Reviewed, UniProtKB/Swiss-Prot O08543 (EFNA5_MOUSE)

Names and origin

Protein names

Recommended name:
    Ephrin-A5
Alternative name(s):
    EPH-related receptor tyrosine kinase ligand 7
      Short name=LERK-7
    AL-1

Gene names

Name:	Efna5
Synonyms:	Epl7, Eplg7, Lerk7

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May function actively to stimulate axon fasciculation. 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 By similarity.
Subunit structure	Binds to the receptor tyrosine kinases EPHA2, EPHA3 and EPHB1 By similarity. Binds to EPHB2.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Note= Compartmentalized in discrete caveolae-like membrane microdomains By similarity.
Sequence similarities	Belongs to the ephrin family.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Developmental protein
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	retinal ganglion cell axon guidance Inferred from direct assay. Source: MGI
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chemorepellent activity Inferred from direct assay. Source: MGI protein binding Ref.3 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ephb2	P54763	1	EBI-1038734,EBI-537711

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: O08543-1)

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.

Isoform Short (identifier: O08543-2)

The sequence of this isoform differs from the canonical sequence as follows:
     163-189: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 203

183

Ephrin-A5

PRO_0000008379

Propeptide

204 – 228

25

Removed in mature form Potential

PRO_0000008380

Amino acid modifications

Lipidation

203

1

GPI-anchor amidated asparagine Potential

Glycosylation

37

1

N-linked (GlcNAc...) Ref.3

Disulfide bond

62 ↔ 102

Ref.3

Disulfide bond

90 ↔ 151

Ref.3

Natural variations

Alternative sequence

163 – 189

27

Missing in isoform Short.

VSP_001449

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

228

Helix Strand Turn

Details...

Beta strand

30 – 35

6

Helix

41 – 44

4

Beta strand

49 – 52

4

Beta strand

57 – 61

5

Beta strand

67 – 69

3

Beta strand

71 – 73

3

Beta strand

77 – 82

6

Helix

84 – 89

6

Turn

93 – 95

3

Beta strand

96 – 102

7

Beta strand

108 – 111

4

Beta strand

113 – 117

5

Beta strand

135 – 144

10

Beta strand

148 – 150

3

Beta strand

153 – 158

6

Turn

161 – 163

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 85439F5337420022	FASTA	228	26,339
	10 20 30 40 50 60 MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV 70 80 90 100 110 120 FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL 130 140 150 160 170 180 FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK 190 200 210 220 VENSLEPADD TVHESAEPSR GENAAQTPRI PSRLLAILLF LLAMLLTL
	Isoform Short. Checksum: C5F5E78FD6674316		201	23,338
	10 20 30 40 50 60 MLHVEMLTLL FLVLWMCVFS QDPGSKVVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV 70 80 90 100 110 120 FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL 130 140 150 160 170 180 FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNDTVHESAE PSRGENAAQT 190 200 PRIPSRLLAI LLFLLAMLLT L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Distinct and overlapping expression patterns of ligands for Eph-related receptor tyrosine kinases during mouse embryogenesis." Flenniken A.M., Gale N.W., Yancopoulos G.D., Wilkinson D.G. Dev. Biol. 179:382-401(1996) [PubMed: 8903354] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Strain: FVB/N. Tissue: Mammary gland.
[3]	"Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling." Himanen J.P., Chumley M.J., Lackmann M., Li C., Barton W.A., Jeffrey P.D., Vearing C., Geleick D., Feldheim D.A., Boyd A.W., Henkemeyer M., Nikolov D.B. Nat. Neurosci. 7:501-509(2004) [PubMed: 15107857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 28-165 ALONE AND IN COMPLEX WITH EPHB2, GLYCOSYLATION AT ASN-37, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U90664 mRNA. Translation: AAB50239.1.
U90665 mRNA. Translation: AAB50240.1.
BC040218 mRNA. Translation: AAH40218.1.

RefSeq

NP_034239.1.
NP_997537.1.

UniGene

Mm.465261
Mm.7978

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SHW	X-ray	2.20	A	28-165	[»]
1SHX	X-ray	2.10	A/B	28-165	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O08543. 2 interactions.

Proteomic databases

PRIDE

O08543.

Genome annotation databases

Ensembl

ENSMUSG00000048915. Mus musculus. [Contig view]

GeneID

13640.

KEGG

mmu:13640.

Organism-specific databases

MGI

MGI:107444. Efna5.

Phylogenomic databases

HOGENOM

O08543.

HOVERGEN

O08543.

Gene expression databases

ArrayExpress

O08543.

CleanEx

MM_EFNA5.

GermOnline

ENSMUSG00000048915. Mus musculus.

Family and domain databases

InterPro

IPR008972. Cupredoxin.
IPR001799. Ephrin.
[Graphical view]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 1 hit.

PANTHER

PTHR11304. Ephrin. 1 hit.

Pfam

PF00812. Ephrin. 1 hit.
[Graphical view]

PRINTS

PR01347. EPHRIN.

ProDom

PD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01299. EPHRIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

284336.

SOURCE

Search...

Entry information

Entry name

EFNA5_MOUSE

Accession

Primary (citable) accession number: O08543
Secondary accession number(s): O08544

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	December 16, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)