ID EPB1B_XENLA Reviewed; 902 AA.
AC Q91736;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 113.
DE RecName: Full=Ephrin type-B receptor 1-B;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase receptor XELK;
DE Flags: Fragment;
GN Name=ephb1-b; Synonyms=xelk;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7478602;
RA Scales J.B., Winning R.S., Renaud C.S., Shea L.J., Sargent T.D.;
RT "Novel members of the eph receptor tyrosine kinase subfamily expressed
RT during Xenopus development.";
RL Oncogene 11:1745-1752(1995).
RN [2]
RP FUNCTION IN TARGETED CELL MIGRATION.
RX PubMed=9259557; DOI=10.1016/S0960-9822(06)00255-7;
RA Smith A., Robinson V., Patel K., Wilkinson D.G.;
RT "The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand
RT regulate targeted migration of branchial neural crest cells.";
RL Curr. Biol. 7:561-570(1997).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC transmembrane ephrin-B family ligands residing on adjacent cells,
CC leading to contact-dependent bidirectional signaling into
CC neighboring cells. The signaling pathway downstream of the
CC receptor is referred to as forward signaling while the signaling
CC pathway downstream of the ephrin ligand is referred to as reverse
CC signaling. May play a role in axon guidance during nervous system
CC development. May also play an important redundant role with other
CC ephrin-B receptors in development and maturation of dendritic
CC spines and synapse formation. More generally, may play a role in
CC targeted cell migration and adhesion. Upon activation by ephrin-B
CC ligands activates the MAPK/ERK and the JNK signaling cascades to
CC regulate cell migration and adhesion respectively (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The
CC heterotetramer is composed of an ephrin dimer and a receptor
CC dimer. Oligomerization is probably required to induce biological
CC responses (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane (By similarity); Single-pass
CC type I membrane protein. Early endosome membrane; Single-pass type
CC I membrane protein (By similarity). Cell projection, dendrite (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Expressed in the embryo in the brain and
CC spinal cord and in the first and fourth visceral arches. Most
CC abundant in adult brain, with lower levels in eye, heart, ovary,
CC oviduct, lung and pharynx.
CC -!- DEVELOPMENTAL STAGE: Expressed during early development.
CC -!- PTM: Phosphorylated. Autophosphorylation is stimulated by ligands
CC (By similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily.
CC -!- SIMILARITY: Contains 1 Eph LBD (Eph ligand-binding) domain.
CC -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR EMBL; L43621; AAA93527.1; -; mRNA.
DR ProteinModelPortal; Q91736; -.
DR SMR; Q91736; 1-115, 354-446, 510-807, 818-902.
DR PRIDE; Q91736; -.
DR HOVERGEN; HBG062180; -.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR009030; Growth_fac_rcpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; Pkinase_Tyr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; FN_III-like; 2.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF57184; Grow_fac_recept; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR SUPFAM; SSF47769; SAM_homology; 1.
DR PROSITE; PS01186; EGF_2; UNKNOWN_1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell adhesion; Cell membrane; Cell projection; Endosome;
KW Glycoprotein; Kinase; Membrane; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN <1 902 Ephrin type-B receptor 1-B.
FT /FTId=PRO_0000160275.
FT TOPO_DOM <1 459 Extracellular (Potential).
FT TRANSMEM 460 480 Helical; (Potential).
FT TOPO_DOM 481 902 Cytoplasmic (Potential).
FT DOMAIN 1 119 Eph LBD.
FT DOMAIN 241 342 Fibronectin type-III 1.
FT DOMAIN 352 443 Fibronectin type-III 2.
FT DOMAIN 537 800 Protein kinase.
FT DOMAIN 829 893 SAM.
FT NP_BIND 543 551 ATP (By similarity).
FT MOTIF 900 902 PDZ-binding (Potential).
FT COMPBIAS 101 237 Cys-rich.
FT ACT_SITE 662 662 Proton acceptor (By similarity).
FT BINDING 569 569 ATP (By similarity).
FT CARBOHYD 252 252 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 344 344 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 398 398 N-linked (GlcNAc...) (Potential).
FT NON_TER 1 1
SQ SEQUENCE 902 AA; 100851 MW; CCB9ABF7D39273CA CRC64;
HRVYVEMRFT VRDCSSLPNV PGSCKETFNL YYYETDSNID NKISTFWNES PYLKVDTIAA
DESFSQVDFG GRLMKVNTEV RSFGPLTRSG FYLAFQDYGA CMSLLSVRVF FKKCPSVVQN
FAVFPETMTG AESTSLVIAR GTCIPNAEEV DVPIKLYCNG DGEWMVPIGK CTCKAGYEPE
NHVVCKACPA AMFKANQGMG ICAQCPANSR STSEASPICI CRNGYYRADF DTPEAPCTSV
PSGPRNVISI VNETAITLEW HPPRETGGRD DVNYNIICKK CQSDRRGCSH CDDNVDFVPR
QLGLTDTRVF ISNLWVHTPY TFEIQAVNGV TNKSPFPPQH VSVNITTNQA APSSVPIMHQ
VKATMKSITL SWPQPEQPNG IILDYEIRYY EKDHHEFNSS LARSQTNTAS IEGLRPGVVY
VVQVRARTVA GYGKFSSKMC FQTLTEEDYK SELREQLPLI AGSAAAGVVF IVSLVAISIV
CSRKRTYSKE AVYSDKLQHY STGRGSPGMK IYIDPFTYED PNEAVREFAK EIDVSFVKIE
EVIGAGEFGE VYKGRLKLPS KREISVAIKT LKAGYSEKQR RDFLSEASIM GQFDHPNIIR
LEGVVTKSRP VMIITEFMEN GALDSFLRQN DGQFTVIQLV GMLRGIAAGM KYLSEMNYVH
RDLAARNILV NSNLVCKVSD FGLSRYLQDD TSDPTYTSSL GGKIPVRWTA PEAIRYRKFT
SASDVWSYGI VMWEVMSYGE RPYWDMSNQD VINAIEQDYR LPPPMDCPAA LHQLMLDCWQ
KDRNSRPRFG EIVNTLDKMI RNPASLKTVA TIPAVPSQPL LDRSIPDISA FTSVDDWLSA
IKMGQYRDNF LSSGFTSLHV VAQMTSEDLL RIGITLAGHQ KKILNSIQSM RVQISQSPTS
IA
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