ID A0A226DET4_FOLCA Unreviewed; 1289 AA.
AC A0A226DET4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein slit {ECO:0000313|EMBL:OXA44085.1};
GN ORFNames=Fcan01_21329 {ECO:0000313|EMBL:OXA44085.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA44085.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA44085.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA44085.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA44085.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OXA44085.1}.
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; LNIX01000020; OXA44085.1; -; Genomic_DNA.
DR STRING; 158441.A0A226DET4; -.
DR OMA; ACAYGFH; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 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; IPR001791; Laminin_G.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; 4.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 3.
DR Pfam; PF01462; LRRNT; 3.
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; 9.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF52058; L domain-like; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 6.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 731..766
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 768..805
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 807..843
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 845..883
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 885..921
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 932..971
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 974..1147
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1184..1221
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1226..1289
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 756..765
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 795..804
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 833..842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 873..882
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 911..920
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 936..946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 961..970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1188..1198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1211..1220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1289 AA; 144411 MW; E21995B076FAA5E8 CRC64;
MLDHNHLTCI DEAAIRPLRD LEVLTLENNN LTSLHKDAFE GLVKLKHFSL GNNPLICDCH
LGWLTRWLRR APKSVSQARC NSPYHLRDRT IDEVLESEFK CAGVVERKWN KCGGDENCPH
PCVCADGVVD CRDLTLKSVP DSLPEDVIEL RLEQNEITEI PPGAFSSYKR LRRLDLSNNQ
IQKIAVDAFR NLKSMTSLVL YGNRITVLPP GIFNGLSSLQ LLLLNANRIT CIRRDTFQDL
NNLSLLSLYD NKIQSLENGT FEALRNIQTL HLARNPFHCD CRLRWLSDYL HGNPIETSGA
RCEAPKRMQR KRLASFREDK MKCDEEDSKT WIDECADIKC PVECVCEGGV VDCSNRAFRE
IPQDIPEQVT HLCLSGNNLS RIRNGWISLL PNLQKLDLSG NRISAIEDGA FRDASSLQEV
AISGNKLKEI NNKMFLGLTH LKTLSLADNH ISCIMPGSFD SLSNLQSLDL DGNAFICNCH
LAWFADWLRR EESLFPSSGP KCVAPMRHKD TLIRSLPTHE FRCTSDDRGC LGEEYCPPQC
NCTGTVVWCS RSSLREIPSG IPAATSELYL DVNEIQRIDL SRIRHLKYLT KLDLSNNQIT
MISNHTFANL TKLSTLIISY NRLQCIERDA LAGLTALRIL SIHANEISMI PEGTFRDLRA
ITHLALGGNP LFCDCGLKWL ADWVKRDFLE PGIARCSEPE SMRNKLILTT PPGDFECWKD
SIPASIQAKC DACYNFPCSN GATCRTMPDR GFECECTPGY HGRHCEQVID ACYGQPCINA
GTCKVMEEGR FSCLCRAGFI GHRCETNQDD CVGHKCENNA TCVDLIGHYK CQCPLGFTGE
YCEKKIPFCT KDFNPCKNGA KCVDHFTHHT CECPIGYQGE NCSINIDDCL NNMCQNGGTC
VDGINEYTCQ CTEEFSGRYC EVSPSVAMLY PKTSPCQDND CLHGFCFLPP DSNPPDPVCF
CEAGYTGKRC EFLTSISIGS NGSWVELEPL RTKPEANITL MLSTTELNGV LLYDGEGQHI
AVELFLGRIR VSYDVGNYPA STMYSYEMIA DGEEHRVELL AIKKNFTMRV DGGKARSIIN
DGEKDMLKLT TPLFIGGLPS NVAATALNLW HLRNSTSFHG CLSTVIINHK RVDYSNAKRQ
QGIVPGCAAI QGEEPERQPT PPAVKDVTPT QIQSSFISKI VKEARDVCKD HRCKNGRCLP
SKNGGSYFCR CTPGYGGRFC DEAPTCKKEQ YKDYYTEHGC RSRRPLKIAA CVGSCGDTCC
TPKRSRRRRV RLICNDGTRY TKDVEIIRK
//
