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Protein

Roundabout homolog 1

Gene

Robo1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (By similarity). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (By similarity).By similarity

GO - Molecular functioni

  • axon guidance receptor activity Source: RGD

GO - Biological processi

  • axon guidance Source: RGD
  • axon midline choice point recognition Source: UniProtKB
  • central nervous system development Source: RGD
  • heart development Source: InterPro
  • negative regulation of cell migration Source: UniProtKB
  • positive regulation of Rho protein signal transduction Source: UniProtKB
  • regulation of dendrite morphogenesis Source: UniProtKB
  • Roundabout signaling pathway Source: UniProtKB
  • spinal cord development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Chemotaxis, Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Roundabout homolog 1
Gene namesi
Name:Robo1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61941. Robo1.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cell projectionaxon By similarity

  • Note: Detected at growth cones in thalamus neurons.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 897872ExtracellularSequence analysisAdd
BLAST
Transmembranei898 – 91821HelicalSequence analysisAdd
BLAST
Topological domaini919 – 1651733CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: RGD
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 16511626Roundabout homolog 1PRO_0000031035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 147PROSITE-ProRule annotation
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi191 ↔ 240PROSITE-ProRule annotation
Disulfide bondi283 ↔ 330PROSITE-ProRule annotation
Disulfide bondi372 ↔ 428PROSITE-ProRule annotation
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi476 ↔ 525PROSITE-ProRule annotation
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence analysis
Glycosylationi820 – 8201N-linked (GlcNAc...)Sequence analysis
Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence analysis
Modified residuei940 – 9401PhosphoserineBy similarity
Modified residuei948 – 9481PhosphothreonineBy similarity
Modified residuei1038 – 10381PhosphotyrosineBy similarity
Modified residuei1055 – 10551PhosphoserineBy similarity
Modified residuei1073 – 10731PhosphotyrosineBy similarity
Modified residuei1114 – 11141PhosphotyrosineBy similarity
Modified residuei1240 – 12401PhosphothreonineBy similarity
Modified residuei1297 – 12971PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated. May be deubiquitinated by USP33.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO55005.
PRIDEiO55005.

PTM databases

iPTMnetiO55005.
PhosphoSiteiO55005.

Expressioni

Tissue specificityi

Expressed in embryonal brain and spinal chord.2 Publications

Developmental stagei

In the developing spinal chord expressed at E11 and E13 dorsally in the region of the commissural and association neuron cell bodies and ventrally in subpopulations in the motor column. In the brain detected between E15 and E18, between P0 and P10, and in adult in regions of the hippocampal system and the basal ganglia. Detected at E18, between P0 and P10, and in adult in anterior olfactory nuclei, regions of the cortex and basal telencephalon.2 Publications

Interactioni

Subunit structurei

Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (By similarity). Interacts with SLIT2. Interacts with FLRT3. Interacts with MYO9B (via Rho-GAP domain) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DccQ631552EBI-3505237,EBI-1798965

Protein-protein interaction databases

BioGridi248681. 1 interaction.
DIPiDIP-48941N.
IntActiO55005. 1 interaction.
STRINGi10116.ENSRNOP00000044134.

Structurei

3D structure databases

ProteinModelPortaliO55005.
SMRiO55005. Positions 61-266, 454-564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 16497Ig-like C2-type 1Add
BLAST
Domaini170 – 25788Ig-like C2-type 2Add
BLAST
Domaini262 – 34685Ig-like C2-type 3Add
BLAST
Domaini351 – 44696Ig-like C2-type 4Add
BLAST
Domaini455 – 54187Ig-like C2-type 5Add
BLAST
Domaini563 – 65795Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini676 – 77398Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini778 – 87497Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ROBO family.Curated
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4222. Eukaryota.
ENOG410XPQS. LUCA.
HOGENOMiHOG000010267.
HOVERGENiHBG073476.
InParanoidiO55005.
KOiK06753.
PhylomeDBiO55005.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR032986. Robo1.
[Graphical view]
PANTHERiPTHR10489:SF107. PTHR10489:SF107. 4 hits.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 5 hits.
SM00408. IGc2. 5 hits.
SM00406. IGv. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O55005-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWKHLPLLV MISLLTLSKK HLLLAQLIPD PEDLERGNDN GTPAPTSDND
60 70 80 90 100
DNSLGYTGSR LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE
110 120 130 140 150
WYKGGERVET DKDDPRSHRM LLPSGSLFFL RIVHGRKSRP DEGVYICVAR
160 170 180 190 200
NYLGEAVSHN ASLEVAILRD DFRQNPSDVM VAVGEPAVME CQPPRGHPEP
210 220 230 240 250
TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC VGTNMVGERE
260 270 280 290 300
SKVADVTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTFGWRKDDG
310 320 330 340 350
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP
360 370 380 390 400
PHFVVKPRDQ VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ
410 420 430 440 450
SSSRFSVSQT GDLTVTNVQR SDVGYYICQT LNVAGSIITK AYLEVTDVIA
460 470 480 490 500
DRPPPVIRQG PVNQTVAVDG TLTLSCVATG SPVPTILWRK DGVLVSTQDS
510 520 530 540 550
RIKQLESGVL QIRYAKLGDT GRYTCTASTP SGEATWSAYI EVQEFGVPVQ
560 570 580 590 600
PPRPTDPNLI PSAPSKPEVT DVSKNTVTLL WQPNLNSGAT PTSYIIEAFS
610 620 630 640 650
HASGSSWQTV AENVKTETFA IKGLKPNAIY LFLVRAANAY GISDPSQISD
660 670 680 690 700
PVKTQDVPPT TQGVDHKQVQ RELGNVVLHL HNPTILSSSS VEVHWTVDQQ
710 720 730 740 750
SQYIQGYKIL YRPSGASHGE SEWLVFEVRT PTKNSVVIPD LRKGVNYEIK
760 770 780 790 800
ARPFFNEFQG ADSEIKFAKT LEERPSAPPR SVTVSKNDGN GTAILVTWQP
810 820 830 840 850
PPEDTQNGMV QEYKVWCLGN ETRYHINKTV DGSTFSVVIP FLVPGIRYSV
860 870 880 890 900
EVAASTGAGP GVKSEPQFIQ LDSHGNPVSP EDQVSLAQQI SDVVKQPAFI
910 920 930 940 950
AGIGAACWII LMVFSIWLYR HRKKRNGLSS TYAGIRKVPS FTFTPTVTYQ
960 970 980 990 1000
RGGEAVSSGG RPGLLNISEP ATQPWLADTW PNTGNSHNDC SINCCTASNG
1010 1020 1030 1040 1050
NSDSNLTTYS RPADCIANYN NQLDNKQTNL MLPESTVYGD VDLSNKINEM
1060 1070 1080 1090 1100
KTFNSPNLKD GRFVNPSGQP TPYATTQLIQ ANLINNMNNG GGDSSEKHWK
1110 1120 1130 1140 1150
PPGQQKQEVA PIQYNIMEQN KLNKDYRAND TILPTIPYNH SYDQNTGGSY
1160 1170 1180 1190 1200
NSSDRGSSTS GSQGHKKGAR TPKAPKQGGM NWADLLPPPP AHPPPHSNSE
1210 1220 1230 1240 1250
EYSMSVDESY DQEMPCPVPP ARMYLQQDEL EEEEAERGPT PPVRGAASSP
1260 1270 1280 1290 1300
AAVSYSHQST ATLTPSPQEE LQPMLQDCPE DLGHMPHPPD RRRQPVSPPP
1310 1320 1330 1340 1350
PPRPISPPHT YGYISGPLVS DMDTDAPEEE EDEADMEVAK MQTRRLLLRG
1360 1370 1380 1390 1400
LEQTPASSVG DLESSVTGSM INGWGSASEE DNISSGRSSV SSSDGSFFTD
1410 1420 1430 1440 1450
ADFAQAVAAA AEYAGLKVAR RQMQDAAGRR HFHASQCPRP TSPVSTDSNM
1460 1470 1480 1490 1500
SAAVIQKARP TKKQKHQPGH LRREAYTDDL PPPPVPPPAI KSPSVQSKAQ
1510 1520 1530 1540 1550
LEARPIMGPK LASIEARADR SSDRKGGSYK GREALDGRQV TDLRTSPGDP
1560 1570 1580 1590 1600
REAQEQPNEG KARGTKTAKR DLPPAKTHLI PEDILPYCRP TFPTSNNPRD
1610 1620 1630 1640 1650
PSSSSSMSSR GSGSRQREQA NVGRRNMAEM QVLGGFERGD ENNEELEETE

S
Length:1,651
Mass (Da):180,748
Last modified:June 1, 1998 - v1
Checksum:iFA2452DD46E186B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041082 mRNA. Translation: AAC39960.1.
PIRiT14160.
RefSeqiNP_071524.1. NM_022188.1.
UniGeneiRn.44468.

Genome annotation databases

GeneIDi58946.
KEGGirno:58946.
UCSCiRGD:61941. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041082 mRNA. Translation: AAC39960.1.
PIRiT14160.
RefSeqiNP_071524.1. NM_022188.1.
UniGeneiRn.44468.

3D structure databases

ProteinModelPortaliO55005.
SMRiO55005. Positions 61-266, 454-564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248681. 1 interaction.
DIPiDIP-48941N.
IntActiO55005. 1 interaction.
STRINGi10116.ENSRNOP00000044134.

PTM databases

iPTMnetiO55005.
PhosphoSiteiO55005.

Proteomic databases

PaxDbiO55005.
PRIDEiO55005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58946.
KEGGirno:58946.
UCSCiRGD:61941. rat.

Organism-specific databases

CTDi6091.
RGDi61941. Robo1.

Phylogenomic databases

eggNOGiKOG4222. Eukaryota.
ENOG410XPQS. LUCA.
HOGENOMiHOG000010267.
HOVERGENiHBG073476.
InParanoidiO55005.
KOiK06753.
PhylomeDBiO55005.

Miscellaneous databases

PROiO55005.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR032986. Robo1.
[Graphical view]
PANTHERiPTHR10489:SF107. PTHR10489:SF107. 4 hits.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 5 hits.
SM00408. IGc2. 5 hits.
SM00406. IGv. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Roundabout controls axon crossing of the CNS midline and defines a novel subfamily of evolutionarily conserved guidance receptors."
    Kidd T., Brose K., Mitchell K.J., Fetter R.D., Tessier-Lavigne M., Goodman C.S., Tear G.
    Cell 92:205-215(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Spinal cord.
  2. "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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Spatiotemporal expression patterns of slit and robo genes in the rat brain."
    Marillat V., Cases O., Nguyen-Ba-Charvet K.T., Tessier-Lavigne M., Sotelo C., Chedotal A.
    J. Comp. Neurol. 442:130-155(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiROBO1_RAT
AccessioniPrimary (citable) accession number: O55005
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 120 of the entry and version 1 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. 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.