EVA1_CAEEL
ID EVA1_CAEEL Reviewed; 461 AA.
AC Q9XU98; P91865;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein eva-1;
DE AltName: Full=Enhancer of ventral-axon guidance defects of unc-40 mutants;
DE Flags: Precursor;
GN Name=eva-1; ORFNames=F32A7.3;
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 [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 [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH SAX-3 AND SLT-1.
RX PubMed=17901337; DOI=10.1126/science.1144874;
RA Fujisawa K., Wrana J.L., Culotti J.G.;
RT "The slit receptor EVA-1 coactivates a SAX-3/Robo mediated guidance signal
RT in C. elegans.";
RL Science 317:1934-1938(2007).
RN [3]
RP FUNCTION, INTERACTION WITH MADD-4; SLT-1 AND UNC-40, AND DOMAIN.
RX PubMed=25122090; DOI=10.1371/journal.pgen.1004521;
RA Chan K.K., Seetharaman A., Bagg R., Selman G., Zhang Y., Kim J., Roy P.J.;
RT "EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the
RT MADD-4 guidance cue in Caenorhabditis elegans.";
RL PLoS Genet. 10:E1004521-E1004521(2014).
CC -!- FUNCTION: Acts as a receptor for slt-1 (PubMed:17901337). Required for
CC the guidance of the AVM pioneer axon to the ventral nerve cord
CC (PubMed:17901337). Acts as a unc-40 coreceptor to enhance the
CC sensitivity of unc-40 to the madd-4 midline guidance cue to guide
CC muscle arm extensions (muscle arms) and AVM mechanosensory axons
CC towards the dorsoventral midline (PubMed:25122090).
CC {ECO:0000269|PubMed:17901337, ECO:0000269|PubMed:25122090}.
CC -!- SUBUNIT: Interacts with sax-3 (PubMed:17901337). Interacts with slt-1
CC (PubMed:17901337, PubMed:25122090). Interacts (via the SUEL-type lectin
CC domain) with madd-4 (PubMed:25122090). Interacts (via the transmembrane
CC domain) with unc-40 (PubMed:25122090). {ECO:0000269|PubMed:17901337,
CC ECO:0000269|PubMed:25122090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XU98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XU98-2; Sequence=VSP_044684;
CC -!- DEVELOPMENTAL STAGE: Widely expressed in the developing nervous system
CC during the period of embryogenesis. In first-larval-stage animals,
CC strong expression is observed in ventral and dorsal nerve cords and in
CC the PVM neurons but not in the AVM neurons.
CC {ECO:0000269|PubMed:17901337}.
CC -!- DOMAIN: The SUEL-type lectin domain, the transmembrane domain and the
CC C-terminal region are required for the guidance of the muscle arm
CC extensions to the midline neurons. {ECO:0000269|PubMed:25122090}.
CC -!- SIMILARITY: Belongs to the EVA1 family. {ECO:0000305}.
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DR EMBL; Z83107; CAB05503.2; -; Genomic_DNA.
DR EMBL; Z83107; CAB05506.2; -; Genomic_DNA.
DR PIR; T21628; T21628.
DR RefSeq; NP_493590.2; NM_061189.4. [Q9XU98-1]
DR RefSeq; NP_493591.2; NM_061190.4.
DR AlphaFoldDB; Q9XU98; -.
DR SMR; Q9XU98; -.
DR BioGRID; 38738; 7.
DR DIP; DIP-25574N; -.
DR IntAct; Q9XU98; 1.
DR MINT; Q9XU98; -.
DR STRING; 6239.F32A7.3a; -.
DR EPD; Q9XU98; -.
DR PaxDb; Q9XU98; -.
DR EnsemblMetazoa; F32A7.3a.1; F32A7.3a.1; WBGene00009304. [Q9XU98-1]
DR EnsemblMetazoa; F32A7.3b.1; F32A7.3b.1; WBGene00009304. [Q9XU98-2]
DR EnsemblMetazoa; F32A7.3b.2; F32A7.3b.2; WBGene00009304. [Q9XU98-2]
DR EnsemblMetazoa; F32A7.3b.3; F32A7.3b.3; WBGene00009304. [Q9XU98-2]
DR EnsemblMetazoa; F32A7.3b.4; F32A7.3b.4; WBGene00009304. [Q9XU98-2]
DR GeneID; 173355; -.
DR KEGG; cel:CELE_F32A7.3; -.
DR UCSC; F32A7.3a; c. elegans.
DR CTD; 173355; -.
DR WormBase; F32A7.3a; CE36144; WBGene00009304; eva-1. [Q9XU98-1]
DR WormBase; F32A7.3b; CE36145; WBGene00009304; eva-1. [Q9XU98-2]
DR eggNOG; KOG4729; Eukaryota.
DR InParanoid; Q9XU98; -.
DR OMA; LMCLTAF; -.
DR PhylomeDB; Q9XU98; -.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q9XU98; -.
DR PRO; PR:Q9XU98; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009304; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9XU98; baseline and differential.
DR GO; GO:0030054; C:cell junction; HDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031430; C:M band; HDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR Gene3D; 2.60.120.740; -; 1.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR Pfam; PF02140; Gal_Lectin; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..461
FT /note="Protein eva-1"
FT /id="PRO_0000420839"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 55..160
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT REGION 397..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044684"
SQ SEQUENCE 461 AA; 52073 MW; AC745CF2CAEB0B60 CRC64;
MNMHIVSPVL LLFWFGIIVT DGKLKSGFIG GSHHHEVNPI EGILRESLRS NRVQACDGER
ITLSCPRNTQ ISVQTGFYGR VVPENQLCPP QAGRKHSEAN LDPLSMIHHS STCDVIQAHT
RISELCDKRR KCTVVVDSNT FEDDPCPTTS KYLQMAYGCI PMSFDEETFC TPKPTDPPRP
EIRLECREGR RLAVYSAQMK TSPQCDPETE IRHECVSDVL PQVLRQCHAK EGCTLKSDGI
KGHCRHGHLH VVYVCVNEEI FSEEAIKGEL TSLETYLKEA DAMQKQDDER FFKDVNDKTQ
WERVVDSEPA KDPDVHQIAN DASYVTHDEY RMEKQDPPPI TERVEPNLVG VGHDLLQVVQ
FFKENKEKAV MCIVLAVSMA AIVVLSACII TRLCSSNKDS SRSSRRSRSR RSLETSKLVS
SNYGGSITPQ HMMQDIEDEQ FLRFSMGSAA TSNPHYSHYD F
