ID A0A1I8IV05_9PLAT Unreviewed; 1002 AA.
AC A0A1I8IV05;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Slit homolog 2 (Drosophila) {ECO:0000313|WBParaSite:maker-uti_cns_0017193-snap-gene-0.2-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0017193-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0017193-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I8IV05; -.
DR WBParaSite; maker-uti_cns_0017193-snap-gene-0.2-mRNA-1; maker-uti_cns_0017193-snap-gene-0.2-mRNA-1; maker-uti_cns_0017193-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
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; 7.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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 PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 3.
DR SMART; SM00013; LRRNT; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
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; 6.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 406..441
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 511..547
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 549..587
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 589..627
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 644..680
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 684..861
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 867..907
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 911..986
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 431..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 537..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 577..586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 617..626
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 670..679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 834..861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 897..906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1002 AA; 112111 MW; 0DB176971EAC5F35 CRC64;
TIAGNPFVCD CNLRWLNDFL REHPRLASSD NVCDSPDRMA RKKLGEVASR KFRCRDGESE
ATRNAGRCEL YAECPANCKC EGDTVDCSWK RLTSLPKNLP VATRHLDLSN NLIATIEPDS
FRENSNLEVL NLSGNKLRSL DPRMLSGLDK LKILHLDLNP LHCNCHMKWL PPFAVANHQL
MRNSQPLCRS PDLLKDTPVV SLQSRHFVCQ QDPSMGCQGV PPCCSGDAVS CDHRAFCPKK
CECEGSVVRC IGQGLTEVPD HIPVDSTQLF LGQNLIEQLN FTRLNRLRNL KLLDLSHNQL
YGLKSNMFAN MSNLESLSVS FNKLACVEAR AFAGLSKLKV LGLNQNPIHC DCNVKWLIDF
FQRRGLDNGL SLCASPPDLA MKPIYHARPD DFVCTTATQL NHSKCNICST EPCLNGGTCR
TVSYDRFACD CPAGFEGKRC QNRLDACFGS PCHNQAECEV LRFGRYRLLE SSTDWPLADK
KSTKKHPPLL INYNNRCRCK IGFSGTHCET NIDDCIGHRC QNNATCLDGV NNYTCSCSPG
FTGRYCETRL HYCTHYNPCQ NGGECLTDPA IGYRCKCVTG WEGRNCDTNP DNCRRQTQPC
MNGGSCIDGI GSYTCQCRPG YTGRLCERLE MASLIMDVPD AAVNRGVCTH HECLNGGRCI
QEGSEYRCQC LAGYEGKKCE KLTQVGFYDD SFARIETSRI YPSGNITMEM ATQQRQGLLL
YAGNASAYLI MSLFNGYIRF SYSLGVAPGA NGYTYVKIND GKFHTVQAII NRETVTLSVD
GMAKTISATY VADAVARSVD ALSEAIYIGT LPAAKRDDMQ SNVNIRETFS FGGCVKRMLV
NGKLVNFKLS DPTNRRLIAG CPAFAKPANP CEKPNLCKNR GVCQPRVEQP AGYRCKCRPN
FTGRNCEEKA CKRLASREYY TDPETGCRSR RKLKIRRCQG TCLRSTGYCC QPKRLRHRMI
KFLCPGGRRI TKRVTLVRRC GCAPCGRHNL YSYWYHRTRA RR
//
