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Ephrin-4 (Protein male abnormal 26)

 EFN4_CAEEL              Reviewed;         348 AA.
O44516;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 2.
30-AUG-2017, entry version 122.
RecName: Full=Ephrin-4;
AltName: Full=Protein male abnormal 26;
Flags: Precursor;
Name=efn-4; Synonyms=mab-26; ORFNames=F56A11.3;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
STRAIN=Bristol N2;
PubMed=12403719; DOI=10.1242/dev.00122;
Chin-Sang I.D., Moseley S.L., Ding M., Harrington R.J., George S.E.,
Chisholm A.D.;
"The divergent C. elegans ephrin EFN-4 functions in embryonic
morphogenesis in a pathway independent of the VAB-1 Eph receptor.";
Development 129:5499-5510(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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]
IDENTIFICATION, AND NOMENCLATURE.
PubMed=10635316; DOI=10.1016/S1097-2765(00)80220-8;
Wang X., Roy P.J., Holland S.J., Zhang L.W., Culotti J.G., Pawson T.;
"Multiple ephrins control cell organization in C. elegans using
kinase-dependent and -independent functions of the VAB-1 Eph
receptor.";
Mol. Cell 4:903-913(1999).
[4]
FUNCTION.
PubMed=12679110; DOI=10.1016/S0012-1606(02)00129-X;
Hahn A.C., Emmons S.W.;
"The roles of an ephrin and a semaphorin in patterning cell-cell
contacts in C. elegans sensory organ development.";
Dev. Biol. 256:379-388(2003).
[5]
FUNCTION.
PubMed=15030761; DOI=10.1016/S1534-5807(04)00057-7;
Ikegami R., Zheng H., Ong S.-H., Culotti J.G.;
"Integration of semaphorin-2A/MAB-20, ephrin-4, and UNC-129 TGF-beta
signaling pathways regulates sorting of distinct sensory rays in C.
elegans.";
Dev. Cell 6:383-395(2004).
[6]
FUNCTION, INTERACTION WITH LAD-2, DEVELOPMENTAL STAGE, AND MUTAGENESIS
OF 328-SER--TYR-348.
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: Regulates the formation or stabilization of cell-cell
contacts at several stages of epithelial morphogenesis
(PubMed:12679110). In early embryonic development, involved in
ventral closure of the epidermis (PubMed:12403719). During male
tail morphogenesis, regulates precursor cell sorting together with
mab-20 and allows the formation of distinct sensory rays
(PubMed:15030761). Probably acts as a ligand for lad-2 to regulate
axon guidance of several neurons including SDQL, SDQR, SMD and PLN
neurons during neurogenesis (PubMed:26903502).
{ECO:0000269|PubMed:12403719, ECO:0000269|PubMed:12679110,
ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:26903502}.
-!- SUBUNIT: Interacts with lat-2. {ECO:0000269|PubMed:26903502}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Expressed in the developing nervous system
(PubMed:12403719). Expressed in head and tail neurons, nerve ring,
ventral nerve cord, lateral neurons, CAN neuron, seam cells and
vulva cells (PubMed:26903502). {ECO:0000269|PubMed:12403719,
ECO:0000269|PubMed:26903502}.
-!- PTM: May undergo proteolysis by metalloprotease sup-17 to give
rise to a soluble form. {ECO:0000305|PubMed:26903502}.
-!- DISRUPTION PHENOTYPE: Worms have widespread defects in embryonic
morphogenesis of the posterior body and defects in postembryonic
male tail morphogenesis. {ECO:0000269|PubMed:12403719}.
-!- MISCELLANEOUS: In contrast to other ephrins, does not seem to
signal through the vab-1 receptor. {ECO:0000269|PubMed:12403719}.
-!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
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EMBL; AF410936; AAL05561.1; -; mRNA.
EMBL; FO080624; CCD65257.1; -; Genomic_DNA.
PIR; T32645; T32645.
RefSeq; NP_499947.1; NM_067546.4.
UniGene; Cel.19328; -.
ProteinModelPortal; O44516; -.
BioGrid; 42043; 3.
STRING; 6239.F56A11.3; -.
EPD; O44516; -.
PaxDb; O44516; -.
EnsemblMetazoa; F56A11.3; F56A11.3; WBGene00001165.
GeneID; 176882; -.
KEGG; cel:CELE_F56A11.3; -.
UCSC; F56A11.3; c. elegans.
CTD; 176882; -.
WormBase; F56A11.3; CE29503; WBGene00001165; efn-4.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
HOGENOM; HOG000112341; -.
InParanoid; O44516; -.
OMA; PIPNGKE; -.
OrthoDB; EOG091G0LSC; -.
PhylomeDB; O44516; -.
SignaLink; O44516; -.
PRO; PR:O44516; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00001165; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0042074; P:cell migration involved in gastrulation; IMP:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
GO; GO:0030155; P:regulation of cell adhesion; IMP:WormBase.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR031328; Ephrin.
InterPro; IPR001799; Ephrin_RBD.
PANTHER; PTHR11304; PTHR11304; 1.
Pfam; PF00812; Ephrin; 1.
ProDom; PD002533; Ephrin; 1.
SUPFAM; SSF49503; SSF49503; 1.
PROSITE; PS51551; EPHRIN_RBD_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Developmental protein;
Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Neurogenesis; Reference proteome; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 329 Ephrin-4.
/FTId=PRO_0000248550.
PROPEP 330 348 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000248551.
DOMAIN 21 178 Ephrin RBD. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
LIPID 329 329 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 91 {ECO:0000255|PROSITE-ProRule:PRU00884}.
DISULFID 79 167 {ECO:0000255|PROSITE-ProRule:PRU00884}.
MUTAGEN 328 348 Missing: No defect in SDQL axon
migration. Restores SDQL axon migration
in a sup-17 (n316) mutant background.
{ECO:0000269|PubMed:26903502}.
SEQUENCE 348 AA; 39593 MW; 851E9EB07C0048FF CRC64;
MKQFFEFLIT TFLLLGLAAA DEHIVYWNST NSLFRNRQPT IEVRMGDVVR FVCPDNEEGR
NDGEYLIVYE VTEFAMDDCA LESHSREVIR CAPEGTAEKV LRTQQLSGGR REDWKKQKVP
PKNVAQLIRQ LNPIPNGKEY QPGQTYYYMT TSTGKANGTN HRMYGLCESQ NMRLSMKVSA
SQPHPTRRAP TRRQEDFVTT ASAELMGGQE DEDSDNDNAH LLPRDLEGST NPKFRRPSQL
ETAGVENQQF MKVVQMAQAG KTGTFENEKE AIAQKSSEKD GWHPVNVQYV ADLMNNAYQN
ADERISYQRD FEIHEENDLA VKSLEYSSSS TSLSTNFAIL LAVIYVLY


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