Q61772 (EPHA7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ephrin type-A receptor 7
EC=2.7.10.1

Alternative name(s):
Developmental kinase 1
Short name=mDK-1
EPH homology kinase 3
Short name=EHK-3
Embryonic brain kinase
Short name=EBK

Gene names

Name:	Epha7
Synonyms:	Ebk, Ehk3, Mdk1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	998 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 tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands 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. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties. Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses By similarity. Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain). Ref.7
Subcellular location	Cell membrane Probable; Single-pass type I membrane protein Probable Ref.8.
Tissue specificity	Widely expressed in embryo. In adult, expression restricted to hippocampus, testis and spleen.
Developmental stage	During visual system development, expressed in an anterior to posterior decreasing gradient stretching through the entire midbrain. This gradient has the reverse orientation to the one defined by the expression of ephrins. Isoform 4 and isoform 5 are expressed at the edges of the embryonic cranial neural fold. Ref.8 Ref.10
Post-translational modification	Phosphorylated. Isoform 4 inhibits isoform 1 phosphorylation and may regulate its function in adhesion. Ref.8
Disruption phenotype	Mice are viable, fertile and show no gross morphological or behavioral defects. However, topographic targeting errors of nasal and temporal retinal axons appear during development of the retinocollicular projections in the visual system. 10 percent of the embryos also display exencephalic overgrowth of forebrain tissues which might be the result of reduced apoptosis. Ref.9 Ref.10
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 1 Eph LBD (Eph ligand-binding) domain. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Apoptosis Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from mutant phenotype Ref.9. Source: UniProtKB branching morphogenesis of a nerve Inferred from mutant phenotype Ref.10. Source: MGI positive regulation of neuron apoptotic process Inferred from mutant phenotype Ref.9. Source: MGI regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell-cell adhesion Inferred from direct assay Ref.8. Source: UniProtKB regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay Ref.9. Source: UniProtKB regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.8. Source: UniProtKB regulation of protein autophosphorylation Inferred from direct assay Ref.8. Source: UniProtKB retinal ganglion cell axon guidance Inferred from mutant phenotype Ref.10. Source: MGI
Cellular_component	dendrite Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred by curator Ref.8. Source: UniProtKB neuromuscular junction Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GPI-linked ephrin receptor activity Inferred from direct assay Ref.8. Source: UniProtKB axon guidance receptor activity Inferred from mutant phenotype Ref.11. Source: UniProtKB chemorepellent activity Inferred from direct assay Ref.10. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61772-1)

Also known as: MDK1; EPHA7-FL;

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 2 (identifier: Q61772-2)

Also known as: MDK1-1; Ebk-td1;

The sequence of this isoform differs from the canonical sequence as follows:
     540-544: Missing.

Isoform 3 (identifier: Q61772-3)

Also known as: MDK1-2;

The sequence of this isoform differs from the canonical sequence as follows:
     601-604: Missing.

Isoform 4 (identifier: Q61772-4)

Also known as: MDK1-T1; EPHA7-T1;

The sequence of this isoform differs from the canonical sequence as follows:
     600-610: FKFPGTKTYID → SLVTNEHLSVL
     611-998: Missing.

Note: Truncated receptor lacking the kinase domain.

Isoform 5 (identifier: Q61772-5)

Also known as: MDK1-T2; EPHA7-T2;

The sequence of this isoform differs from the canonical sequence as follows:
     600-626: FKFPGTKTYIDPETYEDPNRAVHQFAK → SLYRERGDGMEKTQHNKKWMIASCSRL
     627-998: Missing.

Note: Truncated receptor lacking the kinase domain.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 998	971	Ephrin type-A receptor 7		PRO_0000016819
Regions
	Topological domain	28 – 555	528	Extracellular Potential
	Transmembrane	556 – 576	21	Helical; Potential
	Topological domain	577 – 998	422	Cytoplasmic Potential
	Domain	32 – 210	179	Eph LBD
	Domain	331 – 433	103	Fibronectin type-III 1
	Domain	443 – 535	93	Fibronectin type-III 2
	Domain	633 – 894	262	Protein kinase
	Domain	923 – 987	65	SAM
	Nucleotide binding	639 – 647	9	ATP By similarity
	Motif	996 – 998	3	PDZ-binding Potential
	Compositional bias	192 – 328	137	Cys-rich
Sites
	Active site	758	1	Proton acceptor By similarity
	Binding site	665	1	ATP By similarity
Amino acid modifications
	Modified residue	608	1	Phosphotyrosine; by autocatalysis Potential
	Modified residue	614	1	Phosphotyrosine; by autocatalysis Potential
	Modified residue	791	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	940	1	Phosphotyrosine; by autocatalysis Potential
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Glycosylation	410	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	540 – 544	5	Missing in isoform 2.		VSP_003006
	Alternative sequence	600 – 626	27	FKFPG…HQFAK → SLYRERGDGMEKTQHNKKWM IASCSRL in isoform 5.		VSP_003010
	Alternative sequence	600 – 610	11	FKFPGTKTYID → SLVTNEHLSVL in isoform 4.		VSP_003008
	Alternative sequence	601 – 604	4	Missing in isoform 3.		VSP_003007
	Alternative sequence	611 – 998	388	Missing in isoform 4.		VSP_003009
	Alternative sequence	627 – 998	372	Missing in isoform 5.		VSP_003011
Experimental info
	Sequence conflict	207	1	S → T in CAA55687. Ref.1
	Sequence conflict	207	1	S → T in CAA55688. Ref.1
	Sequence conflict	207	1	S → T in CAA55689. Ref.1
	Sequence conflict	480	1	Y → H in CAA57224. Ref.6
	Sequence conflict	657	1	K → Q in CAA55687. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MDK1) (EPHA7-FL) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: FCA1E83490E746E1	FASTA	998	111,860
	10 20 30 40 50 60 MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 70 80 90 100 110 120 LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 130 140 150 160 170 180 ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 190 200 210 220 230 240 GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 250 260 270 280 290 300 EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 310 320 330 340 350 360 FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 370 380 390 400 410 420 NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 430 440 450 460 470 480 VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 490 500 510 520 530 540 YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 550 560 570 580 590 600 KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 610 620 630 640 650 660 KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV 670 680 690 700 710 720 AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD 730 740 750 760 770 780 AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS 790 800 810 820 830 840 RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM 850 860 870 880 890 900 SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKDRAER PKFEQIVGIL DKMIRNPSSL 910 920 930 940 950 960 KTPLGTCSRP LSPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI 970 980 990 DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV
	Isoform 2 (MDK1-1) (Ebk-td1) [UniParc]. Checksum: 2D1C811BCD1FA937	FASTA	993	111,268
	10 20 30 40 50 60 MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 70 80 90 100 110 120 LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 130 140 150 160 170 180 ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 190 200 210 220 230 240 GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 250 260 270 280 290 300 EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 310 320 330 340 350 360 FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 370 380 390 400 410 420 NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 430 440 450 460 470 480 VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 490 500 510 520 530 540 YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASA 550 560 570 580 590 600 TAVSSEQNPV IIIAVVAVAG TIILVFMVFG FIIGRRHCGY SKADQEGDEE LYFHFKFPGT 610 620 630 640 650 660 KTYIDPETYE DPNRAVHQFA KELDASCIKI ERVIGAGEFG EVCSGRLKLP GKRDVAVAIK 670 680 690 700 710 720 TLKVGYTEKQ RRDFLCEASI MGQFDHPNVV HLEGVVTRGK PVMIVIEFME NGALDAFLRK 730 740 750 760 770 780 HDGQFTVIQL VGMLRGIAAG MRYLADMGYV HRDLAARNIL VNSNLVCKVS DFGLSRVIED 790 800 810 820 830 840 DPEAVYTTTG GKIPVRWTAP EAIQYRKFTS ASDVWSYGIV MWEVMSYGER PYWDMSNQDV 850 860 870 880 890 900 IKAIEEGYRL PAPMDCPAGL HQLMLDCWQK DRAERPKFEQ IVGILDKMIR NPSSLKTPLG 910 920 930 940 950 960 TCSRPLSPLL DQSTPDFTAF CSVGEWLQAI KMERYKDNFT AAGYNSLESV ARMTIDDVMS 970 980 990 LGITLVGHQK KIMSSIQTMR AQMLHLHGTG IQV
	Isoform 3 (MDK1-2) [UniParc]. Checksum: 25ADED280A8D9FBF	FASTA	994	111,431
	10 20 30 40 50 60 MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 70 80 90 100 110 120 LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 130 140 150 160 170 180 ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 190 200 210 220 230 240 GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 250 260 270 280 290 300 EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 310 320 330 340 350 360 FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 370 380 390 400 410 420 NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 430 440 450 460 470 480 VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 490 500 510 520 530 540 YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 550 560 570 580 590 600 KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 610 620 630 640 650 660 TKTYIDPETY EDPNRAVHQF AKELDASCIK IERVIGAGEF GEVCSGRLKL PGKRDVAVAI 670 680 690 700 710 720 KTLKVGYTEK QRRDFLCEAS IMGQFDHPNV VHLEGVVTRG KPVMIVIEFM ENGALDAFLR 730 740 750 760 770 780 KHDGQFTVIQ LVGMLRGIAA GMRYLADMGY VHRDLAARNI LVNSNLVCKV SDFGLSRVIE 790 800 810 820 830 840 DDPEAVYTTT GGKIPVRWTA PEAIQYRKFT SASDVWSYGI VMWEVMSYGE RPYWDMSNQD 850 860 870 880 890 900 VIKAIEEGYR LPAPMDCPAG LHQLMLDCWQ KDRAERPKFE QIVGILDKMI RNPSSLKTPL 910 920 930 940 950 960 GTCSRPLSPL LDQSTPDFTA FCSVGEWLQA IKMERYKDNF TAAGYNSLES VARMTIDDVM 970 980 990 SLGITLVGHQ KKIMSSIQTM RAQMLHLHGT GIQV
	Isoform 4 (MDK1-T1) (EPHA7-T1) [UniParc]. Checksum: E61310A72FE1E739	FASTA	610	68,286
	10 20 30 40 50 60 MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 70 80 90 100 110 120 LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 130 140 150 160 170 180 ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 190 200 210 220 230 240 GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 250 260 270 280 290 300 EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 310 320 330 340 350 360 FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 370 380 390 400 410 420 NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 430 440 450 460 470 480 VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 490 500 510 520 530 540 YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 550 560 570 580 590 600 KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHS 610 LVTNEHLSVL
	Isoform 5 (MDK1-T2) (EPHA7-T2) [UniParc]. Checksum: F929755DC75B5664	FASTA	626	70,300
	10 20 30 40 50 60 MVVQTRFPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 70 80 90 100 110 120 LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 130 140 150 160 170 180 ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 190 200 210 220 230 240 GFYLAFQDVG ACIALVSVKV YYKKCWSIVE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 250 260 270 280 290 300 EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 310 320 330 340 350 360 FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 370 380 390 400 410 420 NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 430 440 450 460 470 480 VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVQ LSWQEPEHPN GVITEYEIKY 490 500 510 520 530 540 YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAVTA AGYGNYSPRL DVATLEEASG 550 560 570 580 590 600 KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHS 610 620 LYRERGDGME KTQHNKKWMI ASCSRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of alternatively spliced mRNAs encoding variants of MDK1, a novel receptor tyrosine kinase expressed in the murine nervous system." Ciossek T., Millauer B., Ullrich A. Oncogene 10:97-108(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Strain: BALB/c. Tissue: Brain.
[2]	"A novel truncated variant form of Ebk/MDK1 receptor tyrosine kinase is expressed in embryonic mouse brain." Talukder A.H., Muramatsu T., Kaneda N. Cell Struct. Funct. 22:477-485(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Pituitary.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Embryo brain kinase: a novel gene of the eph/elk receptor tyrosine kinase family." Ellis J., Liu Q., Breitman M., Jenkins N.A., Gilbert D.J., Copeland N.G., Tempest H.V., Warren S., Muir E., Schilling H., Fletcher F.A., Ziegler S.F., Rogers J.H. Mech. Dev. 52:319-341(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 431-998 (ISOFORM 1). Tissue: Brain.
[7]	"PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands." Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D. Neuron 21:1453-1463(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIP1 AND PICK1, IDENTIFICATION OF PDZ-BINDING MOTIF.
[8]	"Regulation of repulsion versus adhesion by different splice forms of an Eph receptor." Holmberg J., Clarke D.L., Frisen J. Nature 408:203-206(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL ADHESION AND REPULSION (ISOFORMS 1 AND 4), EFNA5 LIGAND-BINDING, PHOSPHORYLATION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[9]	"Ephrin signalling controls brain size by regulating apoptosis of neural progenitors." Depaepe V., Suarez-Gonzalez N., Dufour A., Passante L., Gorski J.A., Jones K.R., Ledent C., Vanderhaeghen P. Nature 435:1244-1250(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS.
[10]	"Opposing gradients of ephrin-As and EphA7 in the superior colliculus are essential for topographic mapping in the mammalian visual system." Rashid T., Upton A.L., Blentic A., Ciossek T., Knoell B., Thompson I.D., Drescher U. Neuron 47:57-69(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN TOPOGRAPHIC MAPPING, DEVELOPMENTAL STAGE.
[11]	"Dissociation of corticothalamic and thalamocortical axon targeting by an EphA7-mediated mechanism." Torii M., Levitt P. Neuron 48:563-575(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CORTICOTHALAMIC AXON GUIDANCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79082 mRNA. Translation: CAA55687.1. X79083 mRNA. Translation: CAA55688.1. X79084 mRNA. Translation: CAA55689.1. AK030480 mRNA. Translation: BAC26982.1. BX000989 Genomic DNA. Translation: CAM21483.1. CH466538 Genomic DNA. Translation: EDL05518.1. X81466 mRNA. Translation: CAA57224.1.
IPI	IPI00124993. IPI00343893. IPI00380199. IPI00380200. IPI01023292.
PIR	I48612. I48614. JC5672.
RefSeq	NP_034271.3. NM_010141.3.
UniGene	Mm.257266.
3D structure databases
ProteinModelPortal	Q61772.
SMR	Q61772. Positions 30-899, 919-989.
ModBase	Search...
PTM databases
PhosphoSite	Q61772.
Proteomic databases
PaxDb	Q61772.
PRIDE	Q61772.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029964; ENSMUSP00000029964; ENSMUSG00000028289. ENSMUST00000080934; ENSMUSP00000079735; ENSMUSG00000028289. ENSMUST00000108194; ENSMUSP00000103829; ENSMUSG00000028289.
GeneID	13841.
KEGG	mmu:13841.
Organism-specific databases
CTD	2045.
MGI	MGI:95276. Epha7.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00670000097666.
HOGENOM	HOG000233856.
HOVERGEN	HBG062180.
InParanoid	Q8BSU8.
KO	K05108.
OMA	LEDNYVT.
OrthoDB	EOG4H19TZ.
Enzyme and pathway databases
BRENDA	2.7.10.1. 3474.
Gene expression databases
ArrayExpress	Q61772.
Bgee	Q61772.
CleanEx	MM_EPHA7.
Genevestigator	Q61772.
GermOnline	ENSMUSG00000028289. Mus musculus.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 2.60.40.10. 2 hits.
InterPro	IPR001090. Ephrin_rcpt_lig-bd_dom. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR009030. Growth_fac_rcpt. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR021129. SAM_type1. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016257. Tyr_kinase_ephrin_rcpt. IPR001426. Tyr_kinase_rcpt_V_CS. [Graphical view]
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.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF57184. Grow_fac_recept. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS01186. EGF_2. 1 hit. Uncertain. PS51550. EPH_LBD. 1 hit. 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
ChiTaRS	EPHA7. mouse.
NextBio	284676.
SOURCE	Search...

Entry information

Entry name

EPHA7_MOUSE

Accession

Primary (citable) accession number: Q61772
Secondary accession number(s): Q61505 , Q61773, Q61774, Q8BSU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program