GENTAUR Molecular Products.

 EFN4_CAEEL              Reviewed;         348 AA.
 O44516;
 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2001, sequence version 2.
 05-DEC-2018, entry version 130.
 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;
 Rhabditina; Rhabditomorpha; 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; -.
 SMR; O44516; -.
 BioGrid; 42043; 3.
 STRING; 6239.F56A11.3; -.
 EPD; O44516; -.
 PaxDb; O44516; -.
 PRIDE; 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.
 GeneTree; ENSGT00940000175201; -.
 HOGENOM; HOG000112341; -.
 InParanoid; O44516; -.
 OMA; PIPNGKE; -.
 OrthoDB; EOG091G0LSC; -.
 PhylomeDB; O44516; -.
 SignaLink; O44516; -.
 PRO; PR:O44516; -.
 Proteomes; UP000001940; Chromosome IV.
 Bgee; WBGene00001165; Expressed in 5 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
 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:1902667; P:regulation of axon guidance; IMP:UniProtKB.
 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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