P24014 (SLIT_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein slit
Short name=dSlit

Cleaved into the following 2 chains:

1. Protein slit N-product
2. Protein slit C-product

Gene names

Name:	sli
ORF Names:	CG8355

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	A short-range repellent, controlling axon crossing of the midline and a long-range chemorepellent, controlling mesoderm migration and patterning away from the midline. May interact with extracellular matrix molecules. Repulsive ligand for the guidance receptor roundabout (robo) and prevents inappropriate midline crossing by Robo-expressing axons. Ref.1 Ref.2 Ref.5 Ref.6
Subunit structure	Interacts with robo. Ref.6
Subcellular location	Secreted Ref.1 Ref.5.
Tissue specificity	In embryos, highest expression occurs around the midline glia and low expression is observed around CNS axons lateral to the midline. Expression can be seen on the commissural axons traversing the glial cells but it is absent from the cell bodies of these neurons. Ref.1 Ref.2 Ref.5
Miscellaneous	Flies lacking sli exhibit disruption of the developing midline cells and the commissural axon pathways.
Sequence similarities	Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 7 EGF-like domains. Contains 1 laminin G-like domain. Contains 19 LRR (leucine-rich) repeats. Contains 4 LRRCT domains. Contains 4 LRRNT domains.
Sequence caution	The sequence AAA72722.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Leucine-rich repeat Repeat Signal
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Roundabout signaling pathway Inferred from genetic interaction Ref.2. Source: FlyBase axon midline choice point recognition Inferred from mutant phenotype PubMed 15147761PubMed 17049509PubMed 17121810PubMed 17409115. Source: FlyBase dendrite morphogenesis Inferred from mutant phenotype PubMed 18817767. Source: FlyBase digestive tract mesoderm development Inferred from mutant phenotype PubMed 21377458. Source: FlyBase embryonic heart tube development Inferred from mutant phenotype PubMed 16360689PubMed 16516189PubMed 16888037. Source: FlyBase epithelial cell migration, open tracheal system Inferred from mutant phenotype PubMed 15229181. Source: FlyBase glial cell migration Inferred from mutant phenotype Ref.1. Source: UniProtKB gonad development Inferred from mutant phenotype PubMed 21377458. Source: FlyBase induction of negative chemotaxis Inferred from mutant phenotype Ref.1. Source: UniProtKB lateral inhibition Inferred from mutant phenotype PubMed 19363474. Source: FlyBase mesodermal cell migration Inferred from mutant phenotype Ref.2. Source: FlyBase neuron migration Inferred from mutant phenotype PubMed 15296748. Source: FlyBase outflow tract morphogenesis Inferred from mutant phenotype PubMed 18250318. Source: FlyBase positive regulation of cell-cell adhesion Inferred from mutant phenotype PubMed 16888037. Source: FlyBase regulation of epithelial cell migration, open tracheal system Inferred from mutant phenotype PubMed 12397103. Source: FlyBase salivary gland boundary specification Inferred from mutant phenotype PubMed 15950216. Source: FlyBase
Cellular_component	Slit-Robo signaling complex Inferred from direct assay PubMed 17062560. Source: FlyBase plasma membrane Traceable author statement. Source: Reactome proteinaceous extracellular matrix Traceable author statement PubMed 7760738. Source: FlyBase
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Inferred from direct assay PubMed 17062560. Source: FlyBase
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform C (identifier: P24014-1)

Also known as: E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A (identifier: P24014-2)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     152-175: Missing.

Isoform B (identifier: P24014-3)

The sequence of this isoform differs from the canonical sequence as follows:
     152-175: Missing.
     1418-1428: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 36

36

Chain

37 – 1504

1468

Protein slit

PRO_0000007719

Chain

37 – 1135

1099

Protein slit N-product By similarity

PRO_0000007720

Chain

1136 – 1504

369

Protein slit C-product By similarity

PRO_0000007721

Regions

Domain

64 – 100

37

LRRNT 1

Repeat

101 – 122

22

LRR 1

Repeat

125 – 146

22

LRR 2

Repeat

149 – 170

22

LRR 3

Repeat

173 – 194

22

LRR 4

Repeat

197 – 218

22

LRR 5

Repeat

221 – 242

22

LRR 6

Domain

254 – 304

51

LRRCT 1

Domain

310 – 346

37

LRRNT 2

Repeat

347 – 368

22

LRR 7

Repeat

371 – 392

22

LRR 8

Repeat

395 – 416

22

LRR 9

Repeat

419 – 440

22

LRR 10

Repeat

443 – 464

22

LRR 11

Domain

476 – 526

51

LRRCT 2

Domain

534 – 570

37

LRRNT 3

Repeat

571 – 592

22

LRR 12

Repeat

596 – 617

22

LRR 13

Repeat

620 – 641

22

LRR 14

Repeat

644 – 665

22

LRR 15

Domain

677 – 727

51

LRRCT 3

Domain

730 – 766

37

LRRNT 4

Repeat

767 – 788

22

LRR 16

Repeat

791 – 812

22

LRR 17

Repeat

815 – 836

22

LRR 18

Repeat

839 – 860

22

LRR 19

Domain

872 – 922

51

LRRCT 4

Domain

931 – 968

38

EGF-like 1

Domain

970 – 1007

38

EGF-like 2

Domain

1009 – 1046

38

EGF-like 3; calcium-binding Potential

Domain

1048 – 1086

39

EGF-like 4

Domain

1088 – 1124

37

EGF-like 5; calcium-binding Potential

Domain

1135 – 1173

39

EGF-like 6

Domain

1176 – 1349

174

Laminin G-like

Domain

1377 – 1416

40

EGF-like 7

Domain

1433 – 1504

72

CTCK

Sites

Site

1135 – 1136

2

Cleavage By similarity

Amino acid modifications

Glycosylation

111

1

N-linked (GlcNAc...) Potential

Glycosylation

231

1

N-linked (GlcNAc...) Potential

Glycosylation

381

1

N-linked (GlcNAc...) Potential

Glycosylation

459

1

N-linked (GlcNAc...) Potential

Glycosylation

807

1

N-linked (GlcNAc...) Potential

Glycosylation

812

1

N-linked (GlcNAc...) Potential

Glycosylation

982

1

N-linked (GlcNAc...) Potential

Glycosylation

1022

1

N-linked (GlcNAc...) Potential

Glycosylation

1084

1

N-linked (GlcNAc...) Potential

Glycosylation

1183

1

N-linked (GlcNAc...) Potential

Glycosylation

1199

1

N-linked (GlcNAc...) Potential

Glycosylation

1267

1

N-linked (GlcNAc...) Potential

Glycosylation

1316

1

N-linked (GlcNAc...) Potential

Disulfide bond

543 ↔ 549

Ref.7

Disulfide bond

547 ↔ 556

Ref.7

Disulfide bond

657 ↔ 733

Ref.7

Disulfide bond

681 ↔ 704

Ref.7

Disulfide bond

683 ↔ 725

Ref.7

Disulfide bond

935 ↔ 946

By similarity

Disulfide bond

940 ↔ 956

By similarity

Disulfide bond

958 ↔ 967

By similarity

Disulfide bond

974 ↔ 985

By similarity

Disulfide bond

979 ↔ 995

By similarity

Disulfide bond

997 ↔ 1006

By similarity

Disulfide bond

1013 ↔ 1025

By similarity

Disulfide bond

1019 ↔ 1034

By similarity

Disulfide bond

1036 ↔ 1045

By similarity

Disulfide bond

1052 ↔ 1065

By similarity

Disulfide bond

1059 ↔ 1074

By similarity

Disulfide bond

1076 ↔ 1085

By similarity

Disulfide bond

1092 ↔ 1103

By similarity

Disulfide bond

1097 ↔ 1112

By similarity

Disulfide bond

1114 ↔ 1123

By similarity

Disulfide bond

1139 ↔ 1149

By similarity

Disulfide bond

1144 ↔ 1161

By similarity

Disulfide bond

1163 ↔ 1172

By similarity

Disulfide bond

1323 ↔ 1349

By similarity

Disulfide bond

1381 ↔ 1392

By similarity

Disulfide bond

1386 ↔ 1404

By similarity

Disulfide bond

1406 ↔ 1415

By similarity

Disulfide bond

1433 ↔ 1467

By similarity

Disulfide bond

1447 ↔ 1481

By similarity

Disulfide bond

1458 ↔ 1497

By similarity

Disulfide bond

1462 ↔ 1499

By similarity

Natural variations

Alternative sequence

152 – 175

24

Missing in isoform A and isoform B.

VSP_001408

Alternative sequence

1418 – 1428

11

Missing in isoform B.

VSP_001409

Experimental info

Sequence conflict

350 – 351

2

EL → DV in CAA37910. Ref.1

Sequence conflict

350 – 351

2

EL → DV in AAD26567. Ref.2

Sequence conflict

421

1

Q → R in CAA37910. Ref.1

Sequence conflict

468

1

I → M in CAA37910. Ref.1

Sequence conflict

527

1

D → G in CAA37910. Ref.1

Sequence conflict

560

1

G → R in CAA37910. Ref.1

Sequence conflict

691 – 692

2

WL → CV in CAA37910. Ref.1

Sequence conflict

751

1

R → A in CAA37910. Ref.1

Sequence conflict

843

1

L → V in CAA37910. Ref.1

Sequence conflict

1207 – 1208

2

AE → G in AAA72722. Ref.5

Sequence conflict

1429 – 1435

7

AASTCRK → GTYIYHA in AAA72722. Ref.5

Secondary structure

1

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.

.

.

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.

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1504

Helix Strand Turn

Details...

Beta strand

547 – 550

4

Beta strand

553 – 555

3

Beta strand

573 – 576

4

Helix

591 – 593

3

Beta strand

599 – 601

3

Turn

612 – 617

6

Beta strand

623 – 625

3

Beta strand

636 – 639

4

Beta strand

647 – 649

3

Beta strand

671 – 673

3

Helix

683 – 685

3

Helix

686 – 695

10

Helix

699 – 701

3

Turn

708 – 712

5

Helix

715 – 717

3

Turn

720 – 722

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform C (E) [UniParc]. Last modified February 28, 2003. Version 2. Checksum: 836A3F5022BF234F	FASTA	1,504	168,599
	10 20 30 40 50 60 MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI 70 80 90 100 110 120 PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF 130 140 150 160 170 180 QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLRLNNNRL KAIPENFVTS SASLLRLDIS 190 200 210 220 230 240 NNVITTVGRR VFKGAQSLRS LQLDNNQITC LDEHAFKGLV ELEILTLNNN NLTSLPHNIF 250 260 270 280 290 300 GGLGRLRALR LSDNPFACDC HLSWLSRFLR SATRLAPYTR CQSPSQLKGQ NVADLHDQEF 310 320 330 340 350 360 KCSGLTEHAP MECGAENSCP HPCRCADGIV DCREKSLTSV PVTLPDDTTE LRLEQNFITE 370 380 390 400 410 420 LPPKSFSSFR RLRRIDLSNN NISRIAHDAL SGLKQLTTLV LYGNKIKDLP SGVFKGLGSL 430 440 450 460 470 480 QLLLLNANEI SCIRKDAFRD LHSLSLLSLY DNNIQSLANG TFDAMKSIKT VHLAKNPFIC 490 500 510 520 530 540 DCNLRWLADY LHKNPIETSG ARCESPKRMH RRRIESLREE KFKCSWDELR MKLSGECRMD 550 560 570 580 590 600 SDCPAMCHCE GTTVDCTGRG LKEIPRDIPL HTTELLLNDN ELGRISSDGL FGRLPHLVKL 610 620 630 640 650 660 ELKRNQLTGI EPNAFEGASH IQELQLGENK IKEISNKMFL GLHQLKTLNL YDNQISCVMP 670 680 690 700 710 720 GSFEHLNSLT SLNLASNPFN CNCHLAWFAE WLRKKSLNGG AARCGAPSKV RDVQIKDLPH 730 740 750 760 770 780 SEFKCSSENS EGCLGDGYCP PSCTCTGTVV RCSRNQLKEI PRGIPAETSE LYLESNEIEQ 790 800 810 820 830 840 IHYERIRHLR SLTRLDLSNN QITILSNYTF ANLTKLSTLI ISYNKLQCLQ RHALSGLNNL 850 860 870 880 890 900 RVLSLHGNRI SMLPEGSFED LKSLTHIALG SNPLYCDCGL KWFSDWIKLD YVEPGIARCA 910 920 930 940 950 960 EPEQMKDKLI LSTPSSSFVC RGRVRNDILA KCNACFEQPC QNQAQCVALP QREYQCLCQP 970 980 990 1000 1010 1020 GYHGKHCEFM IDACYGNPCR NNATCTVLEE GRFSCQCAPG YTGARCETNI DDCLGEIKCQ 1030 1040 1050 1060 1070 1080 NNATCIDGVE SYKCECQPGF SGEFCDTKIQ FCSPEFNPCA NGAKCMDHFT HYSCDCQAGF 1090 1100 1110 1120 1130 1140 HGTNCTDNID DCQNHMCQNG GTCVDGINDY QCRCPDDYTG KYCEGHNMIS MMYPQTSPCQ 1150 1160 1170 1180 1190 1200 NHECKHGVCF QPNAQGSDYL CRCHPGYTGK WCEYLTSISF VHNNSFVELE PLRTRPEANV 1210 1220 1230 1240 1250 1260 TIVFSSAEQN GILMYDGQDA HLAVELFNGR IRVSYDVGNH PVSTMYSFEM VADGKYHAVE 1270 1280 1290 1300 1310 1320 LLAIKKNFTL RVDRGLARSI INEGSNDYLK LTTPMFLGGL PVDPAQQAYK NWQIRNLTSF 1330 1340 1350 1360 1370 1380 KGCMKEVWIN HKLVDFGNAQ RQQKITPGCA LLEGEQQEEE DDEQDFMDET PHIKEEPVDP 1390 1400 1410 1420 1430 1440 CLENKCRRGS RCVPNSNARD GYQCKCKHGQ RGRYCDQGEG STEPPTVTAA STCRKEQVRE 1450 1460 1470 1480 1490 1500 YYTENDCRSR QPLKYAKCVG GCGNQCCAAK IVRRRKVRMV CSNNRKYIKN LDIVRKCGCT KKCY
	Isoform A (D) [UniParc]. Checksum: F456BC617D8453ED	FASTA	1,480	165,890
	10 20 30 40 50 60 MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI 70 80 90 100 110 120 PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF 130 140 150 160 170 180 QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLDISNNVI TTVGRRVFKG AQSLRSLQLD 190 200 210 220 230 240 NNQITCLDEH AFKGLVELEI LTLNNNNLTS LPHNIFGGLG RLRALRLSDN PFACDCHLSW 250 260 270 280 290 300 LSRFLRSATR LAPYTRCQSP SQLKGQNVAD LHDQEFKCSG LTEHAPMECG AENSCPHPCR 310 320 330 340 350 360 CADGIVDCRE KSLTSVPVTL PDDTTELRLE QNFITELPPK SFSSFRRLRR IDLSNNNISR 370 380 390 400 410 420 IAHDALSGLK QLTTLVLYGN KIKDLPSGVF KGLGSLQLLL LNANEISCIR KDAFRDLHSL 430 440 450 460 470 480 SLLSLYDNNI QSLANGTFDA MKSIKTVHLA KNPFICDCNL RWLADYLHKN PIETSGARCE 490 500 510 520 530 540 SPKRMHRRRI ESLREEKFKC SWDELRMKLS GECRMDSDCP AMCHCEGTTV DCTGRGLKEI 550 560 570 580 590 600 PRDIPLHTTE LLLNDNELGR ISSDGLFGRL PHLVKLELKR NQLTGIEPNA FEGASHIQEL 610 620 630 640 650 660 QLGENKIKEI SNKMFLGLHQ LKTLNLYDNQ ISCVMPGSFE HLNSLTSLNL ASNPFNCNCH 670 680 690 700 710 720 LAWFAEWLRK KSLNGGAARC GAPSKVRDVQ IKDLPHSEFK CSSENSEGCL GDGYCPPSCT 730 740 750 760 770 780 CTGTVVRCSR NQLKEIPRGI PAETSELYLE SNEIEQIHYE RIRHLRSLTR LDLSNNQITI 790 800 810 820 830 840 LSNYTFANLT KLSTLIISYN KLQCLQRHAL SGLNNLRVLS LHGNRISMLP EGSFEDLKSL 850 860 870 880 890 900 THIALGSNPL YCDCGLKWFS DWIKLDYVEP GIARCAEPEQ MKDKLILSTP SSSFVCRGRV 910 920 930 940 950 960 RNDILAKCNA CFEQPCQNQA QCVALPQREY QCLCQPGYHG KHCEFMIDAC YGNPCRNNAT 970 980 990 1000 1010 1020 CTVLEEGRFS CQCAPGYTGA RCETNIDDCL GEIKCQNNAT CIDGVESYKC ECQPGFSGEF 1030 1040 1050 1060 1070 1080 CDTKIQFCSP EFNPCANGAK CMDHFTHYSC DCQAGFHGTN CTDNIDDCQN HMCQNGGTCV 1090 1100 1110 1120 1130 1140 DGINDYQCRC PDDYTGKYCE GHNMISMMYP QTSPCQNHEC KHGVCFQPNA QGSDYLCRCH 1150 1160 1170 1180 1190 1200 PGYTGKWCEY LTSISFVHNN SFVELEPLRT RPEANVTIVF SSAEQNGILM YDGQDAHLAV 1210 1220 1230 1240 1250 1260 ELFNGRIRVS YDVGNHPVST MYSFEMVADG KYHAVELLAI KKNFTLRVDR GLARSIINEG 1270 1280 1290 1300 1310 1320 SNDYLKLTTP MFLGGLPVDP AQQAYKNWQI RNLTSFKGCM KEVWINHKLV DFGNAQRQQK 1330 1340 1350 1360 1370 1380 ITPGCALLEG EQQEEEDDEQ DFMDETPHIK EEPVDPCLEN KCRRGSRCVP NSNARDGYQC 1390 1400 1410 1420 1430 1440 KCKHGQRGRY CDQGEGSTEP PTVTAASTCR KEQVREYYTE NDCRSRQPLK YAKCVGGCGN 1450 1460 1470 1480 QCCAAKIVRR RKVRMVCSNN RKYIKNLDIV RKCGCTKKCY
	Isoform B [UniParc]. Checksum: 14DBA99CE1DAEAC4	FASTA	1,469	164,834
	10 20 30 40 50 60 MAAPSRTTLM PPPFRLQLRL LILPILLLLR HDAVHAEPYS GGFGSSAVSS GGLGSVGIHI 70 80 90 100 110 120 PGGGVGVITE ARCPRVCSCT GLNVDCSHRG LTSVPRKISA DVERLELQGN NLTVIYETDF 130 140 150 160 170 180 QRLTKLRMLQ LTDNQIHTIE RNSFQDLVSL ERLDISNNVI TTVGRRVFKG AQSLRSLQLD 190 200 210 220 230 240 NNQITCLDEH AFKGLVELEI LTLNNNNLTS LPHNIFGGLG RLRALRLSDN PFACDCHLSW 250 260 270 280 290 300 LSRFLRSATR LAPYTRCQSP SQLKGQNVAD LHDQEFKCSG LTEHAPMECG AENSCPHPCR 310 320 330 340 350 360 CADGIVDCRE KSLTSVPVTL PDDTTELRLE QNFITELPPK SFSSFRRLRR IDLSNNNISR 370 380 390 400 410 420 IAHDALSGLK QLTTLVLYGN KIKDLPSGVF KGLGSLQLLL LNANEISCIR KDAFRDLHSL 430 440 450 460 470 480 SLLSLYDNNI QSLANGTFDA MKSIKTVHLA KNPFICDCNL RWLADYLHKN PIETSGARCE 490 500 510 520 530 540 SPKRMHRRRI ESLREEKFKC SWDELRMKLS GECRMDSDCP AMCHCEGTTV DCTGRGLKEI 550 560 570 580 590 600 PRDIPLHTTE LLLNDNELGR ISSDGLFGRL PHLVKLELKR NQLTGIEPNA FEGASHIQEL 610 620 630 640 650 660 QLGENKIKEI SNKMFLGLHQ LKTLNLYDNQ ISCVMPGSFE HLNSLTSLNL ASNPFNCNCH 670 680 690 700 710 720 LAWFAEWLRK KSLNGGAARC GAPSKVRDVQ IKDLPHSEFK CSSENSEGCL GDGYCPPSCT 730 740 750 760 770 780 CTGTVVRCSR NQLKEIPRGI PAETSELYLE SNEIEQIHYE RIRHLRSLTR LDLSNNQITI 790 800 810 820 830 840 LSNYTFANLT KLSTLIISYN KLQCLQRHAL SGLNNLRVLS LHGNRISMLP EGSFEDLKSL 850 860 870 880 890 900 THIALGSNPL YCDCGLKWFS DWIKLDYVEP GIARCAEPEQ MKDKLILSTP SSSFVCRGRV 910 920 930 940 950 960 RNDILAKCNA CFEQPCQNQA QCVALPQREY QCLCQPGYHG KHCEFMIDAC YGNPCRNNAT 970 980 990 1000 1010 1020 CTVLEEGRFS CQCAPGYTGA RCETNIDDCL GEIKCQNNAT CIDGVESYKC ECQPGFSGEF 1030 1040 1050 1060 1070 1080 CDTKIQFCSP EFNPCANGAK CMDHFTHYSC DCQAGFHGTN CTDNIDDCQN HMCQNGGTCV 1090 1100 1110 1120 1130 1140 DGINDYQCRC PDDYTGKYCE GHNMISMMYP QTSPCQNHEC KHGVCFQPNA QGSDYLCRCH 1150 1160 1170 1180 1190 1200 PGYTGKWCEY LTSISFVHNN SFVELEPLRT RPEANVTIVF SSAEQNGILM YDGQDAHLAV 1210 1220 1230 1240 1250 1260 ELFNGRIRVS YDVGNHPVST MYSFEMVADG KYHAVELLAI KKNFTLRVDR GLARSIINEG 1270 1280 1290 1300 1310 1320 SNDYLKLTTP MFLGGLPVDP AQQAYKNWQI RNLTSFKGCM KEVWINHKLV DFGNAQRQQK 1330 1340 1350 1360 1370 1380 ITPGCALLEG EQQEEEDDEQ DFMDETPHIK EEPVDPCLEN KCRRGSRCVP NSNARDGYQC 1390 1400 1410 1420 1430 1440 KCKHGQRGRY CDQAASTCRK EQVREYYTEN DCRSRQPLKY AKCVGGCGNQ CCAAKIVRRR 1450 1460 KVRMVCSNNR KYIKNLDIVR KCGCTKKCY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains." Rothberg J.M., Jacobs J.R., Goodman C.S., Artavanis-Tsakonas S. Genes Dev. 4:2169-2187(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Embryo.
[2]	"Slit is the midline repellent for the robo receptor in Drosophila." Kidd T., Bland K.S., Goodman C.S. Cell 96:785-794(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, TISSUE SPECIFICITY. Tissue: Embryo.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[5]	"slit: an EGF-homologous locus of D. melanogaster involved in the development of the embryonic central nervous system." Rothberg J.M., Hartley D.A., Walther Z., Artavanis-Tsakonas S. Cell 55:1047-1059(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 898-1435, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: Canton-S.
[6]	"Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance." Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S., Tessier-Lavigne M., Kidd T. Cell 96:795-806(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ROBO, CLEAVAGE.
[7]	"Binding site for Robo receptors revealed by dissection of the leucine-rich repeat region of Slit." Howitt J.A., Clout N.J., Hohenester E. EMBO J. 23:4406-4412(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 542-733, DISULFIDE BONDS IN THE LRR REGION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53959 mRNA. Translation: CAA37910.1.
AF126540 mRNA. Translation: AAD26567.1.
AE013599 Genomic DNA. Translation: AAF58097.1.
AE013599 Genomic DNA. Translation: AAF58098.1.
AE013599 Genomic DNA. Translation: AAM70966.1.
AE013599 Genomic DNA. Translation: ABV53816.1.
AE013599 Genomic DNA. Translation: ABV53817.1.
M23543 Genomic DNA. Translation: AAA72722.1. Different initiation.

PIR

A36665.
B36665.

RefSeq

NP_001097333.1. NM_001103863.2.
NP_001097334.1. NM_001103864.2.
NP_476727.1. NM_057379.4.
NP_476728.1. NM_057380.4.
NP_476729.1. NM_057381.4.

UniGene

Dm.4729.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W8A	X-ray	2.80	A	542-733	[»]

ProteinModelPortal

P24014.

SMR

P24014. Positions 73-920, 932-1433.

ModBase

Search...

Proteomic databases

PaxDb

P24014.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0330731; FBpp0303575; FBgn0264089.
FBtr0330733; FBpp0303577; FBgn0264089.

GeneID

36746.

KEGG

dme:Dmel_CG8355.

UCSC

CG8355-RD. d. melanogaster.
CG8355-RE. d. melanogaster.

Organism-specific databases

CTD

36746.

FlyBase

FBgn0003425. sli.

Phylogenomic databases

eggNOG

COG4886.

GeneTree

ENSGT00700000104083.

InParanoid

P24014.

KO

K06839.

OMA

RHKMFKG.

OrthoDB

EOG46DJHK.

PhylomeDB

P24014.

Enzyme and pathway databases

Reactome

REACT_113552. Developmental Biology.

Gene expression databases

Bgee

P24014.

GermOnline

CG8355. Drosophila melanogaster.

Family and domain databases

Gene3D

2.60.120.200. 2 hits.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR026906. LRR_5.
[Graphical view]

Pfam

PF00008. EGF. 5 hits.
PF00054. Laminin_G_1. 1 hit.
PF00560. LRR_1. 1 hit.
PF13306. LRR_5. 1 hit.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]

SMART

SM00041. CT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 9 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00010. ASX_HYDROXYL. 3 hits.
PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 7 hits.
PS01186. EGF_2. 5 hits.
PS50026. EGF_3. 7 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 20 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24014.

GenomeRNAi

36746.

NextBio

800151.

Entry information

Entry name

SLIT_DROME

Accession

Primary (citable) accession number: P24014
Secondary accession number(s): A8DYF5 , A8DYF6, Q24526, Q8MLB9, Q9V7F8, Q9V7F9, Q9XYV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	February 28, 2003
Last modified:	May 29, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project