Reviewed, UniProtKB/Swiss-Prot Q60750 (EPHA1_MOUSE)

Names and origin

Protein names

Recommended name:
    Ephrin type-A receptor 1
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor ESK

Gene names

Name:	Epha1
Synonyms:	Esk

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	977 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	Receptor for members of the ephrin-A family. Binds with a low affinity to ephrin-A1.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 977

953

Ephrin type-A receptor 1 By similarity

PRO_0000016799

Regions

Topological domain

25 – 548

524

Extracellular Potential

Transmembrane

549 – 569

21

Potential

Topological domain

570 – 977

408

Cytoplasmic Potential

Domain

333 – 438

106

Fibronectin type-III 1

Domain

447 – 536

90

Fibronectin type-III 2

Domain

625 – 885

261

Protein kinase

Domain

914 – 977

64

SAM

Nucleotide binding

631 – 639

9

ATP By similarity

Motif

975 – 977

3

PDZ-binding Potential

Compositional bias

192 – 330

139

Cys-rich

Sites

Active site

750

1

Proton acceptor By similarity

Binding site

657

1

ATP By similarity

Amino acid modifications

Modified residue

34

1

Phosphothreonine By similarity

Modified residue

35

1

Phosphoserine By similarity

Modified residue

600

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

606

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

782

1

Phosphotyrosine; by autocatalysis Potential

Modified residue

911

1

Phosphoserine Ref.4

Glycosylation

339

1

N-linked (GlcNAc...) Potential

Glycosylation

415

1

N-linked (GlcNAc...) Potential

Glycosylation

479

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

163

1

G → D in AAG12206. Ref.1

Sequence conflict

422

1

S → P in AAC52384. Ref.3

Sequence conflict

504

1

L → R in AAC52384. Ref.3

Sequence conflict

521

1

T → A in AAC52384. Ref.3

Sequence conflict

590

1

D → G in AAC52384. Ref.3

Sequence conflict

636

1

F → Y in AAC52384. Ref.3

Sequence conflict

660

1

K → R in AAC52384. Ref.3

Sequence conflict

720

1

D → G in AAC52384. Ref.3

Sequence conflict

769

1

F → L in AAC52384. Ref.3

Sequence conflict

797

1

E → G in AAC52384. Ref.3

Sequence conflict

817

1

M → T in AAG12206. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

977

Helix Strand Turn

Details...

Beta strand

456 – 460

5

Beta strand

463 – 467

5

Beta strand

481 – 487

7

Beta strand

492 – 506

15

Beta strand

512 – 520

9

Beta strand

522 – 524

3

Beta strand

532 – 535

4

Sequences

	Sequence		Length	Mass (Da)
	Q60750-1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: AB78D6E6C8B2E7F4	FASTA	977	108,578
	10 20 30 40 50 60 MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET GWSEVQQMLN 70 80 90 100 110 120 GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL QFTVRDCKSF PGGAGPLGCK 130 140 150 160 170 180 ETFNLFYMES DQDVGIQLRR PLFQKVTTVA ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR 190 200 210 220 230 240 GLYLAFHNPG SCVALVSVRV FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL 250 260 270 280 290 300 GSSGTPRMHC SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ 310 320 330 340 350 360 HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS LRWEPPRDTG 370 380 390 400 410 420 GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL TTSTVQVQGL EPYANYTFTV 430 440 450 460 470 480 KSQNRVSGLD SSSPSSASLS INMGHAESLS GLSLKLVKKE PRQLELTWAG SRPRNPGGNL 490 500 510 520 530 540 SYELHVLNQD EEWHQMVLEP RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV 550 560 570 580 590 600 SRSLTGGEIV AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY 610 620 630 640 650 660 VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD CKTVAIKTLK 670 680 690 700 710 720 DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM IITEFMENGA LDAFLKERED 730 740 750 760 770 780 QLAPGQLVAM LLGIASGMNC LSGHNYVHRD LAARNILVNQ NLCCKVSDFG LTRLLDDFDG 790 800 810 820 830 840 TYETQGGKIP IRWTAPEAIA HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI 850 860 870 880 890 900 EDGYRLPPPV DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR 910 920 930 940 950 960 VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT AEDLTQMGIT 970 LPGHQKRILC SIQGFKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse EphA1 cDNA -- full coding sequence." Lickliter J.D., Boyd A.W. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Skin.
[3]	"Embryonic stem cells express multiple Eph-subfamily receptor tyrosine kinases." Lickliter J.D., Smith F.M., Olsson J.E., Mackwell K.L., Boyd A.W. Proc. Natl. Acad. Sci. U.S.A. 93:145-150(1996) [PubMed: 8552593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-814. Strain: 129/Sv.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-782, MASS SPECTROMETRY.
[6]	"The solution structure of the second fibronectin type III domain of mouse ephrin type-A receptor 1." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 446-539.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF131197 mRNA. Translation: AAG12206.1.
AK028478 mRNA. Translation: BAC25971.1.
U18084 mRNA. Translation: AAC52384.1.

IPI

IPI00120222.

RefSeq

NP_076069.2.

UniGene

Mm.133330

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X5A	NMR	-	A	446-539	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q60750.

PTM databases

PhosphoSite

Q60750.

Proteomic databases

PRIDE

Q60750.

Genome annotation databases

Ensembl

ENSMUST00000073387; ENSMUSP00000073099; ENSMUSG00000029859; Mus musculus. [Genome view]

GeneID

13835.

KEGG

mmu:13835.

UCSC

uc009brc.1. mouse.

Organism-specific databases

CTD

13835.

MGI

MGI:107381. Epha1.

Phylogenomic databases

HOGENOM

Q60750.

HOVERGEN

Q60750.

OMA

AYEDPAQ.

Enzyme and pathway databases

BRENDA

2.7.10.1. 244.

Gene expression databases

ArrayExpress

Q60750.

Bgee

Q60750.

CleanEx

MM_EPHA1.

Genevestigator

Q60750.

GermOnline

ENSMUSG00000029859. Mus musculus.

Family and domain databases

InterPro

IPR013032. EGF-like_reg_CS.
IPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM_type.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016257. TyrPK_ephrin_receptor.
IPR001426. YKase_receptorV_CS.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.

Pfam

PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000666. TyrPK_ephrin_receptor. 1 hit.

PRINTS

PR00109. TYRKINASE.

ProDom

PD001495. Ephrin_receptor. 1 hit.
PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS01186. EGF_2. 1 hit. Uncertain.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

284652.

SOURCE

Search...

Entry information

Entry name

EPHA1_MOUSE

Accession

Primary (citable) accession number: Q60750
Secondary accession number(s): Q8CED9, Q9ESJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 10, 2004
Last modified:	November 3, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)