SAX3_CAEEL
ID SAX3_CAEEL Reviewed; 1273 AA.
AC G5EBF1; H2KYQ9;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein sax-3;
DE AltName: Full=Sensory axon guidance 3;
DE Flags: Precursor;
GN Name=sax-3 {ECO:0000312|WormBase:ZK377.2b};
GN ORFNames=ZK377.2 {ECO:0000312|WormBase:ZK377.2b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9458046; DOI=10.1016/s0092-8674(00)80916-2;
RA Zallen J.A., Yi B.A., Bargmann C.I.;
RT "The conserved immunoglobulin superfamily member SAX-3/Robo directs
RT multiple aspects of axon guidance in C. elegans.";
RL Cell 92:217-227(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=10993679; DOI=10.1006/dbio.2000.9853;
RA Branda C.S., Stern M.J.;
RT "Mechanisms controlling sex myoblast migration in Caenorhabditis elegans
RT hermaphrodites.";
RL Dev. Biol. 226:137-151(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=28901288; DOI=10.7554/elife.29257;
RA Kim B., Emmons S.W.;
RT "Multiple conserved cell adhesion protein interactions mediate neural
RT wiring of a sensory circuit in C. elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Required to confine migrating sex myoblasts to the ventral
CC muscle quadrants during their migration through the body and for
CC multiple aspects of sensory, motor, and interneuron axon guidance.
CC {ECO:0000269|PubMed:10993679, ECO:0000269|PubMed:9458046}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:ZK377.2b};
CC IsoId=G5EBF1-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZK377.2a};
CC IsoId=G5EBF1-2; Sequence=VSP_060409;
CC -!- TISSUE SPECIFICITY: Expressed in the AVG interneuron and the male-
CC specific sensory neuron HOA. {ECO:0000269|PubMed:28901288}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO/SAX3
CC family. {ECO:0000305}.
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DR EMBL; AF041053; AAC38848.1; -; mRNA.
DR EMBL; BX284606; CCD64328.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD64327.1; -; Genomic_DNA.
DR PIR; T42405; T42405.
DR RefSeq; NP_001024990.1; NM_001029819.3. [G5EBF1-1]
DR RefSeq; NP_741748.2; NM_171652.4. [G5EBF1-2]
DR AlphaFoldDB; G5EBF1; -.
DR SMR; G5EBF1; -.
DR BioGRID; 45576; 30.
DR STRING; 6239.ZK377.2b; -.
DR EPD; G5EBF1; -.
DR PaxDb; G5EBF1; -.
DR PeptideAtlas; G5EBF1; -.
DR EnsemblMetazoa; ZK377.2a.1; ZK377.2a.1; WBGene00004729. [G5EBF1-2]
DR EnsemblMetazoa; ZK377.2b.1; ZK377.2b.1; WBGene00004729. [G5EBF1-1]
DR GeneID; 180637; -.
DR KEGG; cel:CELE_ZK377.2; -.
DR CTD; 180637; -.
DR WormBase; ZK377.2a; CE25688; WBGene00004729; sax-3. [G5EBF1-2]
DR WormBase; ZK377.2b; CE31267; WBGene00004729; sax-3. [G5EBF1-1]
DR eggNOG; KOG4222; Eukaryota.
DR GeneTree; ENSGT00940000167162; -.
DR HOGENOM; CLU_003227_0_0_1; -.
DR InParanoid; G5EBF1; -.
DR OMA; QGAAYMF; -.
DR OrthoDB; 173520at2759; -.
DR PhylomeDB; G5EBF1; -.
DR PRO; PR:G5EBF1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004729; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0008046; F:axon guidance receptor activity; IDA:WormBase.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:WormBase.
DR GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR GO; GO:1905489; P:regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:WormBase.
DR GO; GO:0097374; P:sensory neuron axon guidance; IMP:UniProtKB.
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; 2.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1273
FT /note="Protein sax-3"
FT /id="PRO_0000420957"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 31..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..222
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..312
FT /note="Ig-like C2-type 3"
FT DOMAIN 317..411
FT /note="Ig-like C2-type 4"
FT DOMAIN 425..511
FT /note="Ig-like C2-type 5"
FT DOMAIN 533..628
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 653..750
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 755..849
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1033..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 52..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 154..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 338..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 446..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1142..1145
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060409"
SQ SEQUENCE 1273 AA; 139428 MW; 013E766B51A7BAD7 CRC64;
MFNRKTLLCT ILLVLQAVIR SFCEDASNLA PVIIEHPIDV VVSRGSPATL NCGAKPSTAK
ITWYKDGQPV ITNKEQVNSH RIVLDTGSLF LLKVNSGKNG KDSDAGAYYC VASNEHGEVK
SNEGSLKLAM LREDFRVRPR TVQALGGEMA VLECSPPRGF PEPVVSWRKD DKELRIQDMP
RYTLHSDGNL IIDPVDRSDS GTYQCVANNM VGERVSNPAR LSVFEKPKFE QEPKDMTVDV
GAAVLFDCRV TGDPQPQITW KRKNEPMPVT RAYIAKDNRG LRIERVQPSD EGEYVCYARN
PAGTLEASAH LRVQAPPSFQ TKPADQSVPA GGTATFECTL VGQPSPAYFW SKEGQQDLLF
PSYVSADGRT KVSPTGTLTI EEVRQVDEGA YVCAGMNSAG SSLSKAALKV TTKAVTGNTP
AKPPPTIEHG HQNQTLMVGS SAILPCQASG KPTPGISWLR DGLPIDITDS RISQHSTGSL
HIADLKKPDT GVYTCIAKNE DGESTWSASL TVEDHTSNAQ FVRMPDPSNF PSSPTQPIIV
NVTDTEVELH WNAPSTSGAG PITGYIIQYY SPDLGQTWFN IPDYVASTEY RIKGLKPSHS
YMFVIRAENE KGIGTPSVSS ALVTTSKPAA QVALSDKNKM DMAIAEKRLT SEQLIKLEEV
KTINSTAVRL FWKKRKLEEL IDGYYIKWRG PPRTNDNQYV NVTSPSTENY VVSNLMPFTN
YEFFVIPYHS GVHSIHGAPS NSMDVLTAEA PPSLPPEDVR IRMLNLTTLR ISWKAPKADG
INGILKGFQI VIVGQAPNNN RNITTNERAA SVTLFHLVTG MTYKIRVAAR SNGGVGVSHG
TSEVIMNQDT LEKHLAAQQE NESFLYGLIN KSHVPVIVIV AILIIFVVII IAYCYWRNSR
NSDGKDRSFI KINDGSVHMA SNNLWDVAQN PNQNPMYNTA GRMTMNNRNG QALYSLTPNA
QDFFNNCDDY SGTMHRPGSE HHYHYAQLTG GPGNAMSTFY GNQYHDDPSP YATTTLVLSN
QQPAWLNDKM LRAPAMPTNP VPPEPPARYA DHTAGRRSRS SRASDGRGTL NGGLHHRTSG
SQRSDSPPHT DVSYVQLHSS DGTGSSKERT GERRTPPNKT LMDFIPPPPS NPPPPGGHVY
DDIFQTATRR QLNRGSTPRE DTYDSVSDGA FARVDVNARP TSRNRNLGGR PLKGKRDDDS
QRSSLMMDDD GGSSEADGEN SEGDVPRGGV RKAVPRMGIS ASTLAHSCYG TNGTAQRFRS
IPRNNGIVTQ EQT
