ID A0A091IP68_EGRGA Unreviewed; 1145 AA.
AC A0A091IP68;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Slit 2 protein {ECO:0000313|EMBL:KFP10454.1};
DE Flags: Fragment;
GN ORFNames=Z169_02443 {ECO:0000313|EMBL:KFP10454.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP10454.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP10454.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP10454.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK500814; KFP10454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IP68; -.
DR STRING; 188379.A0A091IP68; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 4.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
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; 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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR PANTHER; PTHR45836:SF2; SLIT HOMOLOG 2 PROTEIN; 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; PF13855; LRR_8; 6.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 3.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00368; LRR_RI; 6.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 15.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF52058; L domain-like; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 4.
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}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 816..855
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 857..893
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 895..933
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 935..971
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 980..1016
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1019..1145
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 845..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 883..892
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 923..932
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 961..970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1006..1015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP10454.1"
FT NON_TER 1145
FT /evidence="ECO:0000313|EMBL:KFP10454.1"
SQ SEQUENCE 1145 AA; 127191 MW; F822F5ED6AB24E34 CRC64;
DLSENQIQAI PRKAFRGAVD IKNLQLDYNQ ISCIEDGAFR ALRDLEVLTL NNNNITRLSV
ASFNHMPKLR TFRLHSNNLY CDCHLAWLSD WLRQRPRVGL YTQCMGPSHL RGHNVAEVQK
REFVCSGHQS FMAPSCSVLH CPAACTCSNN IVDCRGKGLT EIPTNLPETI TEIRLEQNSI
KVIPPGAFSP YKKLRRIDLS NNQISEAAPD AFQGLRSLNS LVLYGNKITE LPKGLFEGLF
SLQLLLLNAN KINCLRVDAF QDLHNLNLLS LYDNKLQTIA KGTFSPLRAI QTLHLAQNPF
ICDCHLKWLA DYLHTNPIET SGARCTSPRR LANKRIGQIK SKKFRCSAKE QYFIPGTEDY
RSKLSGDCFA DLACPEKCRC EGTTVDCSNQ KLNKIPDHIP QYTAELRLNN NEFSVLEATG
IFKKLPQLRK INLSNNKITD IEEGAFDGAS GVNELLLTSN RLESVRHKMF KGLESLKTLM
LRSNRVSCVG NDSFTGLSSV RLLSLYDNQI TTVAPGSFDT LHSLSTLNLL ANPFNCNCHL
AWLGDWLRKK RIVTGNPRCQ KPYFLKEIPI QDVAIQDFTC DDGNDDNSCS PLSRCPAECT
CLDTVVRCSN KGLKALPKGI PKDVTELYLD GNQFTLVPKE LSNYKHLTLI DLSNNRISTL
SNQSFSNMTQ LLTLILSYNR LRCIPARTFD GLKSLRLLSL HGNDISVVPE GAFNDLSALS
HLAIGANPLY CDCNMQWLSD WVKSEYKEPG IARCAGPGEM ADKLLLTTPS KKFTCQEIPG
PCGFLIPGKV ITRIGMGDLI KNGPSDLPFG QDCDIPIHAC ISNPCHHGGT CHLKEGEKDG
FWCTCADGFE GENCEVNVDD CEDNDCENNS TCVDGINNYT CLCPPEYTGE LCEEKLDFCA
QNLNPCQHDS KCILTPKGYK CDCTPGYVGE HCDIDFDDCQ DNKCKNGAQC TDAVNGYTCI
CPEGYSGLFC EFSPPMVLPR TSPCDNYECQ NGAQCIIKES EPICQCLSGY QGEKCEKLIS
INFVNKESYL QIPSAKIRPQ TNITLQIATD EDSGILLYKG DKDHIAVELY RGRVRVSYDT
GSYPASAIYS VETINDGNFH IVELLAMDQI LSLSIDGGSP KIITNLSKQS TLNFDSPLYV
GGKSI
//
