ID A0A452G720_CAPHI Unreviewed; 1333 AA.
AC A0A452G720;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Slit guidance ligand 2 {ECO:0000313|Ensembl:ENSCHIP00000032267.1};
GN Name=SLIT2 {ECO:0000313|Ensembl:ENSCHIP00000032267.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000032267.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000032267.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000032267.1}
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}.
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; LWLT01000006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000040142.1; ENSCHIP00000032267.1; ENSCHIG00000026290.1.
DR GeneTree; ENSGT00940000158402; -.
DR OMA; CQAIRCK; -.
DR Proteomes; UP000291000; Chromosome 6.
DR Bgee; ENSCHIG00000026290; Expressed in frontal cortex and 15 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; 8.
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; IPR003645; Fol_N.
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; 5.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00365; LRR_SD22; 6.
DR SMART; SM00369; LRR_TYP; 11.
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; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 9.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 723..758
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 760..799
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 801..837
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 839..877
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 879..915
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 924..960
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 963..1137
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1141..1172
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1175..1211
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1216..1252
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1257..1332
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 748..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 789..798
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 827..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 867..876
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 905..914
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 950..959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1162..1171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1179..1189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1201..1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1220..1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1242..1251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1333 AA; 147712 MW; 9BED60C574CC4FE9 CRC64;
MPKLRTFRLH SNNLYCDCHL AWLSDWLRQR PRVGLYTQCM GPSHLRGHNV AEVQKREFVC
SGHQSFMAPS CSVLHCPAAC TCSNNIVDCR GKGLTEIPTN LPETITEIRL EQNSIKVIPP
GAFSPYKKLR RIDLSNNQIS ELAPDAFQGL RSLNSLVLYG NKITELPKSL FEGLFSLQLL
LLNANKINCL RVDAFQDLHN LNLLSLYDNK LQTIAKGTFS PLRAIQTMHL AQNPFICDCH
LKWLADYLHT NPIETSGARC TSPRRLANKR IGQIKSKKFR CSAKEQYFIP GTEDYRSKLS
GDCFADLACP EKCRCEGTTV DCSNQKLTKI PDHIPQYTAE LRLNNNEFTV LEATGIFKKL
PQLRKINFSN NKITDIEEGA FEGASGVNEI LLTSNRLENV QHKMFKGLES LKTLMLRSNR
ISCVGNDSFI GLSSVRLLSL YDNQITTIAP GAFDTLHSLS TLNLLANPFN CNCYLAWLGE
WLRKKRIVTG NPRCQKPYFL KEIPIQDVAI QDFTCDDGND DNSCSPLSRC PAECTCLDTV
VRCSNKALKV LPKGIPRDVT ELYLDGNQFT LVPKELSNYK HLTLIDLSNN RISTLSNQSF
SNMTQLLTLI LSYNRLRCIP PRTFDGLKSL RLLSLHGNDI SVVPEGAFND LAALSHLAIG
ANPLYCDCNM QWLSDWVKSE YKEPGIARCA GPGEMADKLL LTTPSKKFTC QGPVDVTILA
KCNPCLSNPC KNDGTCNNDP VDFYRCTCPY GFKGQDCDVP IHACISNPCK HGGTCHLKEG
EKDGFWCICA DGFEGENCEI NVDDCEDNDC ENNSTCVDGI NNYTCLCPPE YTGELCEEKL
DFCAQDLNPC QHDSKCILTP KGYKCDCTPG YIGEHCDIDF DDCQDNKCKN GAHCTDAVNG
YTCTCPEGYS GLFCEFSPPM VLPRTSPCDN FDCQNGAQCI IRINEPICQC LPGYQGEKCE
KLVSVNFVNK ESYLQIPSAK VRPQTNITLQ IATDEDSGIL LYKGDKDHIA VELYRGRVRA
SYDTGSHPAS AIYSVETIND GNFHIVELLA LDQSLSLSVD GGSPKIITNL SKQSTLNFDS
PLYVGGMPGK NNVAAALRQA PGQNGTSFHG CIRNLYINSE LQDFRKVPMQ TGILPGCEPC
HKKVCAHGTC QPSSQAGFTC ECEEGWTGPL CDQRTNDPCL GNKCVHGTCL PINAFSYSCK
CLEGHGGVLC DEEEDLFNPC QAIKCKHGKC RLSGLGQPYC ECSSGYTGDS CDREISCRGE
RIRDYYQKQQ GYAACQTTKK VSRLECRGGC AGGQCCGPLR SKRRKYSFEC TDGSSFVDEV
EKVVKCGCTR CTS
//