="ECO:0000250"
FT DISULFID 935..944
FT /evidence="ECO:0000250"
FT DISULFID 951..962
FT /evidence="ECO:0000250"
FT DISULFID 956..971
FT /evidence="ECO:0000250"
FT DISULFID 973..982
FT /evidence="ECO:0000250"
FT DISULFID 989..1002
FT /evidence="ECO:0000250"
FT DISULFID 996..1011
FT /evidence="ECO:0000250"
FT DISULFID 1013..1022
FT /evidence="ECO:0000250"
FT DISULFID 1029..1040
FT /evidence="ECO:0000250"
FT DISULFID 1034..1049
FT /evidence="ECO:0000250"
FT DISULFID 1051..1060
FT /evidence="ECO:0000250"
FT DISULFID 1076..1086
FT /evidence="ECO:0000250"
FT DISULFID 1081..1097
FT /evidence="ECO:0000250"
FT DISULFID 1099..1108
FT /evidence="ECO:0000250"
FT DISULFID 1259..1285
FT /evidence="ECO:0000250"
FT DISULFID 1292..1302
FT /evidence="ECO:0000250"
FT DISULFID 1297..1314
FT /evidence="ECO:0000250"
FT DISULFID 1316..1325
FT /evidence="ECO:0000250"
FT DISULFID 1332..1368
FT /evidence="ECO:0000250"
FT DISULFID 1346..1382
FT /evidence="ECO:0000250"
FT DISULFID 1357..1398
FT /evidence="ECO:0000250"
FT DISULFID 1361..1400
FT /evidence="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
