ROBO3_MOUSE
ID ROBO3_MOUSE Reviewed; 1366 AA.
AC Q9Z2I4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Roundabout homolog 3;
DE AltName: Full=Retinoblastoma-inhibiting gene 1 protein;
DE Short=Rig-1;
DE Flags: Precursor;
GN Name=Robo3; Synonyms=Rbig1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10049565; DOI=10.1006/dbio.1998.9141;
RA Yuan S.S., Cox L.A., Dasika G.K., Lee E.Y.-H.P.;
RT "Cloning and functional studies of a novel gene aberrantly expressed in RB-
RT deficient embryos.";
RL Dev. Biol. 207:62-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-53 (ISOFORM 1).
RG The MGC Project Team;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP RECONSTRUCTION FROM GENOMIC SEQUENCE AND ESTS, AND CONCEPTUAL TRANSLATION
RP OF 1-53 (ISOFORM 1).
RA Roechert B.;
RL Unpublished observations (MAY-2004).
RN [4]
RP FUNCTION, INTERACTION WITH SLIT2, AND TISSUE SPECIFICITY.
RX PubMed=15084255; DOI=10.1016/s0092-8674(04)00303-4;
RA Sabatier C., Plump A.S., Ma L., Brose K., Tamada A., Murakami F.,
RA Lee E.Y.-H.P., Tessier-Lavigne M.;
RT "The divergent Robo family protein rig-1/Robo3 is a negative regulator of
RT slit responsiveness required for midline crossing by commissural axons.";
RL Cell 117:157-169(2004).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=14678835; DOI=10.1016/s1567-133x(03)00142-x;
RA Camurri L., Mambetisaeva E., Sundaresan V.;
RT "Rig-1 a new member of Robo family genes exhibits distinct pattern of
RT expression during mouse development.";
RL Gene Expr. Patterns 4:99-103(2004).
RN [6]
RP FUNCTION.
RX PubMed=30843071; DOI=10.1093/nar/gkz157;
RA Zhuang M., Li X., Zhu J., Zhang J., Niu F., Liang F., Chen M., Li D.,
RA Han P., Ji S.J.;
RT "The m6A reader YTHDF1 regulates axon guidance through translational
RT control of Robo3.1 expression.";
RL Nucleic Acids Res. 47:4765-4777(2019).
CC -!- FUNCTION: Thought to be involved during neural development in axonal
CC navigation at the ventral midline of the neural tube (PubMed:15084255,
CC PubMed:30843071). In spinal cord development plays a role in guiding
CC commissural axons probably by preventing premature sensitivity to Slit
CC proteins thus inhibiting Slit signaling through ROBO1
CC (PubMed:15084255). Required for hindbrain axon midline crossing
CC (PubMed:30843071). {ECO:0000269|PubMed:15084255,
CC ECO:0000269|PubMed:30843071}.
CC -!- SUBUNIT: Probably interacts with SLIT2. {ECO:0000269|PubMed:15084255}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10049565}; Single-
CC pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q9Z2I4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2I4-2; Sequence=VSP_010652, VSP_010653;
CC -!- TISSUE SPECIFICITY: Detected in embryonal spinal cord and hindbrain.
CC {ECO:0000269|PubMed:10049565, ECO:0000269|PubMed:15084255}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc is expressed in long stripes in the
CC dorso-ventral part of the neural tube. Later at 11.5, 12.5 and 13.5 dpc
CC expression gradually moves dorsally and medially towards the roof
CC plate. At 11.5 dpc highly expressed in spinal cord commissural exons
CC before crossing the floor plate. After midline crossing initially
CC continues to be expressed but then gets down-regulated.
CC {ECO:0000269|PubMed:14678835}.
CC -!- MISCELLANEOUS: ROBO3 null deficient mice lack embryonal spinal chord
CC commissural axons crossing the floor plate.
CC -!- MISCELLANEOUS: [Isoform 1]: The region from 1 to 53 was deduced from
CC the genomic sequence and ESTs by similarity to the human sequence.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
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DR EMBL; AF060570; AAD11628.1; -; mRNA.
DR EMBL; BQ769335; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T14316; T14316.
DR AlphaFoldDB; Q9Z2I4; -.
DR SMR; Q9Z2I4; -.
DR STRING; 10090.ENSMUSP00000110690; -.
DR GlyGen; Q9Z2I4; 12 sites.
DR iPTMnet; Q9Z2I4; -.
DR PhosphoSitePlus; Q9Z2I4; -.
DR MaxQB; Q9Z2I4; -.
DR PaxDb; Q9Z2I4; -.
DR PRIDE; Q9Z2I4; -.
DR ProteomicsDB; 301635; -. [Q9Z2I4-1]
DR ProteomicsDB; 301636; -. [Q9Z2I4-2]
DR MGI; MGI:1343102; Robo3.
DR eggNOG; KOG4222; Eukaryota.
DR InParanoid; Q9Z2I4; -.
DR PhylomeDB; Q9Z2I4; -.
DR ChiTaRS; Robo3; mouse.
DR PRO; PR:Q9Z2I4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z2I4; protein.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
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; IPR032987; Robo3.
DR PANTHER; PTHR12231:SF236; PTHR12231:SF236; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
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 Alternative splicing; Chemotaxis; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Neurogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1366
FT /note="Roundabout homolog 3"
FT /id="PRO_0000031039"
FT TOPO_DOM 21..891
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..1366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 64..160
FT /note="Ig-like C2-type 1"
FT DOMAIN 166..253
FT /note="Ig-like C2-type 2"
FT DOMAIN 258..342
FT /note="Ig-like C2-type 3"
FT DOMAIN 347..440
FT /note="Ig-like C2-type 4"
FT DOMAIN 450..531
FT /note="Ig-like C2-type 5"
FT DOMAIN 558..652
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 672..766
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 771..869
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 540..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MS0"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 187..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 279..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 368..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 472..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10049565"
FT /id="VSP_010652"
FT VAR_SEQ 23..53
FT /note="ISNSSELLFGFNSSLAALNPSLLPPGDPSLN -> MSEAEGSLTLQSKPGLP
FT PVALPGYLELPSSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10049565"
FT /id="VSP_010653"
SQ SEQUENCE 1366 AA; 146054 MW; FAD8987DC9DE8C3F CRC64;
MLRYLLKTLL QMNLFADSLA RDISNSSELL FGFNSSLAAL NPSLLPPGDP SLNGSRVGPE
DAMPRIVEQP PDLVVSRGEP ATLPCRAEGR PRPNIEWYKN GARVATARED PRAHRLLLPS
GALFFPRIVH GRRSRPDEGV YTCVARNYLG AAASRNASLE VAVLRDDFRQ SPGNVVVAVG
EPAVMECVPP KGHPEPLVTW KKGKIKLKEE EGRITIRGGK LMMSHTFKSD AGMYMCVASN
MAGERESGAA ELVVLERPSF LRRPINQVVL ADAPVNFLCE VQGDPQPNLH WRKDDGELPA
GRYEIRSDHS LWIDQVSSED EGTYTCVAEN SVGRAEASGS LSVHVPPQFV TKPQNQTVAP
GANVSFQCET KGNPPPAIFW QKEGSQVLLF PSQSLQPMGR LLVSPRGQLN ITEVKIGDGG
YYVCQAVSVA GSILAKALLE IKGASIDGLP PIILQGPANQ TLVLGSSVWL PCRVIGNPQP
NIQWKKDERW LQGDDSQFNL MDNGTLHIAS IQEMDMGFYS CVAKSSIGEA TWNSWLRKQE
DWGASPGPAT GPSNPPGPPS QPIVTEVTAN SITLTWKPNP QSGATATSYV IEAFSQAAGN
TWRTVADGVQ LETYTISGLQ PNTIYLFLVR AVGAWGLSEP SPVSEPVQTQ DSSLSRPAED
PWKGQRGLAE VAVRMQEPTV LGPRTLQVSW TVDGPVQLVQ GFRVSWRIAG LDQGSWTMLD
LQSPHKQSTV LRGLPPGAQI QIKVQVQGQE GLGAESPFVT RSIPEEAPSG PPQGVAVALG
GDRNSSVTVS WEPPLPSQRN GVITEYQIWC LGNESRFHLN RSAAGWARSV TFSGLLPGQI
YRALVAAATS AGVGVASAPV LVQLPFPPAA EPGPEVSEGL AERLAKVLRK PAFLAGSSAA
CGALLLGFCA ALYRRQKQRK ELSHYTASFA YTPAVSFPHS EGLSGSSSRP PMGLGPAAYP
WLADSWPHPP RSPSAQEPRG SCCPSNPDPD DRYYNEAGIS LYLAQTARGA NASGEGPVYS
TIDPVGEELQ TFHGGFPQHS SGDPSTWSQY APPEWSEGDS GARGGQGKLL GKPVQMPSLS
WPEALPPPPP SCELSCPEGP EEELKGSSDL EEWCPPVPEK SHLVGSSSSG ACMVAPAPRD
TPSPTSSYGQ QSTATLTPSP PDPPQPPTDI PHLHQMPRRV PLGPSSPLSV SQPALSSHDG
RPVGLGAGPV LSYHASPSPV PSTASSAPGR TRQVTGEMTP PLHGHRARIR KKPKALPYRR
EHSPGDLPPP PLPPPELRDK LALGSAGSRQ HVFPRARAQW GEESGAGSAS RGPTSSQRGP
HPDGKESQGR GRGLEACRSP NSPQLPLDSC IWSTLKLSLV SFIPSK
