ID A0A1S3AC89_ERIEU Unreviewed; 1535 AA.
AC A0A1S3AC89;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Slit homolog 1 protein isoform X3 {ECO:0000313|RefSeq:XP_007532719.1};
GN Name=SLIT1 {ECO:0000313|RefSeq:XP_007532719.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007532719.1};
RN [1] {ECO:0000313|RefSeq:XP_007532719.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_007532719.1; XM_007532657.2.
DR GeneID; 103122076; -.
DR CTD; 6585; -.
DR eggNOG; KOG4237; Eukaryota.
DR InParanoid; A0A1S3AC89; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; 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; IPR003645; Fol_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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:SF4; PROTEIN SLIT; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 6.
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; 8.
DR SMART; SM00274; FOLN; 2.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00368; LRR_RI; 4.
DR SMART; SM00365; LRR_SD22; 7.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
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; 9.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 9.
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 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:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1535
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010211637"
FT DOMAIN 927..962
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 964..1003
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1005..1041
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1043..1081
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1083..1119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1127..1163
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1166..1339
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1340..1374
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1377..1413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1418..1454
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1459..1535
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 952..961
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 993..1002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1031..1040
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1071..1080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1109..1118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1153..1162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1342..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1381..1391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1403..1412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1422..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1444..1453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1535 AA; 167595 MW; A75E047EC84CA6FC CRC64;
MALTAHGARS AGRLGPALWL LFCTAAWRPG AWACPALCTC SGTTVDCHAA GLQAVPRNIP
RGTERLELNG NNITRIHRND FAGLKQLRVL QLMENQITVV ERGAFDDMKE LERLRLNRNL
LHMLPELLFQ NNQALSRLDL SENTIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPAGLRG LNVAEVQKSE FSCSGQGEAG RMPSCTLSSG SCPAMCACSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQILEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ASMVECSSLK LTKIPERIPQ
ATAELRLNNN EISILEATGM FKKLSHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIA TISPGAFDTL
QALSTLNLLA NPFNCNCQLA WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEGGCLP RPQCPQECSC LDTVVRCSNK HLQALPKGLP KNVTELYLDG NQFTLVPGQL
STFKFLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LSSLRLLSLH
GNDISTLPEG IFADVTALSH LAIGANPLYC DCHLRWLSGW VKTGYKEPGI ARCAGPPDME
GKLLLTTPAK KFECQGPPTL DVLAKCDPCL SSPCQNQGTC HKDPQEVHRC VCPSGYMGRD
CEVSLDSCSS GPCANGGSCH MQEGEDAGFT CSCPAGFEGP TCGVNVDDCV EHACANGGTC
VDGVGNYTCQ CPLQYSGRAC EQLVDFCAPE RNPCQHQARC VGTPDGPRCE CVPGYTGDNC
SENRDDCRDH RCQNGASCVD QVNSYACVCA EGYSGQFCEL TPRPPAPKIP CEGTECQNGA
NCVNQGSQPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN
GILLYNGDND HMAVELYQGH VRVSYDPGSS PSSAIYSAET INDGQFHTVE LVTFDQMVNL
SIDGGSPMTM DNFGKHSTLN SEAPLYVGGM PVDVNSAAFR LWQILNGSSF HGCIRNLYIN
NELQDFTKTR MKPGVVPGCE PCRKLYCLHG ICQPNATPGP VCHCEAGWGG PHCDQPAEGP
CHGHKCVHGK CVPLDALSYS CQCQDGYSGA LCNQAGPPAD ACGALQCLHG HCQASATKGA
QCVCDSGFSG KLCEQESECR GDPVRDFHQV QRGYAICQTT RPLSWVECRG SCPGRGCCQG
LRLKRRKFAF ECSDGTSFAE EVEKPTKCGC ATKCG
//
