ID A0A1S3RTF2_SALSA Unreviewed; 1524 AA.
AC A0A1S3RTF2;
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 3 protein-like isoform X2 {ECO:0000313|RefSeq:XP_014055553.1};
GN Name=LOC106604933 {ECO:0000313|RefSeq:XP_014055553.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014055553.1};
RN [1] {ECO:0000313|RefSeq:XP_014055553.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055553.1};
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_014055553.1; XM_014200078.1.
DR Ensembl; ENSSSAT00000072046; ENSSSAP00000045233; ENSSSAG00000044758.
DR GeneID; 106604933; -.
DR OrthoDB; 5475408at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Bgee; ENSSSAG00000044758; Expressed in pharyngeal gill and 13 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:0048513; P:animal organ development; IEA:UniProt.
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:UniProt.
DR CDD; cd00053; EGF; 1.
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; SLIT HOMOLOG; 1.
DR PANTHER; PTHR45836:SF9; SLIT HOMOLOG 3 PROTEIN; 1.
DR Pfam; PF00008; EGF; 5.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF13855; LRR_8; 6.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 4.
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; SM00368; LRR_RI; 5.
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; 4.
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; 8.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS51450; LRR; 4.
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:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1524
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010346351"
FT DOMAIN 917..952
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 954..993
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 995..1031
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1033..1071
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1073..1109
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1118..1154
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1157..1331
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1368..1403
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1407..1443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1448..1523
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT DISULFID 942..951
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 983..992
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1021..1030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1061..1070
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1099..1108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1144..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1304..1331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 1372..1382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1393..1402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1411..1421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1433..1442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1524 AA; 167486 MW; 0DCF406765DE9DB1 CRC64;
MLPTVQEKWT AYHWGIWVLM CGLLCSAAVN GCPHKCSCSG SHVDCQGQGF RTVPKGIPRN
AERLDLDRNN ITRITKVDFS GIKNLRVLHL EDNQITVIER GAFQDLKQLE RLRLNRNKLQ
VLPELLFQST PKLGRLDLSE NQIQAVPRKA FRGITTVKNL QLDSNHISCI EDGAFRALRD
LEILTLNNNN ITLIPLSSFN HMPKLRTLRL HSNNLHCDCH LSWLSDWLRQ RHGLAPFTQC
MAPASMRGLN IPDVQKKDFT CTGPAQAEPR TCVPQASVCP ISCTCNNNIV DCRHKGLTEI
PANLPEGIVE IRLEQNLIKN IPAGAFSPYK KLKRIDLSKN QISDIAADAF TGLRSLTSLV
LYGNKIAEIP KGLFDGLVSL QLLLLNANKI NCLRVNTFQD LQSLNLLSLY DNKLQTISKG
LFAPLRSIKT LHLAQNPFMC DCHLKWLADY LFDNPIETSG ARCSHPRRLA NKRISQVKGK
KFRCTGTEDY RSRLSGECFQ DLVCPEKCRC EGTVVDCSNL KLTKLPPHLP EHTTDLRLND
NEISVLEAVG TFKKLPNLKK INLSNNKLRD IREGAFDGAA GVLEVLLTGN KLQALQGRMF
RGLTGLKTLM LRSNQIGCVD NTTFTGLSSV RLLSLYDNRI STIAPGAFTT LHSLSTINLL
SNPYVCDCHL AWLGLWLKKT RVVSGNPRCQ KPAFLKEIPI QDVANPDFTC DGTEENVCFP
VSRCPESCTC SDTVVRCSNR GLRTLPKGIP KDTTELYMEG NLLISIPKEL STLKQLSLVD
LSNNSISTVA SMTFSNMTQL ATLILSYNQI RCIQVHAFDG LKSLRLLTLH GNDLSTIPEG
AFNHLTSLSH LALGANPLYC NCDLRWLSQW VKAGFKEPGI ARCTGPPDMA DRLLLTTPLN
RFQCKGPVDL NLMAKCAPCL AGPCLNNGTC ASDVSGSYHC TCPIGYKGQN CEIAINACIS
LPCANGGTCH LMPGQVEQFS CACPPGYEGL QCEVNPDDCE DNDCENNSTC VDGINNYTCV
CPPNYTGDLC EEVVDPCMQG FDPCQHDSKC IPLTKGFRCE CLPGYVGQHC EQDYNDCLEN
KCQHGAECVD AVNGYTCVCK EGFSGLFCEN PPPMILLQTS PCDQSECQNG AQCLVVEGEP
VCRCLPGFTG NKCHKIVTVH LLGKETYLEL PSIKIRNSVH ISLQVATDKD NGILLYKEDH
DPLALELYQG HIRIIYDIAN YPPTTVYSVE SVSDGLFHTV ELLIQNHSLS LVVDKGSPKS
LGKLPRQPSV DHNTQLYIGG VPSAVMASRL RSGPDRSPQA FNGCIHNVRI NGELQDLGAA
LRGLEGILPG CHSCSVCAQG ACRQRGETGV SCECPPSRSG PLCDQKIAPS PCQSSRCVHG
LCVPKASSYS CHCADGYTGQ YCDRREEPQA CKGHQCGHGE CRVTESGEPS CHCQPGYTGP
TCDAEPACQG EVVRELLKRH QPMKTCTSTS KIPRVECPRA CDGGFCCAPS KSRRRKVVFK
CTDGSSYSEE METTLECGCA KCPL
//
