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Database: UniProt
Entry: A0A3Q2UUR5_HAPBU
LinkDB: A0A3Q2UUR5_HAPBU
Original site: A0A3Q2UUR5_HAPBU 
ID   A0A3Q2UUR5_HAPBU        Unreviewed;       971 AA.
AC   A0A3Q2UUR5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=EPHB1 {ECO:0000313|Ensembl:ENSHBUP00000001335.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000001335.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000001335.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A3Q2UUR5; -.
DR   Ensembl; ENSHBUT00000013966.1; ENSHBUP00000001335.1; ENSHBUG00000002547.1.
DR   GeneTree; ENSGT00940000155297; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd09551; SAM_EPH-B1; 1.
DR   Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR042819; EphB1_SAM.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
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   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF17; EPHRIN TYPE-B RECEPTOR 1; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW   2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          1..188
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          309..419
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          420..515
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          606..869
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          898..962
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        731
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         612..620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         638
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        48..170
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        83..93
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   971 AA;  108439 MW;  643E360ADBA3A588 CRC64;
     MYGSILFEKV KFVFIGGLRK SLWQEYPDWE EVSGYDENLN TIRTYQVCNV FEPSQNNWLL
     TTFIDRRGAQ RIYVEIRFTV RDCSSIPNVP GSCKETFNLY YYENDAVIAT KGTVFWMEAP
     YLKVDTIAAD ESFSQVDFGG RLMKVNTEVR SFGPLSKNGF YLAFQDYGAC MSLLSVRVFY
     KKCPSVVQNF AVFPETMTGA ESTSLVIARG TCIANSEEVD VPIKLYCNGD GEWMVPIGSC
     TCKAGFEPDN GNVCRACPPG TFKSTQGPSL CLQCPPNSRS TSEAATICVC RNGYYRGDGD
     QPDKPCTSVP SSPRNVISIV NETSVILEWH APRETGGRDD VVYNIVCKKC QANRRSCSHC
     DDNVEFVPRQ LGLTETRVFI SNLLAHTVYS FEIQAVNGVS NKSPYPAQHV SIDITTNQAA
     PSIVPIMHQI SSTMNSFTLS WPQPEQPNGI ILDYELRYYE KDHAEINSTI LRSQTNTARV
     EALRPGTVYV VQVRARTVAG FGKYSSKMCF QTLTDGKDCR SELREQLPLI AGSAAAGVVF
     IVSLIAISIV CKLSLRADMS NCPSPLGCPT HFSGSPGMKI YIDPFTYEDP NEAVREFAKE
     IDVSTVKIEE VIGAGEFGEV YKGRLKLPGK REIYVAIKTL KAGYVEKQRR DFLSEASIMG
     QFDHPNIIRL EGVVTKSRPV MIVTEFMENG ALDSFLRQND GQFTVIQLVG MMRGISAGMK
     YLSEMNYVHR DLAARNILVN SNLVCKVSDF GLSRYLQDDT SDPSYTSSLG GKIPVRWTAP
     EAIAYRKFTS ASDVWSYGIV MWEVMSFGER PYWDMSNQDV INAIEQDYRL PPPMDCPSAL
     HQLMLDCWQK DRNVRPRFTD IVSTLDKMIR NPASLKAVAN IPAVPSQPLL DRSIPDVNTF
     SSVEDWLAAI KMSQYRDNFL NSGFTSLQLV AQMTSEDLLR IGVTLAGHQK KILTNIQSMR
     VQMSQSSTPM A
//
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