EFN4_CAEBR
ID EFN4_CAEBR Reviewed; 354 AA.
AC Q624D2; A8WR91;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ephrin-4;
DE Flags: Precursor;
GN Name=efn-4; ORFNames=CBG01610;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Regulates the formation or stabilization of cell-cell
CC contacts at several stages of epithelial morphogenesis. In early
CC embryonic development, involved in ventral closure of the epidermis.
CC During male tail morphogenesis, regulates precursor cell sorting
CC together with mab-20 and allows the formation of distinct sensory rays.
CC Probably acts as a ligand for lad-2 to regulate axon guidance of
CC several neurons including SDQL, SDQR, SMD and PLN neurons during
CC neurogenesis. {ECO:0000250|UniProtKB:O44516}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- PTM: May undergo proteolysis by metalloprotease sup-17 to give rise to
CC a soluble form. {ECO:0000250|UniProtKB:O44516}.
CC -!- MISCELLANEOUS: In contrast to other ephrins, does not seem to signal
CC through the vab-1 receptor. {ECO:0000250|UniProtKB:O44516}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; HE601298; CAP22999.1; -; Genomic_DNA.
DR RefSeq; XP_002634068.1; XM_002634022.1.
DR AlphaFoldDB; Q624D2; -.
DR SMR; Q624D2; -.
DR STRING; 6238.CBG01610; -.
DR EnsemblMetazoa; CBG01610.1; CBG01610.1; WBGene00024824.
DR GeneID; 8576063; -.
DR KEGG; cbr:CBG_01610; -.
DR CTD; 8576063; -.
DR WormBase; CBG01610; CBP14187; WBGene00024824; Cbr-efn-4.
DR eggNOG; KOG3858; Eukaryota.
DR HOGENOM; CLU_779010_0_0_1; -.
DR InParanoid; Q624D2; -.
DR OMA; FVCPDNE; -.
DR OrthoDB; 1247864at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0043025; C:neuronal cell body; IEA:EnsemblMetazoa.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:EnsemblMetazoa.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:1902667; P:regulation of axon guidance; IEA:EnsemblMetazoa.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:EnsemblMetazoa.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Neurogenesis; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..335
FT /note="Ephrin-4"
FT /id="PRO_0000248548"
FT PROPEP 336..354
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000248549"
FT DOMAIN 23..173
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 335
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 80..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 354 AA; 39730 MW; 19BA81C4C6B1491B CRC64;
MKRPLDFLLA ICLILLRSST FADEHTVHWN STNSMFRNRH PSIEVRLGDV VRFVCPDNEG
RKNGEYLTVY EVSEFAMGEC ALESNSREVI KCGVDTNTEK IIRTHQLPIG ESREPPKNVA
QFIRSVNPIP NGKEYQPGQT YYYITTSSGK PGGIGQQMYG LCVSKNMRLS MKVLSSQPTP
SPSSKPARSR TDARRQEDFI TKSSAELMGG QEDEDSENDN AHLLPRDLEI ATNPKFRRPS
QFDQAAASAG VLDGQFLKVV QMAKEGKTGT FENDREVQKS AEKDAWDPIN RHYVADLMNS
AYKNANDRVV YQREPDFLIH EEDISTNSLG YSSSSSSSLP TFLIVFLIAV NLLF
