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P52797

- EFNA3_HUMAN

UniProt

P52797 - EFNA3_HUMAN

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Protein

Ephrin-A3

Gene
EFNA3, EFL2, EPLG3, LERK3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

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

GO - Biological processi

  1. axon guidance Source: RefGenome
  2. cell-cell signaling Source: ProtInc
  3. ephrin receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

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: Chromosome 1

Organism-specific databases

HGNCiHGNC:3223. EFNA3.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed predictionAdd
BLAST
Chaini23 – 214192Ephrin-A3PRO_0000008369Add
BLAST
Propeptidei215 – 23824Removed in mature form Reviewed predictionPRO_0000008370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi63 ↔ 110 By similarity
Glycosylationi67 – 671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi99 ↔ 158 By similarity
Glycosylationi100 – 1001N-linked (GlcNAc...) Reviewed prediction
Lipidationi214 – 2141GPI-anchor amidated glycine Reviewed prediction

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

ArrayExpressiP52797.
BgeeiP52797.
CleanExiHS_EFNA3.
GenevestigatoriP52797.

Organism-specific databases

HPAiCAB010494.

Interactioni

Subunit structurei

Interacts with EPHA8; activates EPHA8.

Protein-protein interaction databases

BioGridi108264. 3 interactions.
IntActiP52797. 1 interaction.
MINTiMINT-1378559.
STRINGi9606.ENSP00000357393.

Structurei

3D structure databases

ProteinModelPortaliP52797.
SMRiP52797. Positions 31-165.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the ephrin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG295575.
HOGENOMiHOG000234373.
HOVERGENiHBG051447.
InParanoidiP52797.
KOiK05462.
OMAiCEQKSGP.
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. Align

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

MAAAPLLLLL LLVPVPLLPL LAQGPGGALG NRHAVYWNSS NQHLRREGYT    50
VQVNVNDYLD IYCPHYNSSG VGPGAGPGPG GGAEQYVLYM VSRNGYRTCN 100
ASQGFKRWEC NRPHAPHSPI KFSEKFQRYS AFSLGYEFHA GHEYYYISTP 150
THNLHWKCLR MKVFVCCAST SHSGEKPVPT LPQFTMGPNV KINVLEDFEG 200
ENPQVPKLEK SISGTSPKRE HLPLAVGIAF FLMTFLAS 238
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

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. VSP_055483Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 744Missing in AAA52368. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiI38849.
RefSeqiNP_004943.1. NM_004952.4.
UniGeneiHs.516656.

Genome annotation databases

EnsembliENST00000368408; ENSP00000357393; ENSG00000143590.
ENST00000418360; ENSP00000391370; ENSG00000143590.
GeneIDi1944.
KEGGihsa:1944.
UCSCiuc001fhf.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1090.1.
PIRi I38849.
RefSeqi NP_004943.1. NM_004952.4.
UniGenei Hs.516656.

3D structure databases

ProteinModelPortali P52797.
SMRi P52797. Positions 31-165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108264. 3 interactions.
IntActi P52797. 1 interaction.
MINTi MINT-1378559.
STRINGi 9606.ENSP00000357393.

Proteomic databases

PRIDEi P52797.

Protocols and materials databases

DNASUi 1944.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368408 ; ENSP00000357393 ; ENSG00000143590 .
ENST00000418360 ; ENSP00000391370 ; ENSG00000143590 .
GeneIDi 1944.
KEGGi hsa:1944.
UCSCi uc001fhf.3. human.

Organism-specific databases

CTDi 1944.
GeneCardsi GC01P155051.
HGNCi HGNC:3223. EFNA3.
HPAi CAB010494.
MIMi 601381. gene.
neXtProti NX_P52797.
PharmGKBi PA27658.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295575.
HOGENOMi HOG000234373.
HOVERGENi HBG051447.
InParanoidi P52797.
KOi K05462.
OMAi CEQKSGP.
OrthoDBi EOG70W3FD.
PhylomeDBi P52797.

Enzyme and pathway databases

SignaLinki P52797.

Miscellaneous databases

GeneWikii EFNA3.
GenomeRNAii 1944.
NextBioi 7875.
PROi P52797.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52797.
Bgeei P52797.
CleanExi HS_EFNA3.
Genevestigatori P52797.

Family and domain databases

Gene3Di 2.60.40.420. 1 hit.
InterProi IPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view ]
PANTHERi PTHR11304. PTHR11304. 1 hit.
Pfami PF00812. Ephrin. 1 hit.
[Graphical view ]
PRINTSi PR01347. EPHRIN.
ProDomi PD002533. Ephrin. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49503. SSF49503. 1 hit.
PROSITEi PS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 121 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

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