ID A0A2K5C380_AOTNA Unreviewed; 1530 AA.
AC A0A2K5C380;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Slit guidance ligand 3 {ECO:0000313|Ensembl:ENSANAP00000003156.1};
GN Name=SLIT3 {ECO:0000313|Ensembl:ENSANAP00000003156.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000003156.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000003156.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 37293.ENSANAP00000003156; -.
DR Ensembl; ENSANAT00000020768.1; ENSANAP00000003156.1; ENSANAG00000019388.1.
DR GeneTree; ENSGT00940000159322; -.
DR Proteomes; UP000233020; Unplaced.
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:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0061364; P:apoptotic process involved in luteolysis; IEA:Ensembl.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051414; P:response to cortisol; IEA:Ensembl.
DR GO; GO:0035385; P:Roundabout signaling pathway; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 4.
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; 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 PANTHER; PTHR45836:SF23; LRRCT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 6.
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; 8.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00368; LRR_RI; 6.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
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; 7.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 5.
PE 4: Predicted;
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:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014366096"
FT DOMAIN 925..960
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 962..1001
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1003..1039
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1041..1079
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1081..1117
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1126..1162
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1165..1339
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1375..1410
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1415..1451
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1456..1530
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 950..959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 991..1000
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1029..1038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1069..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1107..1116
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1152..1161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1312..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 1379..1389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1400..1409
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1419..1429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1441..1450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1530 AA; 168307 MW; 6EE5C6EB549E379B CRC64;
MAPGRTGVGA AVRARLALAL ALASVLSGPP TVACPTKCTC SAASVDCHGL GLRAVPRGIP
RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
LQVLPELLFQ STPKLSRLDL SENQIQGIPR KAFRGITDVK NLQLDNNHIS CIEDGAFRAL
RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTVGQFT
LCMAPVHLRG FNVADVQKKE YVCPGPHSEP PSCNANSISC PSPCTCSNSI VDCRGKGLTE
IPANLPEGIV EIRLEQNSIK SIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
VLYGNKITEI AKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
KKFRCSGSED YRSRFSSECF MDLMCPEKCR CEGTIVDCSN QKLARVPSHL PEYVTDLRLN
DNEISVLEAT GIFKKLPNLR KINLSNNKIK EVREGAFDGA ASVQELMLTG NQLEAVHGRM
FRGLSGLKTL MLRSNLISCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
LSNPFNCNCH LAWLGKWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNDESSCQ
LSPRCPEQCT CVETVVRCSN KGLRALPKGM PKDVTELYLE GNHLTAVPRE LSALRHLTLI
DLSNNSISVL TNYTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPEPM ADRLLLTTPT
HRFQCKVLWF CCLGPVDINI AAKCNACLSG PCKNNGSCTQ DPVELYRCAC PYSYKGKDCT
VPINTCIQNP CQHGGTCHLS DSHKDGFSCS CPLGFEGQRC EINPDDCEDN DCENNATCVD
GINNYACICP PNYTGELCDE VIDHCVPELN LCQHEAKCIP LDKGFRCECV PGYSGKLCET
DNDDCVAHKC RHGAQCVDAV NGYTCTCPQG FSGLFCEHPP PMVLLQTSPC DQYECQNGAQ
CIVVQQEPTC RCPSGFAGPR CEKLITVNFV GKDSYVELAS AKVRPQANIS LQVATDKDNG
ILLYKGDNDP LALELYQGHV RLVYDSLSSP PTTVYSVETV NDGQFHSVEL VMLNQSLNLV
VDKGTPKSLG KLQKQPAVGI NSPLYLGGIP TSTGLSALRQ GTDRPLGGFH GCIHEVRINN
ELQDFKALPP QSLGVSPGCK SCTVCKHGLC RPVEKDSMVC ECHPGWTGPL CDQEARDPCL
GHSCNHGKCV ATGTSYMCKC AEGYGGALCD HKNDSANACS AFKCHHGQCH ISDQGEPYCL
CQPGFSGEHC QQENPCLGQV VREVIRRQKG YASCATASKV PIMECHGGCG PQCCQPTRSK
RRKYVFQCTD GSSFVEEVER HLECGCLVCS
//
