ID   ROBO4_RAT               Reviewed;         961 AA.
AC   Q80W87;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Roundabout homolog 4;
DE   Flags: Precursor;
GN   Name=Robo4;
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 VARIANT PRO-70.
RA   Roberts K.G., Stewart L.M.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for Slit proteins, at least for SLIT2, and seems to
CC       be involved in angiogenesis and vascular patterning. May mediate the
CC       inhibition of primary endothelial cell migration by Slit proteins (By
CC       similarity). Involved in the maintenance of endothelial barrier
CC       organization and function (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q8WZ75}.
CC   -!- SUBUNIT: Interacts with SLIT2 and ENAH. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC       {ECO:0000305}.
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DR   EMBL; AY277635; AAP32918.1; -; mRNA.
DR   RefSeq; NP_852040.1; NM_181375.1.
DR   AlphaFoldDB; Q80W87; -.
DR   SMR; Q80W87; -.
DR   STRING; 10116.ENSRNOP00000044365; -.
DR   GlyGen; Q80W87; 9 sites.
DR   iPTMnet; Q80W87; -.
DR   PhosphoSitePlus; Q80W87; -.
DR   PaxDb; Q80W87; -.
DR   PRIDE; Q80W87; -.
DR   GeneID; 100911068; -.
DR   UCSC; RGD:727947; rat.
DR   CTD; 100911068; -.
DR   RGD; 727947; Robo4.
DR   eggNOG; KOG4222; Eukaryota.
DR   InParanoid; Q80W87; -.
DR   OrthoDB; 242944at2759; -.
DR   PhylomeDB; Q80W87; -.
DR   PRO; PR:Q80W87; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 4.
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   Pfam; PF07679; I-set; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..961
FT                   /note="Roundabout homolog 4"
FT                   /id="PRO_0000031042"
FT   DOMAIN          42..142
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          148..235
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          259..356
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          358..453
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          544..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         823
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZ75"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        691
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        169..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         70
FT                   /note="L -> P"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   961 AA;  102580 MW;  1D21E7D4B611899F CRC64;
     MGQGEELRAA VDSGGMGLLG TKCPLPLLLL FIMGGKALDS PPQILVHPQD QLLQGSGPAK
     MSCRASGQPL PTIRWLLNGQ PLSMATPDLH YLQSDGTLLL HRPPTHGRPQ DDQNILSAIL
     GVYTCEASNR LGTAVSRGAR LSVAVLQEDF RIQPRDTVAV VGESLVLECG PPWGYPKPSV
     SWWKDGKPLV LQPGKRTVSG DSLMVARAEK NDTGTYMCMA TNNAGQRESR AARVSIQESP
     DHKEHLELLA VRIQLENVTL LNPEPVKGPK PGPAVWLSWK VSGPAAPAQS YTALFRAQRD
     PRDQGSPWTE VLLDGLLNAK LGGLRWGQDY EFKVRPSSGR ARGPDSNVLL LRLPEQVPSA
     PPQEVTLRPG NGSVFVSWAP PPAENHNGFI RGYQVWSLGN ASLPAANWTV VGEQTQLEIA
     ARMPGSYCVQ VAAVTGAGAG EPSIPVCLLL EQAMEQSARD PSKHVSWTLE QLRATLKRPE
     VIASGAVLLW LLLLGIAVCI YRRRKAGVHL GPGLYRYTSE DAILKHRMDH SDSPWLADTW
     RSTSGSRDLS SSSSLSSRLG VDPRDPLDGR RSLISWDPRS PGVPLLPDTS TFYGSLIAEQ
     TSSPPVRPSP QTPAARRLPP KLTGTSSPWA SSDSLCSRRG LCSPRMSLAP AEAWKAKKKQ
     ELHQANSSPL LQGSHPMEIW AWELGSRASK NLSQSPGPNT CSPREAPGAV VAWRALGPQL
     HRNSSELAAR PLPPTPLSLR GAPSHDPQSQ CVEKLQAPSS DPLPAAPLSV LNSSRPSSPQ
     ASFLSVPSPG SSNLSSSSLS SLEEEDQDSV LTPEEVALCL ELSDGEETPT NSVSPMPRAP
     SPPATYGYIS IPTSSGLADM GRAGGGVGSE VGNLLCPPRL CPTPTPSEGS LANGWGSASE
     DNVPSARASL VSSSDGSFLA DAHFARALAV AVDSFGFSLE PREADCVFTG MWARPPPLEW
     T