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Database: UniProt
Entry: Q91736
LinkDB: Q91736
Original site: Q91736 
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   29-OCT-2014, entry version 121.
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       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein. Early endosome membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Cell
CC       projection, dendrite {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 Eph LBD (Eph ligand-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00883}.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00184}.
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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:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of 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:0060996; P:dendritic spine development; ISS:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; 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; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR027936; Eph_TM.
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_N_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_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; PF14575; EphA2_TM; 1.
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; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS01186; EGF_2; 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. {ECO:0000255}.
FT   TRANSMEM    460    480       Helical. {ECO:0000255}.
FT   TOPO_DOM    481    902       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN        1    119       Eph LBD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00883}.
FT   DOMAIN      240    350       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      351    448       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      537    800       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      829    893       SAM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00184}.
FT   NP_BIND     543    551       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       900    902       PDZ-binding. {ECO:0000255}.
FT   COMPBIAS    101    237       Cys-rich.
FT   ACT_SITE    662    662       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING     569    569       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD    252    252       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    344    344       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    398    398       N-linked (GlcNAc...). {ECO:0000255}.
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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