ID A0A093HFZ4_STRCA Unreviewed; 742 AA.
AC A0A093HFZ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Discoidin domain-containing receptor 2 {ECO:0000313|EMBL:KFV77877.1};
DE Flags: Fragment;
GN ORFNames=N308_04839 {ECO:0000313|EMBL:KFV77877.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV77877.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV77877.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV77877.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
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; KL205999; KFV77877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HFZ4; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:UniProt.
DR CDD; cd05097; PTKc_DDR_like; 1.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF297; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFV77877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..47
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 448..734
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV77877.1"
FT NON_TER 742
FT /evidence="ECO:0000313|EMBL:KFV77877.1"
SQ SEQUENCE 742 AA; 84538 MW; 4A87AA92665BC8EB CRC64;
QVIQGNIDTY DVVLKDLRPP IIARFIRVIP VTELPMTVCM RVELYGCVWY DGLASYSIPE
GGTIAAPGFP IVYLNDSTYD GYHERRHLYG GLGQLTDGVL GLDDFTQSHQ YRVWPGYDYV
GWKNESFSTG AVEMEFQFDR PRNFTSMKVH CNNMFSKGVK IFQKVECLFK PRLIADWESE
PVGVATVLDD KNPSARFVTV PLNQRVGKAI LCRFYFADSW MMMSEISFQS DMESVNPILV
TVAPSTTEPL EAEYNVTEGI WETTSSVTST WIGEKADDSN TSILVGCLVA IILLLLMIII
IILWKQYVQK RLEKAPRRIL EEDATVRLSF YSYTIANNQT QIHQSNPTYE RAFPLDLEYH
QPATLLHKLP ELSQSAEDSV CSGDYAEPDL TKSTPHQGFQ NNVPHYAETD IVHLQGVTGN
NMYAVPALTV DSLTKKDISV GEFPRQQLRL KEKLGEGQFG EVHLCEADGL LEFLGVSSTE
FTRQPVLVAV KMLRSDVNKT ARNDFLKEIK IMSRLKNPNI IRLLGVCVRD DPLCMITEYM
ENGDLNQFLS QREIYSKFAV SNNIPCVSYS NLLYMATQIA SGMKYLASLN FVHRDLATRN
CLVGNNYTIK IADFGMSRNL YSGDYYRIQG RAVLPIRWMA WESILLGKFT TASDVWAFGV
TLWEMFILCK EQPYSLLSDE QVIENTGEFF RSQGRQIYLS QTPLCPNPVF DLMLKCWSRD
IKDRPTFDMI HHFLLEQMES NI
//
