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Protein

Ephrin-A5

Gene

EFNA5

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation (By similarity). Induces growth cone collapse and repulsion of retinal ganglion cell axons.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin-A5
Alternative name(s):
EPH-related receptor tyrosine kinase ligand 7
Short name:
LERK-7
Repulsive axon guidance signal protein
Gene namesi
Name:EFNA5
Synonyms:RAGS
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000000838321 – 203Ephrin-A5Add BLAST183
PropeptideiPRO_0000008384204 – 228Removed in mature formSequence analysisAdd BLAST25

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi37N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi62 ↔ 102PROSITE-ProRule annotation
Disulfide bondi90 ↔ 151PROSITE-ProRule annotation
Lipidationi203GPI-anchor amidated asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP52804.

Expressioni

Tissue specificityi

Expressed in a graded fashion across the tectum being more strongly expressed towards the posterior pole.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000000368.

Structurei

3D structure databases

ProteinModelPortaliP52804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 162Ephrin RBDPROSITE-ProRule annotationAdd BLAST134

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

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52804.
KOiK05462.
PhylomeDBiP52804.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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]

Sequencei

Sequence statusi: Complete.

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

P52804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHVEMLLLA VAALWVCVRG QEPGRKAVAD RYAVYWNSTN PRFQQGDYHI
60 70 80 90 100
DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSSC DHISKGFKRW
110 120 130 140 150
ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS
160 170 180 190 200
CLKLKVFVRP ANSCMKTIGV HDRVFDVNDK VENSLEPADD TVRESAEPSR
210 220
GENAAQTPRI PIRLLATLLF LLAMLLIL
Length:228
Mass (Da):26,206
Last modified:October 1, 1996 - v1
Checksum:i56D8E4FBDECF18AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90377 mRNA. Translation: CAA62027.1.
PIRiA57084.
RefSeqiNP_990515.1. NM_205184.2.
UniGeneiGga.19368.
Gga.651.

Genome annotation databases

GeneIDi396100.
KEGGigga:396100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90377 mRNA. Translation: CAA62027.1.
PIRiA57084.
RefSeqiNP_990515.1. NM_205184.2.
UniGeneiGga.19368.
Gga.651.

3D structure databases

ProteinModelPortaliP52804.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000000368.

Proteomic databases

PaxDbiP52804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396100.
KEGGigga:396100.

Organism-specific databases

CTDi1946.

Phylogenomic databases

eggNOGiKOG3858. Eukaryota.
ENOG4111FMJ. LUCA.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52804.
KOiK05462.
PhylomeDBiP52804.

Miscellaneous databases

PROiP52804.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR008972. Cupredoxin.
IPR031328. Ephrin.
IPR019765. Ephrin_CS.
IPR001799. Ephrin_RBD.
[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...

Entry informationi

Entry nameiEFNA5_CHICK
AccessioniPrimary (citable) accession number: P52804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 5, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.