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Protein

Ephrin-A3

Gene

EFNA3

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. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity).By similarity

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • transmembrane-ephrin receptor activity Source: ProtInc

GO - Biological processi

  • axon guidance Source: GO_Central
  • cell-cell signaling Source: ProtInc
  • ephrin receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264548. EPHA-mediated growth cone collapse.
SignaLinkiP52797.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-A3
Alternative name(s):
EFL-2
EHK1 ligand
Short name:
EHK1-L
EPH-related receptor tyrosine kinase ligand 3
Short name:
LERK-3
Gene namesi
Name:EFNA3
Synonyms:EFL2, EPLG3, LERK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3223. EFNA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27658.

Polymorphism and mutation databases

BioMutaiEFNA3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 214192Ephrin-A3PRO_0000008369Add
BLAST
Propeptidei215 – 23824Removed in mature formSequence AnalysisPRO_0000008370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi63 ↔ 110PROSITE-ProRule annotation
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi99 ↔ 158PROSITE-ProRule annotation
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
Lipidationi214 – 2141GPI-anchor amidated glycineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiP52797.

Expressioni

Tissue specificityi

Expressed in brain, skeletal muscle, spleen, thymus, prostate, testis, ovary, small intestine, and peripheral blood leukocytes.

Gene expression databases

BgeeiP52797.
CleanExiHS_EFNA3.
GenevisibleiP52797. HS.

Organism-specific databases

HPAiCAB010494.

Interactioni

Subunit structurei

Interacts with EPHA8; activates EPHA8.

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-722730,EBI-10172134
NOTCH2NLQ7Z3S93EBI-722730,EBI-945833

Protein-protein interaction databases

BioGridi108264. 6 interactions.
IntActiP52797. 3 interactions.
MINTiMINT-1378559.
STRINGi9606.ENSP00000357393.

Structurei

3D structure databases

ProteinModelPortaliP52797.
SMRiP52797. Positions 31-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 169140Ephrin 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

eggNOGiNOG295575.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52797.
KOiK05462.
OMAiGPHVKIN.
OrthoDBiEOG70W3FD.
PhylomeDBiP52797.

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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P52797-1) [UniParc]FASTAAdd to basket

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
MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT
60 70 80 90 100
VQVNVNDYLD IYCPHYNSSG VGPGAGPGPG GGAEQYVLYM VSRNGYRTCN
110 120 130 140 150
ASQGFKRWEC NRPHAPHSPI KFSEKFQRYS AFSLGYEFHA GHEYYYISTP
160 170 180 190 200
THNLHWKCLR MKVFVCCAST SHSGEKPVPT LPQFTMGPNV KINVLEDFEG
210 220 230
ENPQVPKLEK SISGTSPKRE HLPLAVGIAF FLMTFLAS
Length:238
Mass (Da):26,350
Last modified:October 1, 1996 - v1
Checksum:i8EFD6AE8FE33FDDA
GO
Isoform 2 (identifier: P52797-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-196: TSHSGEKPVPTLPQFTMGPNVKINVLE → K

Note: No experimental confirmation available.
Show »
Length:212
Mass (Da):23,575
Checksum:i275AA7F0383A5074
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 744Missing in AAA52368 (PubMed:7973638).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901V → M.
Corresponds to variant rs17723260 [ dbSNP | Ensembl ].
VAR_048937

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 19627TSHSG…INVLE → K in isoform 2. 1 PublicationVSP_055483Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14187 mRNA. Translation: AAC50078.1.
L37360 mRNA. Translation: AAA52368.1.
AK316248 mRNA. Translation: BAH14619.1.
AL691442 Genomic DNA. Translation: CAI15318.1.
CH471121 Genomic DNA. Translation: EAW53137.1.
BC017722 mRNA. Translation: AAH17722.1.
BC110406 mRNA. Translation: AAI10407.1.
CCDSiCCDS1090.1. [P52797-1]
PIRiI38849.
RefSeqiNP_004943.1. NM_004952.4. [P52797-1]
UniGeneiHs.516656.

Genome annotation databases

EnsembliENST00000368408; ENSP00000357393; ENSG00000143590.
GeneIDi1944.
KEGGihsa:1944.
UCSCiuc001fhf.3. human. [P52797-1]
uc010pex.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14187 mRNA. Translation: AAC50078.1.
L37360 mRNA. Translation: AAA52368.1.
AK316248 mRNA. Translation: BAH14619.1.
AL691442 Genomic DNA. Translation: CAI15318.1.
CH471121 Genomic DNA. Translation: EAW53137.1.
BC017722 mRNA. Translation: AAH17722.1.
BC110406 mRNA. Translation: AAI10407.1.
CCDSiCCDS1090.1. [P52797-1]
PIRiI38849.
RefSeqiNP_004943.1. NM_004952.4. [P52797-1]
UniGeneiHs.516656.

3D structure databases

ProteinModelPortaliP52797.
SMRiP52797. Positions 31-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108264. 6 interactions.
IntActiP52797. 3 interactions.
MINTiMINT-1378559.
STRINGi9606.ENSP00000357393.

Polymorphism and mutation databases

BioMutaiEFNA3.

Proteomic databases

PRIDEiP52797.

Protocols and materials databases

DNASUi1944.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368408; ENSP00000357393; ENSG00000143590.
GeneIDi1944.
KEGGihsa:1944.
UCSCiuc001fhf.3. human. [P52797-1]
uc010pex.2. human.

Organism-specific databases

CTDi1944.
GeneCardsiGC01P155051.
HGNCiHGNC:3223. EFNA3.
HPAiCAB010494.
MIMi601381. gene.
neXtProtiNX_P52797.
PharmGKBiPA27658.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG295575.
GeneTreeiENSGT00390000015107.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52797.
KOiK05462.
OMAiGPHVKIN.
OrthoDBiEOG70W3FD.
PhylomeDBiP52797.

Enzyme and pathway databases

ReactomeiREACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264548. EPHA-mediated growth cone collapse.
SignaLinkiP52797.

Miscellaneous databases

GeneWikiiEFNA3.
GenomeRNAii1944.
NextBioi35480881.
PROiP52797.
SOURCEiSearch...

Gene expression databases

BgeeiP52797.
CleanExiHS_EFNA3.
GenevisibleiP52797. HS.

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. "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity."
    Davis S., Gale N.W., Aldrich T.H., Maisonpierre P.C., Lhotak V., Pawson T., Goldfarb M., Yancopoulos G.D.
    Science 266:816-819(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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).
    Tissue: Brain and Duodenum.

Entry informationi

Entry nameiEFNA3_HUMAN
AccessioniPrimary (citable) accession number: P52797
Secondary accession number(s): B7ZAD3
, D3DV85, Q0VGC9, Q5SR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.