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Database: UniProt
Entry: A0A091SFH2_9GRUI
LinkDB: A0A091SFH2_9GRUI
Original site: A0A091SFH2_9GRUI 
ID   A0A091SFH2_9GRUI        Unreviewed;       946 AA.
AC   A0A091SFH2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE   Flags: Fragment;
GN   ORFNames=N332_05385 {ECO:0000313|EMBL:KFQ39000.1};
OS   Mesitornis unicolor (brown roatelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX   NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ39000.1, ECO:0000313|Proteomes:UP000053369};
RN   [1] {ECO:0000313|EMBL:KFQ39000.1, ECO:0000313|Proteomes:UP000053369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ39000.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; KK817998; KFQ39000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091SFH2; -.
DR   Proteomes; UP000053369; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd10486; EphR_LBD_A8; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 1.
DR   CDD; cd09550; SAM_EPH-A8; 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; IPR034287; EphA8_rcpt_lig-bd.
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; 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; 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:SF7; EPHRIN TYPE-A RECEPTOR 8; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00014; FNTYPEIII.
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; 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:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFQ39000.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..178
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          297..407
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          408..503
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          592..853
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          885..945
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        717
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         598..606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         624
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        42..160
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        77..87
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ39000.1"
FT   NON_TER         946
FT                   /evidence="ECO:0000313|EMBL:KFQ39000.1"
SQ   SEQUENCE   946 AA;  105963 MW;  2B6BF4E9ED49E8E6 CRC64;
     VNLLDTSTIP GDWGWMTYPS HGWDSINEMD EFFSPIHTYQ VCNVMTPNQN NWLRTNWVQR
     DGARRVYAEI KFTLRDCNSM PGVLGTCKET FNLYYLESDR DLGTSTRESQ FMKIDTIAAD
     ESFTNVDLGV RRLKLNTEVR GVGPLSKRGF YLAFQDIGAC IAIVSVRVYY KKCPAMVRNL
     ASFSEAVTGA DSSSLVEVRG ECVGHSEERD TPKMYCSAEG EWLVPIGKCV CSAGYEEQRD
     SCMACQMGFY KSAPGDQLCA KCPLHSHSES RAARVCRCDN TFYRAVQDPP SAACTRPPSA
     PVNLISSVNG TSVTLEWGPP LDKGGRADIV YNVVCRRCMG DDGQCEACGS GIRYVPQQMS
     LVQGALTVTN LLAHTNYSFW VEAVNGVSDL SVESRRAAVA NITTNQAAPS QVVVVHQEST
     GQNSVTLLWQ EPDQPNGIIL EYEIKYYEKD KEMQSYSTLK SKDTAATISG LKPATRYIFQ
     VRARTSAGCG RFSQTVEVET GKPVSLRYDT MTIVWICLTL ITGLVALLVV LICKKRHCGY
     SKAFQDSDEE KMHYQNGQVK FPESKFYVDP HTYEDPCQAV HEFTREIEAS RIKIEKVIGS
     GESGEVCYGR LKLPGKREIP VAIKALKAGY TEKQRRDFLS EASIMAQFDH PNIIHLEGVV
     TRSKLVMIVT EYMENGSLDT FLRKHDGQFT IIQLVGMLRG IGAGMRYLSD LGYVHRDLAA
     RNILVNSNLV CKVSDFGLSR ILEDDPDAAY TTTGGKIPIR WTAPEAIAYR KFSSASDVWS
     YGIVMWEVLA YGERPYWNMT NRDVINSVEE GYRLPAPMGC PTALHQLMLD CWQKDRSERP
     RFSQIVGILD KLIRNPDHLK CTATVNRFTQ TRLDRGLFDL AGCLTVEDWL DSIRLGHYRD
     NFAMAGYSSL GMVMRMNIED VRSLGITMMG HQKKILSSIQ AMRSQL
//
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