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Ephrin receptor 1 (EC 2.7.10.1) (Tyrosine-protein kinase Eph receptor) (Variable abnormal protein 1)

 VAB1_CAEEL              Reviewed;        1122 AA.
O61460; Q21477;
19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 156.
RecName: Full=Ephrin receptor 1;
EC=2.7.10.1 {ECO:0000269|PubMed:19853560};
AltName: Full=Tyrosine-protein kinase Eph receptor;
AltName: Full=Variable abnormal protein 1;
Flags: Precursor;
Name=vab-1; ORFNames=M03A1.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|EMBL:AAC38970.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF GLU-62; THR-63; GLU-195; GLY-917 AND CYS-966.
STRAIN=Bristol N2;
PubMed=9506518; DOI=10.1016/S0092-8674(00)81131-9;
George S.E., Simokat K., Hardin J., Chisholm A.D.;
"The VAB-1 Eph receptor tyrosine kinase functions in neural and
epithelial morphogenesis in C. elegans.";
Cell 92:633-643(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-238, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Bristol N2;
PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
Taoka M., Takahashi N., Isobe T.;
"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
elegans and suggests an atypical translocation mechanism for integral
membrane proteins.";
Mol. Cell. Proteomics 6:2100-2109(2007).
[4]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH
DAF-18, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
MUTAGENESIS OF GLY-917.
PubMed=19853560; DOI=10.1016/j.devcel.2009.08.009;
Brisbin S., Liu J., Boudreau J., Peng J., Evangelista M.,
Chin-Sang I.;
"A role for C. elegans Eph RTK signaling in PTEN regulation.";
Dev. Cell 17:459-469(2009).
[5]
FUNCTION.
PubMed=26903502; DOI=10.1242/dev.128934;
Dong B., Moseley-Alldredge M., Schwieterman A.A., Donelson C.J.,
McMurry J.L., Hudson M.L., Chen L.;
"EFN-4 functions in LAD-2-mediated axon guidance in Caenorhabditis
elegans.";
Development 143:1182-1191(2016).
-!- FUNCTION: Receptor for members of the ephrin family (By
similarity). Involved in interactions between neuronal substrate
cells and a migrating epithelial sheet in head epidermis
morphogenesis (PubMed:9506518). Also required for cell movements
following gastrulation and during ventral closure of the epidermis
(PubMed:9506518). Phosphorylates phosphatase daf-18/PTEN which
probably promotes daf-18 degradation (PubMed:19853560). By
inactivating daf-18, regulates positively insulin-like daf-2
signaling cascade (PubMed:9506518). Involved in axon guidance of
SDQL neurons during neurogenesis (PubMed:26903502). Regulates
oocyte maturation (PubMed:19853560).
{ECO:0000250|UniProtKB:Q62413, ECO:0000269|PubMed:19853560,
ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:9506518}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000269|PubMed:19853560}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
-!- ENZYME REGULATION: Dephosphorylated by daf-18.
{ECO:0000269|PubMed:19853560}.
-!- SUBUNIT: Interacts (via kinase domain) with daf-18 (via C-
terminus); the interaction is independent of vab-1 kinase
activity. {ECO:0000269|PubMed:19853560}.
-!- INTERACTION:
G5EE01:daf-18; NbExp=3; IntAct=EBI-1788319, EBI-2914422;
O44782:vpr-1; NbExp=2; IntAct=EBI-1788319, EBI-320991;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19853560};
Single-pass type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a {ECO:0000305};
IsoId=O61460-1; Sequence=Displayed;
Name=b {ECO:0000305};
IsoId=O61460-2; Sequence=VSP_050207;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: During ventral enclosure of the epidermis,
expression is seen in clusters of presumptive head neuronal cells
and several cells in the tail region. Early larvae show expression
in the nerve ring and ventral nerve cord. Strong expression is
also seen in the procorpus and terminal bulb of the pharynx.
Expression in the nervous system is seen through to adulthood
(PubMed:9506518, PubMed:19853560). Expressed in Z2/Z3 germline
precursor cells and in oocytes (at protein level).
{ECO:0000269|PubMed:19853560, ECO:0000269|PubMed:9506518}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19853560}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AF040269; AAC38970.1; -; Genomic_DNA.
EMBL; FO081295; CCD70550.1; -; Genomic_DNA.
EMBL; FO081295; CCD70551.1; -; Genomic_DNA.
PIR; T42400; T42400.
RefSeq; NP_494806.1; NM_062405.5. [O61460-1]
RefSeq; NP_494807.1; NM_062406.3. [O61460-2]
UniGene; Cel.5002; -.
ProteinModelPortal; O61460; -.
SMR; O61460; -.
BioGrid; 39149; 45.
IntAct; O61460; 2.
STRING; 6239.M03A1.1b; -.
iPTMnet; O61460; -.
PaxDb; O61460; -.
PeptideAtlas; O61460; -.
PRIDE; O61460; -.
EnsemblMetazoa; M03A1.1b; M03A1.1b; WBGene00006868. [O61460-1]
GeneID; 173794; -.
KEGG; cel:CELE_M03A1.1; -.
UCSC; M03A1.1a; c. elegans. [O61460-1]
CTD; 173794; -.
WormBase; M03A1.1a; CE25060; WBGene00006868; vab-1. [O61460-2]
WormBase; M03A1.1b; CE28617; WBGene00006868; vab-1. [O61460-1]
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000141182; -.
HOGENOM; HOG000233856; -.
InParanoid; O61460; -.
KO; K05110; -.
OMA; SNPTYTG; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; O61460; -.
BRENDA; 2.7.10.1; 1045.
Reactome; R-CEL-2682334; EPH-Ephrin signaling.
Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
Reactome; R-CEL-3928664; Ephrin signaling.
Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; O61460; -.
PRO; PR:O61460; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00006868; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005003; F:ephrin receptor activity; IDA:WormBase.
GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:WormBase.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; ISS:WormBase.
GO; GO:0007411; P:axon guidance; IMP:WormBase.
GO; GO:0007409; P:axonogenesis; IMP:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IMP:WormBase.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:WormBase.
GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Developmental protein; Glycoprotein; Kinase; Membrane; Neurogenesis;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1122 Ephrin receptor 1.
/FTId=PRO_0000016839.
TOPO_DOM 30 559 Extracellular. {ECO:0000255}.
TRANSMEM 560 580 Helical. {ECO:0000255}.
TOPO_DOM 581 1122 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 217 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 341 445 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 451 537 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 692 988 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 698 706 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 1120 1122 PDZ-binding. {ECO:0000255}.
COMPBIAS 199 338 Cys-rich.
ACT_SITE 849 849 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 748 748 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 667 667 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 673 673 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 885 885 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 1048 1048 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17761667}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 843 847 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_050207.
MUTAGEN 62 62 E->K: In ju8; most die as larvae.
{ECO:0000269|PubMed:9506518}.
MUTAGEN 63 63 T->I: In e699; most die as larvae.
{ECO:0000269|PubMed:9506518}.
MUTAGEN 195 195 E->K: In e856; most die as larvae.
{ECO:0000269|PubMed:9506518}.
MUTAGEN 917 917 G->E: In e2; about 80% animals reach
adulthood. No effect on interaction with
daf-18. Increased daf-18 protein levels
in embryos. May lack kinase activity.
{ECO:0000269|PubMed:19853560,
ECO:0000269|PubMed:9506518}.
MUTAGEN 966 966 C->F: In ju22; about 80% animals reach
adulthood. {ECO:0000269|PubMed:9506518}.
MUTAGEN 966 966 C->Y: In e1063; about 80% animals reach
adulthood. {ECO:0000269|PubMed:9506518}.
SEQUENCE 1122 AA; 125264 MW; 6E4A3037BB92A1D0 CRC64;
MRLYNSRILN PHQSIFILVL QCLITIVTSH QEVLFDLSKV GSDLKWDQVS LRHDRDDVWM
EETWRNPAAT DEKHANQRAY VTCNYDMINP SNWLFSHFIE VKTARRIYIE LLFNTRDCDA
YLNPKSCKET FSVYLKQFKT SRPGSTKIEK ERFSEDIDNW KNIGRLARSN SNMTTETLGM
EIDSDTKTIR IAFEEQGICL SLLNVKIYYR ICDEFTDQLV YFRPQVTGPK ETDMVRMNGS
CIPNASKKIP GVDLIGLCMS TGSGIKTSGE CVCDSGYSQI ADSNGARCES CPTNTYKPKG
QSLCKSCPSN SISSEAASSC RCLNGYFRAE DELISMPCTQ PPSRPIKLVA NAITATSTRL
SWNEPSSLGG RPEIWYEVKC SGRGECGTVV MTPGDKKLST RSVQINGLRP SSDYTFLVFA
KNKVSAQFPE FSEKNAVIDI RTRSEEEDVP PVSHLRVDAS QSDGITIAWS VSDSDVSDFE
VEVRPAIVKK RTFETRHVNM TYTTFIGLNP ETVYQFRVRI RDDLRWSQPI SYQLGRGLMS
SPSSNEVEES QFLNQTGSAL LIIIALILIV IAVALCMIVV QKKSKNRKQM SDLDVLDTYK
QDSMTPDYHT TSRHHHHQGN LPATLHEQLR STTKLNAPLI PSFGSPISQP PPYYGGVHPN
SGKYKTYVDP TTYEDPYQAL IEFTFDISPN DVFITQVIGG GEFGDVCLGG LSKNSPAAAK
WSVSNTTMGR GGGGGGYESE PYETVAIKTL KSGSSAKAKA EFLTEATIMG QFSHPNVIRL
IGVVTSAEPV MIVAEYMANG SLDQFLRNTD QRGEKVHWEK ITEMLYGIAS GMKYLTDMGY
VHRVSFLRDL AARNVLLDME LRCKIADFGL SRGVRSEGSS VEPEYTTNGG KIPVRWTAPE
AITHRKFTPS SDVWSFGVVI WEVCSFGERP YWDWTNQKVI SEVMIGYRLP PPMDCPMGLY
RIAQWCWKME RHERPTFTQL LATFHKYILQ PTLIEHDPGE LPRRVQSQSA LNTYGSVNVG
VVPTPPSSAA PMPSLDDFLR QIGLNHVYGQ LVSNNIHSVS DLANTSHLDL LAYGLMSAEC
STVRDGLNGR ISGSPPGSSG TIHATTRGTR TTRPPREEGF FV


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