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Protein

Roundabout homolog 4

Gene

Robo4

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

Functioni

Receptor for Slit proteins, at least for SLIT2, and seems to be involved in angiogenesis and vascular patterning. May mediate the inhibition of primary endothelial cell migration by Slit proteins.1 Publication

GO - Molecular functioni

  1. receptor activity Source: MGI

GO - Biological processi

  1. angiogenesis Source: MGI
  2. cell differentiation Source: UniProtKB-KW
  3. negative regulation of cell migration Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Roundabout homolog 4
Gene namesi
Name:Robo4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1921394. Robo4.

Subcellular locationi

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. integral component of membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 1012985Roundabout homolog 4PRO_0000031041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 115PROSITE-ProRule annotation
Disulfide bondi159 ↔ 208PROSITE-ProRule annotation
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi681 – 6811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi713 – 7131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi762 – 7621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8C310.
PRIDEiQ8C310.

PTM databases

PhosphoSiteiQ8C310.

Expressioni

Tissue specificityi

Expressed specifically in embryo and adult vascular endothelium.1 Publication

Developmental stagei

In embryonic development of vascular endothelium shows a dynamic expression pattern within vessels, with expression starting in the larger axial vessels and intersomitic vessels at earlier ages, and changing to intersomitic vessel and capillary expression at later stages. At E9.0, is expressed in the central vessels, the dorsal aorta, and intersomitic vessels. At E9.5, is highly expressed in intersomitic vessels with little expression remaining in dorsal aortae. By E10.0, is detected in capillary vessels, the capillary plexus of the limb buds, and throughout the endothelium as microvessels sprout from the dorsal aortae. No expression was detected in the neural tube at E9.0 and E9.5. However, it is detected within the capillaries sprouting into the neural tube, as well as in the adjacent perineural capillary plexus at E10.0.1 Publication

Gene expression databases

BgeeiQ8C310.
CleanExiMM_ROBO4.
ExpressionAtlasiQ8C310. baseline and differential.
GenevestigatoriQ8C310.

Interactioni

Subunit structurei

Interacts with SLIT2 and ENAH.1 Publication

Protein-protein interaction databases

BioGridi216523. 1 interaction.
STRINGi10090.ENSMUSP00000110698.

Structurei

3D structure databases

ProteinModelPortaliQ8C310.
SMRiQ8C310. Positions 8-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 132101Ig-like C2-type 1Add
BLAST
Domaini138 – 22588Ig-like C2-type 2Add
BLAST
Domaini249 – 34698Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 44396Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ROBO family.Curated
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG325715.
GeneTreeiENSGT00780000121850.
HOGENOMiHOG000074193.
HOVERGENiHBG061836.
InParanoidiQ8C310.
KOiK06784.
PhylomeDBiQ8C310.
TreeFamiTF351053.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C310-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGSGGTGLLG TEWPLPLLLL FIMGGEALDS PPQILVHPQD QLLQGSGPAK
60 70 80 90 100
MRCRSSGQPP PTIRWLLNGQ PLSMATPDLH YLLPDGTLLL HRPSVQGRPQ
110 120 130 140 150
DDQNILSAIL GVYTCEASNR LGTAVSRGAR LSVAVLQEDF QIQPRDTVAV
160 170 180 190 200
VGESLVLECG PPWGYPKPSV SWWKDGKPLV LQPGRRTVSG DSLMVSRAEK
210 220 230 240 250
NDSGTYMCMA TNNAGQRESR AARVSIQESQ DHKEHLELLA VRIQLENVTL
260 270 280 290 300
LNPEPVKGPK PGPSVWLSWK VSGPAAPAES YTALFRTQRS PRDQGSPWTE
310 320 330 340 350
VLLRGLQSAK LGGLHWGQDY EFKVRPSSGR ARGPDSNVLL LRLPEQVPSA
360 370 380 390 400
PPQGVTLRSG NGSVFVSWAP PPAESHNGVI RGYQVWSLGN ASLPAANWTV
410 420 430 440 450
VGEQTQLEIA TRLPGSYCVQ VAAVTGAGAG ELSTPVCLLL EQAMEQSARD
460 470 480 490 500
PRKHVPWTLE QLRATLRRPE VIASSAVLLW LLLLGITVCI YRRRKAGVHL
510 520 530 540 550
GPGLYRYTSE DAILKHRMDH SDSPWLADTW RSTSGSRDLS SSSSLSSRLG
560 570 580 590 600
LDPRDPLEGR RSLISWDPRS PGVPLLPDTS TFYGSLIAEQ PSSPPVRPSP
610 620 630 640 650
KTPAARRFPS KLAGTSSPWA SSDSLCSRRG LCSPRMSLTP TEAWKAKKKQ
660 670 680 690 700
ELHQANSSPL LRGSHPMEIW AWELGSRASK NLSQSPGPNS GSPGEAPRAV
710 720 730 740 750
VSWRAVGPQL HRNSSELASR PLPPTPLSLR GASSHDPQSQ CVEKLQAPSS
760 770 780 790 800
DPLPAAPLSV LNSSRPSSPQ ASFLSCPSPS SSNLSSSSLS SLEEEEDQDS
810 820 830 840 850
VLTPEEVALC LELSDGEETP TNSVSPMPRA PSPPTTYGYI SIPTCSGLAD
860 870 880 890 900
MGRAGGGVGS EVGNLLYPPR PCPTPTPSEG SLANGWGSAS EDNVPSARAS
910 920 930 940 950
LVSSSDGSFL ADTHFARALA VAVDSFGLSL DPREADCVFT DASSPPSPRG
960 970 980 990 1000
DLSLTRSFSL PLWEWRPDWL EDAEISHTQR LGRGLPPWPP DSRASSQRSW
1010
LTGAVPKAGD SS
Length:1,012
Mass (Da):108,499
Last modified:June 21, 2004 - v2
Checksum:i9116352CAE767CC1
GO
Isoform 2 (identifier: Q8C310-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     688-694: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:1,005
Mass (Da):107,903
Checksum:i95F8C43EE184E21E
GO
Isoform 3 (identifier: Q8C310-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     440-440: L → LGEGKALSISSTPPPCRPSVSQFLSYIFSSSLSCLLVPLTVPLALPLSSTSQT
     688-694: Missing.

Show »
Length:1,057
Mass (Da):113,251
Checksum:iBDC167380727CBF7
GO

Sequence cautioni

The sequence AAH20129.1 differs from that shown. Reason: Erroneous initiation. Curated
Isoform 2 : The sequence AAH20129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB23506.2 differs from that shown. Reason: Erroneous initiation. Curated
Isoform 2 : The sequence BAB23506.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
Isoform 3 : The sequence BAC39850.1 differs from that shown. Reason: Frameshift at positions 916 and 919. Curated
Isoform 3 : The sequence BAC39850.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei440 – 4401L → LGEGKALSISSTPPPCRPSV SQFLSYIFSSSLSCLLVPLT VPLALPLSSTSQT in isoform 3. 1 PublicationVSP_010663
Alternative sequencei688 – 6947Missing in isoform 2 and isoform 3. 2 PublicationsVSP_010662

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF536772 mRNA. Translation: AAQ10749.1.
AK004723 mRNA. Translation: BAB23506.2. Different initiation.
AK087355 mRNA. Translation: BAC39850.1. Sequence problems.
BC020129 mRNA. Translation: AAH20129.1. Different initiation.
RefSeqiNP_083059.2. NM_028783.2.
UniGeneiMm.485070.

Genome annotation databases

EnsembliENSMUST00000102895; ENSMUSP00000099959; ENSMUSG00000032125.
GeneIDi74144.
KEGGimmu:74144.
UCSCiuc009ous.1. mouse. [Q8C310-2]
uc012gqy.1. mouse. [Q8C310-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF536772 mRNA. Translation: AAQ10749.1.
AK004723 mRNA. Translation: BAB23506.2. Different initiation.
AK087355 mRNA. Translation: BAC39850.1. Sequence problems.
BC020129 mRNA. Translation: AAH20129.1. Different initiation.
RefSeqiNP_083059.2. NM_028783.2.
UniGeneiMm.485070.

3D structure databases

ProteinModelPortaliQ8C310.
SMRiQ8C310. Positions 8-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216523. 1 interaction.
STRINGi10090.ENSMUSP00000110698.

PTM databases

PhosphoSiteiQ8C310.

Proteomic databases

PaxDbiQ8C310.
PRIDEiQ8C310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102895; ENSMUSP00000099959; ENSMUSG00000032125.
GeneIDi74144.
KEGGimmu:74144.
UCSCiuc009ous.1. mouse. [Q8C310-2]
uc012gqy.1. mouse. [Q8C310-1]

Organism-specific databases

CTDi54538.
MGIiMGI:1921394. Robo4.

Phylogenomic databases

eggNOGiNOG325715.
GeneTreeiENSGT00780000121850.
HOGENOMiHOG000074193.
HOVERGENiHBG061836.
InParanoidiQ8C310.
KOiK06784.
PhylomeDBiQ8C310.
TreeFamiTF351053.

Miscellaneous databases

NextBioi339894.
PROiQ8C310.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C310.
CleanExiMM_ROBO4.
ExpressionAtlasiQ8C310. baseline and differential.
GenevestigatoriQ8C310.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Robo4 is a vascular-specific receptor that inhibits endothelial migration."
    Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y., Chien C.-B., Wu J.Y., Urness L.D., Li D.Y.
    Dev. Biol. 261:251-267(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SLIT2 AND ENAH, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: FVB/N.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Lung.
  3. "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 475-1012 (ISOFORM 2).

Entry informationi

Entry nameiROBO4_MOUSE
AccessioniPrimary (citable) accession number: Q8C310
Secondary accession number(s): Q9DBW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: February 4, 2015
This is version 105 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

External Data

Dasty 3

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 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.