ID W5MD76_LEPOC Unreviewed; 1398 AA.
AC W5MD76;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Roundabout, axon guidance receptor, homolog 3 (Drosophila) {ECO:0000313|Ensembl:ENSLOCP00000006335.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006335.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000006335.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01018498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000006335; -.
DR Ensembl; ENSLOCT00000006343.1; ENSLOCP00000006335.1; ENSLOCG00000005170.1.
DR eggNOG; KOG4222; Eukaryota.
DR GeneTree; ENSGT00940000155457; -.
DR InParanoid; W5MD76; -.
DR OMA; NCCTTNH; -.
DR Proteomes; UP000018468; Linkage group LG26.
DR Bgee; ENSLOCG00000005170; Expressed in camera-type eye and 9 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR CDD; cd07693; IgC_1_Robo; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR PANTHER; PTHR44170:SF37; ROUNDABOUT GUIDANCE RECEPTOR 3; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004865910"
FT TRANSMEM 862..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 134..221
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 226..310
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 315..408
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 419..505
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 526..621
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 641..732
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 737..834
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 151834 MW; 97B249B55847587A CRC64;
MVFHLAWDAL LLSYALVGMA LGSRLRLEDA PPHIVEHPSD LIVSKGEPAT LNCKAEGRPA
PTVEWYKDGE RVETDRDDPR SHRMLLPSGS LFFLRIIHGR RSKPDEGVYV CVARNYLGEA
VSRNASLEVA ILRDDFRQAP SDVVVAAGEP AVMECIPPRG HPEPTISWKR NNIRVNDKDE
RITIRGGKLM ISNTRKSDAG MYVCVGTNMV GERDSDPAEL VVFERPTFVR RPVNQVVLAE
DSLDFLCEVV GDPTPTVRWR KEEGELPRGR HEIRSDNTLR LTQVRAEDEG AYTCVSENSV
GKAEASGTLQ VHVPPQIVVR PRDQIVAQGR TVTFLCGTKG NPPPAVFWQK EGSQILLFPS
QPPEQSGRFS VSLSGELTIS DVQSEDSGYY ICQAISVAGS ILTKALLEVE NAPSDRVPPI
IRQGPANQTL ALGATAQLQC HVMGNPLPSI QWEKDGQRIL GNDARISLME NGTLQITLLQ
ETDSGVYTCI ASSASGETSW SGILTVQESG APSAPQPSEP SLLPGPPQKP IVTNVTRNSV
TLTWQPNPHE GGAPVSSYII EAFSQSAGST WQTVADFVKL EKHTVGGLFP NTIYLFIIRA
VNSYGLSDPS PISEPVRTQD VSPTGQGVDH RQVQRELGEV VVRLLEPVVL SASSVQLSWT
VDSQSRYIQG YRLLYRPKGS AWLVQDVKAA PERSTVLADL RKGTEYEVKI RPYFDEFQGI
DSQLLIVHTP EEAPSAPPQS VTVVTVKLSN STSISVSWEP PPVEKRNGVI QEYKIWCLGN
ETRFHINKTV GGTVLSTTVT GLLPGILYQV EVAAVTSAGV GARSQPVSVL IKLPSDQPSA
PAEPGENVSL AEQITDVVKQ PAFIAGIGGA CWVILMGFSV WIYCRRKKRK ELSHYTASFA
YTPAVGFSHG EASGLINGRP GMLGTNMGNY PWLADSWPTT NLVHSGKESV TCCTAKHDSA
ERYYNEAGIS NYLSQTEKFS SGSNEGPIYS TIDPTSDDLR TFNSSYSQHA TPYASTPVMP
FATQGPYSPD QEGGHWMAQP GPSGSQYAQP DRSRTDNAVK LGKQKSMGKA VKTPSLNWTE
SLPPPPPAGE LEECVEESEE DGDDEELGSE EEDWCPPLPE RTYLTDGPSE DVPSPPPRGE
ASSPATSYGH QSTATLTPSP REEGRPSEDI PRLHHLDMPQ LARRVPCGPV PVPRAPSPPL
TQSNPNLVMV QEGSEVGTSP MHRPGHRRDQ SQGAVLSVDN VSSSGPGRAR LAPGDSTHTP
PGQKSRAKKK SSKTVQYRRE LNQGDLPPPP EPPPADEFPQ VSAGSLDCSR TSLERDGSAP
SSVERRAEHS TPHRKASAQR HREDEDIIPY SRPSFLSRGQ VSSNCSTTGS SSSRGSTGSR
GPVPGRSRPI AERSEEKR
//
