ID A0A3B3VJN3_9TELE Unreviewed; 1297 AA.
AC A0A3B3VJN3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Slit homolog 1 protein-like {ECO:0000313|Ensembl:ENSPLAP00000025127.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000025127.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000025127.1}
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 Ensembl; ENSPLAT00000001652.1; ENSPLAP00000025127.1; ENSPLAG00000000788.1.
DR GeneTree; ENSGT00940000157322; -.
DR Proteomes; UP000261500; Unplaced.
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; 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; 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; 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:SF3; SLIT HOMOLOG 1 PROTEIN; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 2.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00282; LamG; 1.
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; 5.
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; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 3.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 690..725
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 727..765
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 767..803
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 805..843
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 845..881
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 886..922
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 925..1099
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1174..1209
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1214..1297
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 715..724
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 736..753
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 755..764
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 793..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 833..842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 871..880
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 912..921
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1178..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1199..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1297 AA; 141741 MW; ABE2F4B5CC5FAAAF CRC64;
GATDIKNLQL DKNHITCIEE GAFRALRSLE VLTMNNNNIS SIPVSSFNHM PKLRTFRLHS
NALRCDCHLA WLSPWLRQRS ALGLYTQCSS PPALRGLNLA ELRKSDFACS GHSGSAFVQP
CSLASGSCPP MCSCSNNIVN CRGRGLTAIP AHLPEAMTEI RLEQNGIKSV PPGAFTSYKK
LHRIDLSNNQ ISEIAPDAFH GLRALNSLVL YGNKITELPS GVFDGLVSLE LLLLNANKIH
CIRAAAFKDL ENLALLSLYD NKIQSLAKGT FSSLHSIQTL HLAQNPFVCD CHVKWLADFL
GSNPIETSGA RCASPRRLAN KRIAQIKSHK FRCSAKEQYH IPGTEDRRLS YDCNSKPVCP
AKCRCEANVV DCSNLRLTKF PEHLLPSTEE LRLNNNDLSM LEATGAFKGL SHLKKINLSN
NKISEIEDGA FEGASSVGEL HLTANHLESV RGSMFRGMEG LRMLMLRNNR ISCIHNSSFT
GLPNVRLLSL YDNQLTTILP GAFDTLPNLS TLNLLANPFT CDCHLSWFGA WLRSRRIVTG
NPRCQSPAFL RGIPLQDVAV PDFRCEDVLE DRSCVAGPQC PSQCSCMDTV VRCSNKHLQA
LPRGLPRNIT ELVSSSSLSC CLFRAIGANP LYCDCRLLWL SDWVKSGYKE PGIARCAGPR
GLEGKLLLTT PADKFQCLGE RTGSASAKCT PCVSSPCQNQ GTCQIHQSQQ YTCACKSGFT
GKHCETPVDA CVSNPCTNGG SCLRDEQTGG FSCACAFGFH GTFCEVNVDD CEDHGCDNGA
TCVDGVGNYT CLCPPNYRGL LCEEEDDVCS PGRNPCQHQS TCISSPTGPR CVCIPGWVGP
DCGIDYNECA DHRCQNSAQC IDHLDGYSCV CPQGFSGEFC EVTDLQQTPC QMAKCQNGAP
CNDKLGTAIC QCPPGFEGQS CEKLVSVNFV DRDSYVELQD VKNWPQSNIT LQVSTAEDNG
ILLYNGDHEP IAVELHQGHV RVTYDPGNQP ATAIYSSETV NDGNFHTVEL VTFNQMVNLS
VDGGEPTTLD SQGRGQPLTG ETPLYVGGMP EEVIPSSRGL SSQSLNTSSF HGCIRNLYIN
HELQDFTRSQ MKPGVVPGCQ PCRKLYCLHG ICQPNSAQVT THRAVTVFLI NVLNQMSWNS
KCVKGACVAL DAQTYRCECE KGFRGALCHL QEEPAGPCQR LQCLHGRCQK TEDGESCVCD
QGYTGESCAT ETPCRGEPVR DYHRLQHGSV LCQTSKPFSW VDCRGHCRAE AERGAAAVSC
CAPLRVRRRR ITFECDDGTS FTQDVEKPVE CGCKDCV
//
