Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin-A4

Gene

EFNA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.

GO - Molecular functioni

  1. ephrin receptor binding Source: UniProtKB
  2. transmembrane-ephrin receptor activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: GO_Central
  2. bone remodeling Source: GO_Central
  3. cell-cell signaling Source: ProtInc
  4. ephrin receptor signaling pathway Source: GO_Central
  5. osteoclast differentiation Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_228063. EPHA-mediated growth cone collapse.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52798.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-A4
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 4
Short name:
LERK-4
Gene namesi
Name:EFNA4
Synonyms:EPLG4, LERK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3224. EFNA4.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27659.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 170145Ephrin-A4PRO_0000008373Add
BLAST
Propeptidei171 – 20131Removed in mature formSequence AnalysisPRO_0000008374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi58 ↔ 99PROSITE-ProRule annotation
Disulfide bondi86 ↔ 144PROSITE-ProRule annotation
Lipidationi170 – 1701GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP52798.
PRIDEiP52798.

PTM databases

PhosphoSiteiP52798.

Expressioni

Tissue specificityi

Expressed in the adult spleen, lymph node, prostate, ovary, small intestine, and colon, and in fetal heart, lung, liver and kidney. Also detected in hematopoietic cell lines.

Gene expression databases

BgeeiP52798.
CleanExiHS_EFNA4.
GenevestigatoriP52798.

Organism-specific databases

HPAiCAB021350.

Interactioni

Protein-protein interaction databases

BioGridi108265. 1 interaction.
DIPiDIP-48295N.
IntActiP52798. 1 interaction.
STRINGi9606.ENSP00000403005.

Structurei

3D structure databases

ProteinModelPortaliP52798.
SMRiP52798. Positions 24-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 155130Ephrin RBDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ephrin family.PROSITE-ProRule annotation
Contains 1 ephrin RBD (ephrin receptor-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG266803.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52798.
KOiK05462.
OMAiCCKESKS.
OrthoDBiEOG70W3FD.
PhylomeDBiP52798.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52798-1) [UniParc]FASTAAdd to Basket

Also known as: GPI-anchored

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLLPLLRTV LWAAFLGSPL RGGSSLRHVV YWNSSNPRLL RGDAVVELGL
60 70 80 90 100
NDYLDIVCPH YEGPGPPEGP ETFALYMVDW PGYESCQAEG PRAYKRWVCS
110 120 130 140 150
LPFGHVQFSE KIQRFTPFSL GFEFLPGETY YYISVPTPES SGQCLRLQVS
160 170 180 190 200
VCCKERKSES AHPVGSPGES GTSGWRGGDT PSPLCLLLLL LLLILRLLRI

L
Length:201
Mass (Da):22,386
Last modified:October 1, 1996 - v1
Checksum:iABE8D5443A9AF28D
GO
Isoform 2 (identifier: P52798-2) [UniParc]FASTAAdd to Basket

Also known as: Secreted

The sequence of this isoform differs from the canonical sequence as follows:
     157-201: KSESAHPVGS...LLILRLLRIL → NLPSHPKEPE...VPIQTDKMEH

Show »
Length:193
Mass (Da):21,699
Checksum:iD0817324CC728EF5
GO
Isoform 3 (identifier: P52798-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     157-201: KSESAHPVGS...LLILRLLRIL → RARVLPRSPG...LAGACPLITG

Note: Gene prediction based on EST data.

Show »
Length:207
Mass (Da):22,584
Checksum:i67767F6020B4530B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei157 – 20145KSESA…LLRIL → NLPSHPKEPESSQDPLEEEG SLLPALGVPIQTDKMEH in isoform 2. 1 PublicationVSP_001448Add
BLAST
Alternative sequencei157 – 20145KSESA…LLRIL → RARVLPRSPGGGGIPAACTG GANSDRQDGALMGEIRGSEV TLAGACPLITG in isoform 3. CuratedVSP_046707Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14188 mRNA. Translation: AAC50079.1.
AJ006352 mRNA. Translation: CAA06992.1.
AJ006353 mRNA. Translation: CAA06993.1.
CR533569 mRNA. Translation: CAG38600.1.
AL691442 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW53138.1.
CH471121 Genomic DNA. Translation: EAW53139.1.
BC107483 mRNA. Translation: AAI07484.1.
CCDSiCCDS1089.1. [P52798-1]
CCDS41407.1. [P52798-2]
CCDS44237.1. [P52798-3]
PIRiI38850.
RefSeqiNP_005218.1. NM_005227.2. [P52798-1]
NP_872631.1. NM_182689.1. [P52798-3]
NP_872632.2. NM_182690.2. [P52798-2]
UniGeneiHs.449913.
Hs.639422.

Genome annotation databases

EnsembliENST00000359751; ENSP00000352789; ENSG00000243364. [P52798-2]
ENST00000368409; ENSP00000357394; ENSG00000243364. [P52798-1]
ENST00000427683; ENSP00000414378; ENSG00000243364. [P52798-3]
GeneIDi1945.
KEGGihsa:1945.
UCSCiuc001fhc.3. human.
uc001fhd.3. human. [P52798-1]
uc001fhe.3. human. [P52798-2]

Polymorphism databases

DMDMi1706672.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14188 mRNA. Translation: AAC50079.1.
AJ006352 mRNA. Translation: CAA06992.1.
AJ006353 mRNA. Translation: CAA06993.1.
CR533569 mRNA. Translation: CAG38600.1.
AL691442 Genomic DNA. No translation available.
CH471121 Genomic DNA. Translation: EAW53138.1.
CH471121 Genomic DNA. Translation: EAW53139.1.
BC107483 mRNA. Translation: AAI07484.1.
CCDSiCCDS1089.1. [P52798-1]
CCDS41407.1. [P52798-2]
CCDS44237.1. [P52798-3]
PIRiI38850.
RefSeqiNP_005218.1. NM_005227.2. [P52798-1]
NP_872631.1. NM_182689.1. [P52798-3]
NP_872632.2. NM_182690.2. [P52798-2]
UniGeneiHs.449913.
Hs.639422.

3D structure databases

ProteinModelPortaliP52798.
SMRiP52798. Positions 24-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108265. 1 interaction.
DIPiDIP-48295N.
IntActiP52798. 1 interaction.
STRINGi9606.ENSP00000403005.

PTM databases

PhosphoSiteiP52798.

Polymorphism databases

DMDMi1706672.

Proteomic databases

PaxDbiP52798.
PRIDEiP52798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359751; ENSP00000352789; ENSG00000243364. [P52798-2]
ENST00000368409; ENSP00000357394; ENSG00000243364. [P52798-1]
ENST00000427683; ENSP00000414378; ENSG00000243364. [P52798-3]
GeneIDi1945.
KEGGihsa:1945.
UCSCiuc001fhc.3. human.
uc001fhd.3. human. [P52798-1]
uc001fhe.3. human. [P52798-2]

Organism-specific databases

CTDi1945.
GeneCardsiGC01P155036.
HGNCiHGNC:3224. EFNA4.
HPAiCAB021350.
MIMi601380. gene.
neXtProtiNX_P52798.
PharmGKBiPA27659.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266803.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52798.
KOiK05462.
OMAiCCKESKS.
OrthoDBiEOG70W3FD.
PhylomeDBiP52798.

Enzyme and pathway databases

ReactomeiREACT_228063. EPHA-mediated growth cone collapse.
REACT_228170. EPH-Ephrin signaling.
REACT_228189. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52798.

Miscellaneous databases

GeneWikiiEFNA4.
GenomeRNAii1945.
NextBioi7879.
PROiP52798.
SOURCEiSearch...

Gene expression databases

BgeeiP52798.
CleanExiHS_EFNA4.
GenevestigatoriP52798.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERiPTHR11304. PTHR11304. 1 hit.
PfamiPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSiPR01347. EPHRIN.
ProDomiPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins."
    Kozlosky C.J., Maraskovsky E., McGrew J.T., Vanden Bos T., Teepe M., Lyman S.D., Srinivasan S., Fletcher F.A., Gayle R.B. III, Cerretti D.P., Beckmann M.P.
    Oncogene 10:299-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A splice variant of human ephrin-A4 encodes a soluble molecule that is secreted by activated human B lymphocytes."
    Aasheim H.-C., Munthe E., Funderud S., Smeland E.B., Beiske K., Logtenberg T.
    Blood 95:221-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: B-cell.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-40.

Entry informationi

Entry nameiEFNA4_HUMAN
AccessioniPrimary (citable) accession number: P52798
Secondary accession number(s): C9JHJ8
, G3XAK2, O95457, Q5SR71, Q6FI57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.