ROBO2_MOUSE
ID ROBO2_MOUSE Reviewed; 1470 AA.
AC Q7TPD3; Q8BJ59;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Roundabout homolog 2;
DE Flags: Precursor;
GN Name=Robo2; Synonyms=Kiaa1568;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-1470 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15091338; DOI=10.1016/s0896-6273(04)00179-5;
RA Long H., Sabatier C., Ma L., Plump A., Yuan W., Ornitz D.M., Tamada A.,
RA Murakami F., Goodman C.S., Tessier-Lavigne M.;
RT "Conserved roles for slit and robo proteins in midline commissural axon
RT guidance.";
RL Neuron 42:213-223(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157 AND SER-1159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for SLIT2, and probably SLIT1, which are thought to
CC act as molecular guidance cue 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.
CC {ECO:0000269|PubMed:15091338}.
CC -!- SUBUNIT: Interacts with SLIT2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TPD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TPD3-2; Sequence=VSP_010648, VSP_010649;
CC -!- TISSUE SPECIFICITY: Expressed in embryonal spinal chord.
CC {ECO:0000269|PubMed:15091338}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 11.5 dpc in spinal chord.
CC {ECO:0000269|PubMed:15091338}.
CC -!- DISRUPTION PHENOTYPE: Mice show defects in commissural axon guidance in
CC spinal cord including an altered lateral and ventral funiculi
CC projection. The phenotype resembles that of a SLIT1;SLIT2;SLIT3 triple
CC mutant. {ECO:0000269|PubMed:15091338}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
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DR EMBL; BC055333; AAH55333.1; -; mRNA.
DR EMBL; AK129396; BAC98206.1; -; mRNA.
DR AlphaFoldDB; Q7TPD3; -.
DR SMR; Q7TPD3; -.
DR IntAct; Q7TPD3; 1.
DR STRING; 10090.ENSMUSP00000112776; -.
DR GlyConnect; 2688; 12 N-Linked glycans (2 sites).
DR GlyGen; Q7TPD3; 6 sites, 12 N-linked glycans (2 sites).
DR iPTMnet; Q7TPD3; -.
DR PhosphoSitePlus; Q7TPD3; -.
DR MaxQB; Q7TPD3; -.
DR PaxDb; Q7TPD3; -.
DR PRIDE; Q7TPD3; -.
DR ProteomicsDB; 300508; -. [Q7TPD3-1]
DR ProteomicsDB; 300509; -. [Q7TPD3-2]
DR ABCD; Q7TPD3; 22 sequenced antibodies.
DR UCSC; uc007zrf.1; mouse. [Q7TPD3-1]
DR MGI; MGI:1890110; Robo2.
DR eggNOG; KOG4222; Eukaryota.
DR InParanoid; Q7TPD3; -.
DR ChiTaRS; Robo2; mouse.
DR PRO; PR:Q7TPD3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TPD3; protein.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0035904; P:aorta development; IGI:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; IGI:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0003272; P:endocardial cushion formation; IGI:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0050925; P:negative regulation of negative chemotaxis; ISO:MGI.
DR GO; GO:0021891; P:olfactory bulb interneuron development; IMP:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; IDA:BHF-UCL.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IGI:BHF-UCL.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IGI:BHF-UCL.
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 Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 4.
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 Alternative splicing; Chemotaxis; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1470
FT /note="Roundabout homolog 2"
FT /id="PRO_0000031037"
FT TOPO_DOM 22..863
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 885..1470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..220
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..309
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..413
FT /note="Ig-like C2-type 4"
FT DOMAIN 422..508
FT /note="Ig-like C2-type 5"
FT DOMAIN 528..622
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 641..739
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 743..840
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1036..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1157
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 443..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 807..946
FT /note="GLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITENNNSITEQITD
FT VVKQPAFIAGIGGACWVILMGFSIWLYWRRKKRKGLSNYAVTFQRGDGGLMSNGSRPGL
FT LNAGDPNYPWLADSWPATSLPVNNSNSGP -> ASTSRPPEWNYSGI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010648"
FT VAR_SEQ 947..1470
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010649"
SQ SEQUENCE 1470 AA; 161190 MW; 3C61DE40DA39109E CRC64;
MNPLMFTLLL LFGFLCIQID GSRLRQEDFP PRIVEHPSDV IVSKGEPTTL NCKAEGRPTP
TIEWYKDGER VETDKDDPRS HRMLLPSGSL FFLRIVHGRR SKPDEGSYVC VARNYLGEAV
SRNASLEVAL LRDDFRQNPT DVVVAAGEPA ILECQPPRGH PEPTIYWKKD KVRIDDKEER
ISIRGGKLMI SNTRKSDAGM YTCVGTNMVG ERDSDPAELT VFERPTFLRR PINQVVLEEE
AVEFRCQVQG DPQPTVRWKK DDADLPRGRY DIKDDYTLRI KKAMSTDEGT YVCIAENRVG
KVEASATLTV RVRPVAPPQF VVRPRDQIVA QGRTVTFPCE TKGNPQPAVF WQKEGSQNLL
FPNQPQQPNS RCSVSPTGDL TITNIQRSDA GYYICQALTV AGSILAKAQL EVTDVLTDRP
PPIILQGPIN QTLAVDGTAL LKCKATGEPL PVISWLKEGF TFLGRDPRAT IQDQGTLQIK
NLRISDTGTY TCVATSSSGE TSWSAVLDVT ESGATISKNY DMNDLPGPPS KPQVTDVSKN
SVTLSWQPGT PGVLPASAYI IEAFSQSVSN SWQTVANHVK TTLYTVRGLR PNTIYLFMVR
AINPQGLSDP SPMSDPVRTQ DISPPAQGVD HRQVQKELGD VVVRLHNPVV LTPTTVQVTW
TVDRQPQFIQ GYRVMYRQTS GLQASTVWQN LDAKVPTERS AVLVNLKKGV TYEIKVRPYF
NEFQGMDSES KTVRTTEEAP SAPPQSVTVL TVGSHNSTSI SVSWDPPPAD HQNGIIQEYK
IWCLGNETRF HINKTVDAAI RSVVIGGLFP GIQYRVEVAA STSAGVGVKS EPQPIIIGGR
NEVVITENNN SITEQITDVV KQPAFIAGIG GACWVILMGF SIWLYWRRKK RKGLSNYAVT
FQRGDGGLMS NGSRPGLLNA GDPNYPWLAD SWPATSLPVN NSNSGPNEIG NFGRGDVLPP
VPGQGDKTAT MLSDGAIYSS IDFTTKTTYN SSSQITQATP YATTQILHSN SIHELAVDLP
DPQWKSSVQQ KTDLMGFGYS LPDQNKGNNG GKGGKKKKTK NSSKAQKNNG STWANVPLPP
PPVQPLPGTE LGHYAAEQEN GYDSDSWCPP LPVQTYLHQG MEDELEEDED RVPTPPVRGV
ASSPAISFGQ QSTATLTPSP REEMQPMLQA HLDELTRAYQ FDIAKQTWHI QSNTPPPQPP
APPLGYVSGA LISDLETDVP DEDADDEEEP LEIPRPLRAL DQTPGSSMDN LDSSVTGKAF
SSSQRQRPTS PFSTDSNTSA AQNQSQRPRP TKKHKGGRMD PQPVLPHRRE GMPDDLPPPP
DPPPGQGLRQ QIGLSQHSGN VENSTERKGS SLERQQAANL EDTKSSLDCP AKTVLEWQRQ
TQDWINSTER QEETRKAPHK QGVGSEESLV PYSKPSFPSP GGHSSSGTSS SKGSTGPRKA
DVLRGSHQRN ANDLLDIGYV GSNSQGQFTE
