ID A0A0N1IQB9_PAPXU Unreviewed; 485 AA.
AC A0A0N1IQB9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protein slit {ECO:0000313|EMBL:KPJ20613.1};
GN ORFNames=RR46_00196 {ECO:0000313|EMBL:KPJ20613.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ20613.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPJ20613.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ20613.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ20613.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ20613.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LADI01005777; KPJ20613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IQB9; -.
DR STRING; 66420.A0A0N1IQB9; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
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; 5.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000483; Cys-rich_flank_reg_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; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45836:SF4; PROTEIN SLIT; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00054; Laminin_G_1; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 84..118
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 120..156
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 158..194
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 196..234
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 236..272
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 341..485
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 108..117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 124..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 146..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 184..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 224..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 262..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 485 AA; 52650 MW; 616B4391057B091F CRC64;
MLADGVFRDL ESISHVALGS NPLYCDCNTR WLSEWVKSAG EYVEAGIAKC AEPARMRDKL
VLSTASSAFV CTEKAPSDVV SKCDRCVRSP CANGGTCSAT RGGFSCACAR GFHGETCQQR
IDACYGAPCR HGTCTLLEEG RFHCSCEAGY TGVRCEVDID DCAGHKCQNN ATCLDHLEGY
SCKCSPGYMG EFCETKIPFC SAEFNPCENG ASCVDHGSHY TCSCPRGYAG VNCTINPDDC
LDHMCQNGAT CIDGLEEYRC ACAAGYAGRY CEAAPHAALG TSPCAHHDCV HGVCYLPAPA
PAQPAAVQDD IMMERPLLGA TNDYLCKCAP GYSGRLCEYL TSLTFNHNDS LVELEPLRTS
PQANVTLVFS TTQHHGVLLY FGDSEHLAVE LFNGRIRISY DVGNHPTSTM YSFEMVSDGS
YHKAELLAVK KNFTLKVDDG PARSIINEGT KEYLRLDRPM FLGGVPEDVA KEAFSKWHLR
NITSF
//
