ID F6VS40_CALJA Unreviewed; 1534 AA.
AC F6VS40; U3EI69;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Slit guidance ligand 1 {ECO:0000313|Ensembl:ENSCJAP00000030366.4};
DE SubName: Full=Slit homolog 1 protein {ECO:0000313|EMBL:JAB21630.1};
GN Name=SLIT1 {ECO:0000313|EMBL:JAB21630.1,
GN ECO:0000313|Ensembl:ENSCJAP00000030366.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000030366.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000030366.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB21630.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hippocampus {ECO:0000313|EMBL:JAB21630.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000030366.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; GAMS01001506; JAB21630.1; -; mRNA.
DR STRING; 9483.ENSCJAP00000030366; -.
DR Ensembl; ENSCJAT00000032088.5; ENSCJAP00000030366.4; ENSCJAG00000036372.4.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000157322; -.
DR HOGENOM; CLU_001431_2_0_1; -.
DR OMA; ETKCQNN; -.
DR TreeFam; TF332887; -.
DR Proteomes; UP000008225; Chromosome 12.
DR Bgee; ENSCJAG00000036372; Expressed in frontal cortex and 3 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048495; F:Roundabout binding; IEA:Ensembl.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 6.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; IPR003645; Fol_N.
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 PANTHER; PTHR45836:SF4; PROTEIN SLIT; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 6.
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; 7.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 19.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041117931"
FT DOMAIN 927..962
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 964..1003
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1005..1041
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1043..1081
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1083..1119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1127..1163
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1166..1339
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1340..1374
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1377..1413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1418..1454
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1459..1534
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 952..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 993..1002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1031..1040
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1071..1080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1109..1118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1153..1162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1342..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1381..1391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1403..1412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1422..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1444..1453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1534 AA; 168079 MW; 62FABD7AD21FB01B CRC64;
MALTPGRGSS AGRVRPELWM LLWAAAWRLG ASACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LHMLPELLFQ NNQALSRLDL SENAIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKSE FSCSGPGEAG RVPTCTLSSG SCPAMCTCSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ASMVECSSLK LTKIPERIPQ
STAELRLNNN EISILEATGM FKKLTHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIT TVSPGAFDTL
QSLSTLNLLA NPFNCNCQLA WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEGGCLP RPQCPQECAC LDTVVRCSNK HLRALPRGVP KNVTELYLDG NQFTLVPGQL
FTFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDISTLREG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPPDME
GKLLLTTPAK KFECQGPPTL AVQAKCDPCL SSPCQNQGTC HNDPLEVYRC ACPSGYKGRD
CEVSLDSCSS GPCENGGTCH AQEDEDAPFT CSCPTGFEGP TCGVNTDDCV EHACANGGIC
VDGVGNYTCQ CPLQYEGRAC EQLVDLCSPD LNPCQHKAQC VGTPDGPRCE CVPGYAGDNC
SENQDDCRDH RCQNGAQCVD EVNSYSCLCA EGYSGQLCEI PPHPPAPKSP CEGTECQNGA
NCVDQGNRPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN
GILLYNGDND HIAVELYQGH VRVSYDPGSY PSSAIYSAET INDGQFHTVE LVAFDQMVNL
SIDGGSPMTM DNFGKHYTLN SEAPLYVGGM PVDINSAAFR LWQILNGTSF HGCIRNLYIN
NELQDFTKTQ MKPGVVPGCE PCRKLYCLHG ICQPNATPGP TCHCEAGWGG LHCDQPTDGP
CHGHKCVHGQ CVPLDALSYS CQCQDGYSGA LCNQAGAPAE PCRGLQCLHG HCQASATKGA
HCVCDPGFSG ELCEQESECR GDPVRDFHQV QRGYAVCRTT RPLSWVECQG SCPGQGCCQG
LRLKRRKFTF ECSDGTSFAE EVEKPTKCGC ALCA
//
