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Protein

Slit homolog 2 protein

Gene

Slit2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development, may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system, appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration (By similarity).By similarity2 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • chemorepellent activity Source: MGI
  • GTPase inhibitor activity Source: MGI
  • heparin binding Source: MGI
  • identical protein binding Source: MGI
  • laminin-1 binding Source: MGI
  • protein homodimerization activity Source: MGI
  • proteoglycan binding Source: MGI
  • receptor binding Source: MGI
  • Roundabout binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Chemotaxis, Differentiation, Neurogenesis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-MMU-376176. Signaling by Robo receptor.
R-MMU-428890. Role of Abl in Robo-Slit signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Slit homolog 2 protein
Short name:
Slit-2
Cleaved into the following 2 chains:
Gene namesi
Name:Slit2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1315205. Slit2.

Subcellular locationi

  • Secreted By similarity

  • Note: The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.By similarity

GO - Cellular componenti

  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Mice show significant axon guidance errors in a variety of pathways, including corticofugal, callosal and thalamocortical tracts. Mice double-deficient in SLIT1 and SLIT2 show retinal axon guidance defects and a disorganized lateral olfactory tract (LOT).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 15211496Slit homolog 2 proteinPRO_0000007728Add
BLAST
Chaini26 – 11131088Slit homolog 2 protein N-productBy similarityPRO_0000007729Add
BLAST
Chaini1114 – 1521408Slit homolog 2 protein C-productBy similarityPRO_0000007730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi277 ↔ 286By similarity
Disulfide bondi434 ↔ 457By similarity
Disulfide bondi436 ↔ 478By similarity
Disulfide bondi498 ↔ 504By similarity
Disulfide bondi502 ↔ 511By similarity
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence analysis
Glycosylationi615 – 6151N-linked (GlcNAc...)Sequence analysis
Disulfide bondi660 ↔ 683By similarity
Disulfide bondi662 ↔ 704By similarity
Disulfide bondi719 ↔ 725By similarity
Disulfide bondi723 ↔ 732By similarity
Glycosylationi786 – 7861N-linked (GlcNAc...)Sequence analysis
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi855 ↔ 878By similarity
Disulfide bondi857 ↔ 899By similarity
Disulfide bondi914 ↔ 925By similarity
Disulfide bondi919 ↔ 935By similarity
Disulfide bondi937 ↔ 946By similarity
Disulfide bondi953 ↔ 964By similarity
Disulfide bondi958 ↔ 976By similarity
Disulfide bondi978 ↔ 987By similarity
Disulfide bondi994 ↔ 1005By similarity
Disulfide bondi999 ↔ 1014By similarity
Glycosylationi1001 – 10011N-linked (GlcNAc...)Sequence analysis
Glycosylationi1002 – 10021N-linked (GlcNAc...)Sequence analysis
Glycosylationi1011 – 10111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1016 ↔ 1025By similarity
Disulfide bondi1032 ↔ 1045By similarity
Disulfide bondi1039 ↔ 1054By similarity
Disulfide bondi1056 ↔ 1065By similarity
Disulfide bondi1072 ↔ 1083By similarity
Disulfide bondi1077 ↔ 1092By similarity
Disulfide bondi1094 ↔ 1103By similarity
Disulfide bondi1117 ↔ 1128By similarity
Disulfide bondi1122 ↔ 1137By similarity
Disulfide bondi1139 ↔ 1148By similarity
Glycosylationi1175 – 11751N-linked (GlcNAc...)Sequence analysis
Glycosylationi1258 – 12581N-linked (GlcNAc...)Sequence analysis
Glycosylationi1292 – 12921N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1299 ↔ 1325By similarity
Disulfide bondi1333 ↔ 1338By similarity
Disulfide bondi1350 ↔ 1359By similarity
Disulfide bondi1367 ↔ 1377By similarity
Disulfide bondi1372 ↔ 1387By similarity
Disulfide bondi1389 ↔ 1398By similarity
Disulfide bondi1408 ↔ 1418By similarity
Disulfide bondi1413 ↔ 1428By similarity
Disulfide bondi1430 ↔ 1439By similarity
Disulfide bondi1445 ↔ 1484By similarity
Disulfide bondi1463 ↔ 1498By similarity
Disulfide bondi1474 ↔ 1514By similarity
Disulfide bondi1478 ↔ 1516By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1113 – 11142CleavageBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9R1B9.
PaxDbiQ9R1B9.
PRIDEiQ9R1B9.

PTM databases

iPTMnetiQ9R1B9.
PhosphoSiteiQ9R1B9.

Expressioni

Tissue specificityi

Expressed in developing eye, in the optic stalk, and in the ventral diencephalon.1 Publication

Developmental stagei

According to PubMed:10864955 is expressed during retinal development by E14.5 throughout the RGC layer, and is clearly restricted to the inner nuclear layer at E17.5. In the developing optic chiasm is strongly expressed at E12.5 at the ventral midline of the diencephalon in the region in which the RGC axons enter the brain and turn to grow ventrally, the region expression includes the position of the glial knot. At E14.5 expression is maintained at the ventral midline of the diencephalon, in a region directly dorsal to the site of axon divergence. Outside the developing brain. According to PubMed:10433822 prominently expressed in neural and mesodermally derived tissues. From E8.5 to E9.5 expressed strongly in the roof plate, floor plate, and notochord. Beginning at E10.5 intense expression is also observed in the motor columns. By E13.5 the expression decreased in the roof plate but is still retained in the floor plate and motor columns. In the rostral CNS between E8.5 and E9.5 expressed intensely in the dorsal neuroepithelium overlying the hindbrain, in the dorsal midline of the midbrain and forebrain, and in the ventral midbrain region. By E10.5 to E11.5, additional intense expression is observed in the rhombic lip and the rostral midline. From E13.5 to E17.5, the expression decreased dorsally and continued to be detected in the ventral mesencephalon and diencephalon. Outside neuronal development expressed between E8.5 and E9.5 in the clefts between the first, the second, and the third branchial arches. From E10.5 to E11.5, expression is detected in the nasal pit, the developing eye, the otic vesicle, and the visceral grooves. From E13.5 to E17.5 expressed in the developing cochlea (in a pattern consistent with expression in the organ of Corti), in the olfactory epithelium and in the inner neuronal layer of the retina and in the optic nerve. At this stage also expressed in the tongue, in the tooth primordium, and in the outer root sheath of the whisker follicle in the layer surrounding the bulb. At E11.5 is intensely expressed in the rostral lateral ridge flanking the forelimb buds and in lateral ridge tissue between the fore- and the hindlimb buds. Weak expression is observed in a segmented pattern in the posterior part of the sclerotome. Expression is notably absent in the base of the limb buds and weak expression is observed in the interdigital regions of the distal limb bud beginning at E11.5. By E13.5 intensely expressed in interdigital mesenchyme.2 Publications

Gene expression databases

BgeeiQ9R1B9.
CleanExiMM_SLIT2.
ExpressionAtlasiQ9R1B9. baseline and differential.
GenevisibleiQ9R1B9. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with GREM1 (By similarity). Binds ROBO1 and ROBO2 with high affinity.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203328. 1 interaction.
STRINGi10090.ENSMUSP00000127615.

Structurei

3D structure databases

ProteinModelPortaliQ9R1B9.
SMRiQ9R1B9. Positions 271-478, 497-706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 5530LRRNTAdd
BLAST
Repeati56 – 7722LRR 1Add
BLAST
Repeati80 – 10122LRR 2Add
BLAST
Repeati104 – 12522LRR 3Add
BLAST
Repeati128 – 14922LRR 4Add
BLAST
Repeati152 – 17322LRR 5Add
BLAST
Repeati176 – 19722LRR 6Add
BLAST
Domaini209 – 25951LRRCT 1Add
BLAST
Domaini264 – 30037LRRNT 2Add
BLAST
Repeati301 – 32222LRR 7Add
BLAST
Repeati325 – 34622LRR 8Add
BLAST
Repeati349 – 37022LRR 9Add
BLAST
Repeati373 – 39422LRR 10Add
BLAST
Repeati397 – 41822LRR 11Add
BLAST
Domaini430 – 48051LRRCT 2Add
BLAST
Domaini489 – 52537LRRNT 3Add
BLAST
Repeati526 – 54722LRR 12Add
BLAST
Repeati551 – 57222LRR 13Add
BLAST
Repeati575 – 59622LRR 14Add
BLAST
Repeati599 – 62022LRR 15Add
BLAST
Repeati623 – 64422LRR 16Add
BLAST
Domaini656 – 70651LRRCT 3Add
BLAST
Domaini710 – 74637LRRNT 4Add
BLAST
Repeati747 – 76923LRR 17Add
BLAST
Repeati770 – 79122LRR 18Add
BLAST
Repeati794 – 81522LRR 19Add
BLAST
Repeati818 – 83922LRR 20Add
BLAST
Domaini851 – 90151LRRCT 4Add
BLAST
Domaini912 – 94736EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini949 – 98840EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini990 – 102637EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 106639EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini1068 – 110437EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1113 – 114937EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini1152 – 1325174Laminin G-likePROSITE-ProRule annotationAdd
BLAST
Domaini1329 – 136032EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini1363 – 139937EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini1404 – 144037EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini1445 – 152076CTCKPROSITE-ProRule annotationAdd
BLAST

Domaini

The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro.

Sequence similaritiesi

Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 9 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.PROSITE-ProRule annotation
Contains 20 LRR (leucine-rich) repeats.Curated
Contains 4 LRRCT domains.Curated
Contains 4 LRRNT domains.Curated

Keywords - Domaini

EGF-like domain, Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129708.
HOVERGENiHBG057959.
InParanoidiQ9R1B9.
KOiK06839.
TreeFamiTF332887.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR009030. Growth_fac_rcpt_.
IPR032675. L_dom-like.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00008. EGF. 5 hits.
PF00054. Laminin_G_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 3 hits.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00181. EGF. 9 hits.
SM00179. EGF_CA. 6 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 17 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52058. SSF52058. 4 hits.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 9 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 20 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R1B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIGWQTLS LSLGLVLSIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP
60 70 80 90 100
RNIPRNTERL DLNGNNITRI TKIDFAGLRH LRVLQLMENR ISTIERGAFQ
110 120 130 140 150
DLKELERLRL NRNNLQLFPE LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA
160 170 180 190 200
VDIKNLQLDY NQISCIEDGA FRALRDLEVL TLNNNNITRL SVASFNHMPK
210 220 230 240 250
LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS HLRGHNVAEV
260 270 280 290 300
QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE
310 320 330 340 350
TITEIRLEQN SIRVIPPGAF SPYKKLRRLD LSNNQISELA PDAFQGLRSL
360 370 380 390 400
NSLVLYGNKI TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL
410 420 430 440 450
LSLYDNKLQT VAKGTFSALR AIQTMHLAQN PFICDCHLKW LADYLHTNPI
460 470 480 490 500
ETSGARCTSP RRLANKRIGQ IKSKKFRCSG TEDYRSKLSG DCFADLACPE
510 520 530 540 550
KCRCEGTTVD CSNQRLNKIP DHIPQYTAEL RLNNNEFTVL EATGIFKKLP
560 570 580 590 600
QLRKINFSNN KITDIEEGAF EGASGVNEIL LTSNRLENVQ HKMFKGLESL
610 620 630 640 650
KTLMLRSNRI SCVGNDSFIG LGSVRLLSLY DNQITTVAPG AFDSLHSLST
660 670 680 690 700
LNLLANPFNC NCHLAWLGEW LRRKRIVTGN PRCQKPYFLK EIPIQDVAIQ
710 720 730 740 750
DFTCDDGNDD NSCSPLSRCP SECTCLDTVV RCSNKGLKVL PKGIPKDVTE
760 770 780 790 800
LYLDGNQFTL VPKELSNYKH LTLIDLSNNR ISTLSNQSFS NMTQLLTLIL
810 820 830 840 850
SYNRLRCIPP RTFDGLKSLR LLSLHGNDIS VVPEGAFNDL SALSHLAIGA
860 870 880 890 900
NPLYCDCNMQ WLSDWVKSEY KEPGIARCAG PGEMADKLLL TTPSKKFTCQ
910 920 930 940 950
GPVDITIQAK CNPCLSNPCK NDGTCNNDPV DFYRCTCPYG FKGQDCDVPI
960 970 980 990 1000
HACISNPCKH GGTCHLKEGE NAGFWCTCAD GFEGENCEVN IDDCEDNDCE
1010 1020 1030 1040 1050
NNSTCVDGIN NYTCLCPPEY TGELCEEKLD FCAQDLNPCQ HDSKCILTPK
1060 1070 1080 1090 1100
GFKCDCTPGY IGEHCDIDFD DCQDNKCKNG AHCTDAVNGY TCVCPEGYSG
1110 1120 1130 1140 1150
LFCEFSPPMV LPRTSPCDNF DCQNGAQCII RINEPICQCL PGYLGEKCEK
1160 1170 1180 1190 1200
LVSVNFVNKE SYLQIPSAKV RPQTNITLQI ATDEDSGILL YKGDKDHIAV
1210 1220 1230 1240 1250
ELYRGRVRAS YDTGSHPASA IYSVETINDG NFHIVELLTL DSSLSLSVDG
1260 1270 1280 1290 1300
GSPKVITNLS KQSTLNFDSP LYVGGMPGKN NVASLRQAPG QNGTSFHGCI
1310 1320 1330 1340 1350
RNLYINSELQ DFRKMPMQTG ILPGCEPCHK KVCAHGMCQP SSQSGFTCEC
1360 1370 1380 1390 1400
EEGWMGPLCD QRTNDPCLGN KCVHGTCLPI NAFSYSCKCL EGHGGVLCDE
1410 1420 1430 1440 1450
EEDLFNPCQM IKCKHGKCRL SGVGQPYCEC NSGFTGDSCD REISCRGERI
1460 1470 1480 1490 1500
RDYYQKQQGY AACQTTKKVS RLECRGGCAG GQCCGPLRSK RRKYSFECTD
1510 1520
GSSFVDEVEK VVKCGCARCA S
Length:1,521
Mass (Da):168,783
Last modified:July 27, 2011 - v2
Checksum:i0DC3626D46FDB711
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731I → T in AAD44759 (PubMed:10433822).Curated
Sequence conflicti903 – 9031V → M in AAD04345 (PubMed:10349621).Curated
Sequence conflicti1277 – 12771P → S in AAH59267 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144628 mRNA. Translation: AAD44759.1.
AC101004 Genomic DNA. No translation available.
AC113542 Genomic DNA. No translation available.
AC157351 Genomic DNA. No translation available.
AF074960 mRNA. Translation: AAD04345.1.
BC059267 mRNA. Translation: AAH59267.1.
CCDSiCCDS19280.1.
PIRiT42626.
RefSeqiNP_848919.3. NM_178804.5.
UniGeneiMm.289739.
Mm.482843.

Genome annotation databases

EnsembliENSMUST00000173107; ENSMUSP00000133840; ENSMUSG00000031558.
GeneIDi20563.
KEGGimmu:20563.
UCSCiuc008xjo.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144628 mRNA. Translation: AAD44759.1.
AC101004 Genomic DNA. No translation available.
AC113542 Genomic DNA. No translation available.
AC157351 Genomic DNA. No translation available.
AF074960 mRNA. Translation: AAD04345.1.
BC059267 mRNA. Translation: AAH59267.1.
CCDSiCCDS19280.1.
PIRiT42626.
RefSeqiNP_848919.3. NM_178804.5.
UniGeneiMm.289739.
Mm.482843.

3D structure databases

ProteinModelPortaliQ9R1B9.
SMRiQ9R1B9. Positions 271-478, 497-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203328. 1 interaction.
STRINGi10090.ENSMUSP00000127615.

PTM databases

iPTMnetiQ9R1B9.
PhosphoSiteiQ9R1B9.

Proteomic databases

MaxQBiQ9R1B9.
PaxDbiQ9R1B9.
PRIDEiQ9R1B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000173107; ENSMUSP00000133840; ENSMUSG00000031558.
GeneIDi20563.
KEGGimmu:20563.
UCSCiuc008xjo.3. mouse.

Organism-specific databases

CTDi9353.
MGIiMGI:1315205. Slit2.

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129708.
HOVERGENiHBG057959.
InParanoidiQ9R1B9.
KOiK06839.
TreeFamiTF332887.

Enzyme and pathway databases

ReactomeiR-MMU-376176. Signaling by Robo receptor.
R-MMU-428890. Role of Abl in Robo-Slit signaling.

Miscellaneous databases

ChiTaRSiSlit2. mouse.
PROiQ9R1B9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1B9.
CleanExiMM_SLIT2.
ExpressionAtlasiQ9R1B9. baseline and differential.
GenevisibleiQ9R1B9. MM.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR009030. Growth_fac_rcpt_.
IPR032675. L_dom-like.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00008. EGF. 5 hits.
PF00054. Laminin_G_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 3 hits.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00181. EGF. 9 hits.
SM00179. EGF_CA. 6 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 17 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52058. SSF52058. 4 hits.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 9 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 20 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse SLIT family: secreted ligands for ROBO expressed in patterns that suggest a role in morphogenesis and axon guidance."
    Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.
    Dev. Biol. 212:290-306(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: ICR X Swiss Webster.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Distinct but overlapping expression patterns of two vertebrate slit homologs implies functional roles in CNS development and organogenesis."
    Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T., Little M.H.
    Mech. Dev. 79:57-72(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 497-1521.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1521.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Slit1 and slit2 proteins control the development of the lateral olfactory tract."
    Nguyen-Ba-Charvet K.T., Plump A.S., Tessier-Lavigne M., Chedotal A.
    J. Neurosci. 22:5473-5480(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Slit proteins prevent midline crossing and determine the dorsoventral position of major axonal pathways in the mammalian forebrain."
    Bagri A., Marin O., Plump A.S., Mak J., Pleasure S.J., Rubenstein J.L., Tessier-Lavigne M.
    Neuron 33:233-248(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Slit2 is a repellent for retinal ganglion cell axons."
    Niclou S.P., Jia L., Raper J.A.
    J. Neurosci. 20:4962-4974(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Retinal ganglion cell axon guidance in the mouse optic chiasm: expression and function of robos and slits."
    Erskine L., Williams S.E., Brose K., Kidd T., Rachel R.A., Goodman C.S., Tessier-Lavigne M., Mason C.A.
    J. Neurosci. 20:4975-4982(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSLIT2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1B9
Secondary accession number(s): E9QKB4, Q9Z166
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.