ROBO1_RAT
ID ROBO1_RAT Reviewed; 1651 AA.
AC O55005;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Roundabout homolog 1;
DE Flags: Precursor;
GN Name=Robo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Spinal cord;
RX PubMed=9458045; DOI=10.1016/s0092-8674(00)80915-0;
RA Kidd T., Brose K., Mitchell K.J., Fetter R.D., Tessier-Lavigne M.,
RA Goodman C.S., Tear G.;
RT "Roundabout controls axon crossing of the CNS midline and defines a novel
RT subfamily of evolutionarily conserved guidance receptors.";
RL Cell 92:205-215(1998).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10102268; DOI=10.1016/s0092-8674(00)80590-5;
RA Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA Tessier-Lavigne M., Kidd T.;
RT "Slit proteins bind Robo receptors and have an evolutionarily conserved
RT role in repulsive axon guidance.";
RL Cell 96:795-806(1999).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=11754167; DOI=10.1002/cne.10068;
RA Marillat V., Cases O., Nguyen-Ba-Charvet K.T., Tessier-Lavigne M.,
RA Sotelo C., Chedotal A.;
RT "Spatiotemporal expression patterns of slit and robo genes in the rat
RT brain.";
RL J. Comp. Neurol. 442:130-155(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=28859078; DOI=10.1371/journal.pgen.1006865;
RA Justice E.D., Barnum S.J., Kidd T.;
RT "The WAGR syndrome gene PRRG4 is a functional homologue of the
RT commissureless axon guidance gene.";
RL PLoS Genet. 13:E1006865-E1006865(2017).
CC -!- FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses
CC to molecular guidance cues in cellular migration, including axonal
CC navigation at the ventral midline of the neural tube and projection of
CC axons to different regions during neuronal development. Interaction
CC with the intracellular domain of FLRT3 mediates axon attraction towards
CC cells expressing NTN1 (By similarity). In axon growth cones, the
CC silencing of the attractive effect of NTN1 by SLIT2 may require the
CC formation of a ROBO1-DCC complex (By similarity). Plays a role in the
CC regulation of cell migration via its interaction with MYO9B; inhibits
CC MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads
CC to increased levels of active, GTP-bound RHOA (By similarity). May be
CC required for lung development (By similarity).
CC {ECO:0000250|UniProtKB:O89026, ECO:0000250|UniProtKB:Q9Y6N7}.
CC -!- SUBUNIT: Homodimer. Dimerization is mediated by the extracellular
CC domain and is independent of SLIT liganding (By similarity). Interacts
CC with SLIT1 (By similarity). Interacts with SLIT2. Interacts with FLRT3.
CC Interacts with MYO9B (via Rho-GAP domain) (By similarity).
CC {ECO:0000250|UniProtKB:O89026, ECO:0000250|UniProtKB:Q9Y6N7}.
CC -!- INTERACTION:
CC O55005; Q63155: Dcc; NbExp=2; IntAct=EBI-3505237, EBI-1798965;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28859078};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9Y6N7}.
CC Cell projection, axon {ECO:0000250|UniProtKB:O89026}. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane
CC {ECO:0000269|PubMed:28859078}; Single-pass membrane protein
CC {ECO:0000305|PubMed:28859078}. Note=Detected at growth cones in
CC thalamus neurons (By similarity). PRRG4 prevents cell surface location
CC and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the
CC cell nucleus (PubMed:28859078). {ECO:0000250|UniProtKB:O89026,
CC ECO:0000269|PubMed:28859078}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonal brain and spinal chord.
CC {ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:9458045}.
CC -!- DEVELOPMENTAL STAGE: In the developing spinal cord expressed at E11 and
CC E13 dorsally in the region of the commissural and association neuron
CC cell bodies and ventrally in subpopulations in the motor column. In the
CC brain detected between E15 and E18, between P0 and P10, and in adult in
CC regions of the hippocampal system and the basal ganglia. Detected at
CC E18, between P0 and P10, and in adult in anterior olfactory nuclei,
CC regions of the cortex and basal telencephalon.
CC {ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:11754167}.
CC -!- PTM: Ubiquitinated. May be deubiquitinated by USP33.
CC {ECO:0000250|UniProtKB:O89026}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
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DR EMBL; AF041082; AAC39960.1; -; mRNA.
DR PIR; T14160; T14160.
DR RefSeq; NP_071524.1; NM_022188.1.
DR AlphaFoldDB; O55005; -.
DR SMR; O55005; -.
DR BioGRID; 248681; 2.
DR DIP; DIP-48941N; -.
DR IntAct; O55005; 2.
DR STRING; 10116.ENSRNOP00000044134; -.
DR GlyGen; O55005; 5 sites.
DR iPTMnet; O55005; -.
DR PhosphoSitePlus; O55005; -.
DR PaxDb; O55005; -.
DR PRIDE; O55005; -.
DR GeneID; 58946; -.
DR KEGG; rno:58946; -.
DR UCSC; RGD:61941; rat.
DR CTD; 6091; -.
DR RGD; 61941; Robo1.
DR eggNOG; KOG4222; Eukaryota.
DR InParanoid; O55005; -.
DR OrthoDB; 45439at2759; -.
DR PhylomeDB; O55005; -.
DR PRO; PR:O55005; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008046; F:axon guidance receptor activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030275; F:LRR domain binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IDA:RGD.
DR GO; GO:0016199; P:axon midline choice point recognition; IEP:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; ISO:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0003272; P:endocardial cushion formation; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:RGD.
DR GO; GO:0050925; P:negative regulation of negative chemotaxis; ISO:RGD.
DR GO; GO:0021891; P:olfactory bulb interneuron development; ISO:RGD.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; ISO:RGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR032986; Robo1.
DR PANTHER; PTHR12231:SF243; PTHR12231:SF243; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chemotaxis; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1651
FT /note="Roundabout homolog 1"
FT /id="PRO_0000031035"
FT TOPO_DOM 26..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..1651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 68..164
FT /note="Ig-like C2-type 1"
FT DOMAIN 170..257
FT /note="Ig-like C2-type 2"
FT DOMAIN 262..346
FT /note="Ig-like C2-type 3"
FT DOMAIN 351..446
FT /note="Ig-like C2-type 4"
FT DOMAIN 455..541
FT /note="Ig-like C2-type 5"
FT DOMAIN 563..657
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 676..773
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 778..874
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 31..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1038
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1073
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1114
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 191..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 283..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 372..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 476..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1651 AA; 180748 MW; FA2452DD46E186B7 CRC64;
MKWKHLPLLV MISLLTLSKK HLLLAQLIPD PEDLERGNDN GTPAPTSDND DNSLGYTGSR
LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE WYKGGERVET DKDDPRSHRM
LLPSGSLFFL RIVHGRKSRP DEGVYICVAR NYLGEAVSHN ASLEVAILRD DFRQNPSDVM
VAVGEPAVME CQPPRGHPEP TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC
VGTNMVGERE SKVADVTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTFGWRKDDG
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP PHFVVKPRDQ
VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ SSSRFSVSQT GDLTVTNVQR
SDVGYYICQT LNVAGSIITK AYLEVTDVIA DRPPPVIRQG PVNQTVAVDG TLTLSCVATG
SPVPTILWRK DGVLVSTQDS RIKQLESGVL QIRYAKLGDT GRYTCTASTP SGEATWSAYI
EVQEFGVPVQ PPRPTDPNLI PSAPSKPEVT DVSKNTVTLL WQPNLNSGAT PTSYIIEAFS
HASGSSWQTV AENVKTETFA IKGLKPNAIY LFLVRAANAY GISDPSQISD PVKTQDVPPT
TQGVDHKQVQ RELGNVVLHL HNPTILSSSS VEVHWTVDQQ SQYIQGYKIL YRPSGASHGE
SEWLVFEVRT PTKNSVVIPD LRKGVNYEIK ARPFFNEFQG ADSEIKFAKT LEERPSAPPR
SVTVSKNDGN GTAILVTWQP PPEDTQNGMV QEYKVWCLGN ETRYHINKTV DGSTFSVVIP
FLVPGIRYSV EVAASTGAGP GVKSEPQFIQ LDSHGNPVSP EDQVSLAQQI SDVVKQPAFI
AGIGAACWII LMVFSIWLYR HRKKRNGLSS TYAGIRKVPS FTFTPTVTYQ RGGEAVSSGG
RPGLLNISEP ATQPWLADTW PNTGNSHNDC SINCCTASNG NSDSNLTTYS RPADCIANYN
NQLDNKQTNL MLPESTVYGD VDLSNKINEM KTFNSPNLKD GRFVNPSGQP TPYATTQLIQ
ANLINNMNNG GGDSSEKHWK PPGQQKQEVA PIQYNIMEQN KLNKDYRAND TILPTIPYNH
SYDQNTGGSY NSSDRGSSTS GSQGHKKGAR TPKAPKQGGM NWADLLPPPP AHPPPHSNSE
EYSMSVDESY DQEMPCPVPP ARMYLQQDEL EEEEAERGPT PPVRGAASSP AAVSYSHQST
ATLTPSPQEE LQPMLQDCPE DLGHMPHPPD RRRQPVSPPP PPRPISPPHT YGYISGPLVS
DMDTDAPEEE EDEADMEVAK MQTRRLLLRG LEQTPASSVG DLESSVTGSM INGWGSASEE
DNISSGRSSV SSSDGSFFTD ADFAQAVAAA AEYAGLKVAR RQMQDAAGRR HFHASQCPRP
TSPVSTDSNM SAAVIQKARP TKKQKHQPGH LRREAYTDDL PPPPVPPPAI KSPSVQSKAQ
LEARPIMGPK LASIEARADR SSDRKGGSYK GREALDGRQV TDLRTSPGDP REAQEQPNEG
KARGTKTAKR DLPPAKTHLI PEDILPYCRP TFPTSNNPRD PSSSSSMSSR GSGSRQREQA
NVGRRNMAEM QVLGGFERGD ENNEELEETE S
