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Database: UniProt
Entry: A0A1S3RUN1_SALSA
LinkDB: A0A1S3RUN1_SALSA
Original site: A0A1S3RUN1_SALSA 
ID   A0A1S3RUN1_SALSA        Unreviewed;      1532 AA.
AC   A0A1S3RUN1;
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 X1 {ECO:0000313|RefSeq:XP_014055552.1};
GN   Name=LOC106604933 {ECO:0000313|RefSeq:XP_014055552.1};
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_014055552.1};
RN   [1] {ECO:0000313|RefSeq:XP_014055552.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055552.1};
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_014055552.1; XM_014200077.1.
DR   STRING; 8030.ENSSSAP00000045214; -.
DR   PaxDb; 8030-ENSSSAP00000045214; -.
DR   Ensembl; ENSSSAT00000072027; ENSSSAP00000045214; ENSSSAG00000044758.
DR   GeneID; 106604933; -.
DR   KEGG; sasa:106604933; -.
DR   OMA; PACNANS; -.
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; 5.
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; 8.
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..1532
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010331900"
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          1041..1079
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1081..1117
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1126..1162
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1165..1339
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1376..1411
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1415..1451
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1456..1531
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        1069..1078
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1107..1116
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1152..1161
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1312..1339
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT   DISULFID        1380..1390
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1401..1410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1419..1429
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1441..1450
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1532 AA;  168423 MW;  5D11687C346BA54A 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
     CPPNYTADRY DMGKGDLCEE VVDPCMQGFD PCQHDSKCIP LTKGFRCECL PGYVGQHCEQ
     DYNDCLENKC QHGAECVDAV NGYTCVCKEG FSGLFCENPP PMILLQTSPC DQSECQNGAQ
     CLVVEGEPVC RCLPGFTGNK CHKIVTVHLL GKETYLELPS IKIRNSVHIS LQVATDKDNG
     ILLYKEDHDP LALELYQGHI RIIYDIANYP PTTVYSVESV SDGLFHTVEL LIQNHSLSLV
     VDKGSPKSLG KLPRQPSVDH NTQLYIGGVP SAVMASRLRS GPDRSPQAFN GCIHNVRING
     ELQDLGAALR GLEGILPGCH SCSVCAQGAC RQRGETGVSC ECPPSRSGPL CDQKIAPSPC
     QSSRCVHGLC VPKASSYSCH CADGYTGQYC DRREEPQACK GHQCGHGECR VTESGEPSCH
     CQPGYTGPTC DAEPACQGEV VRELLKRHQP MKTCTSTSKI PRVECPRACD GGFCCAPSKS
     RRRKVVFKCT DGSSYSEEME TTLECGCAKC PL
//
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