ID F6RMP9_CIOIN Unreviewed; 831 AA.
AC F6RMP9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Discoidin domain-containing receptor 2 {ECO:0008006|Google:ProtNLM};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000023911.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000023911.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; EAAA01002989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EAAA01002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6RMP9; -.
DR Ensembl; ENSCINT00000024157.2; ENSCINP00000023911.2; ENSCING00000006493.3.
DR GeneTree; ENSGT00940000169525; -.
DR HOGENOM; CLU_008873_2_0_1; -.
DR InParanoid; F6RMP9; -.
DR OMA; IFERVEC; -.
DR TreeFam; TF317840; -.
DR Proteomes; UP000008144; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd05051; PTKc_DDR; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF580; DISCOIDIN DOMAIN RECEPTOR, ISOFORM F; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
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 399..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..181
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 572..831
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 831 AA; 94396 MW; D88A748EAB2AEC2E CRC64;
LSFSTVAHII ELVHSNQLIE LITLCRHALG MQSKRIRDSF LTSSTFHAPG TKGQYARLER
DEGDGAWCPS GYIQPDTIDQ YLQIDLPEPN FITNVATQGR YARGLGREYT SSYMLNYSRD
GETWFQWSNY QGVKKLQGNA DTNTVKRQML NPGVAAASHV RIIPVSTRTM SVCLRLELYG
CHWASGLVSY DIPAPMDSIA GQTNTRNTKY SDDTYDGTIS TNWFRNGLGQ LTDGVIGGND
LSQVGWSRSK SNDVTMTFRF ADVRNFTRMR NYPTQLKLYR LFTSVKVSFS LNGKTFPSTA
NARSLAYEVP KDAFDRTARF VDVPLRNSIA RYVRASFRIG DEYLLVSEVE FDNTTYNFKH
IVTLILTFPD VLPPSDAFRY PDEDVSNEPT VTPTVSNNLP VIIGSLLGVI GLLVFIVLGL
CYRQHRLRKK MVRYLFIFYV GPENIYSRVG EDGTTPLRYS YSRTSDNCGR SDHMVTLEPI
SRQSSSTGAG VVCSHNILSC TREVTRLLNQ PDVTMNTPNS SHYAESSIFL PSLEAQIGNT
SCIHHIFQFA DEMMSLMSLH GDKPPEFPRE KLEVVEQLGE GQFGEVQLCE LDEPVLVAVK
VLRADATSNA KEDFLKEVRV MSQMQDPNIV HLIAVCTNDE PYAMITEYME NGDLNQYLRS
CAVFSNEVLI NMCVQIASGM RYLSSHKFVH RDLATRNCLV DSNHSIRIAD FGMSRNMYQS
DYYRIQGRAV LPIRWMSWEC VLMGKFSSAS DAWAFGVTLW EIFSFCKLQP HNSLTDQQVI
ENMHHVFKRT GEEVHLQRPK RCPATLFNLI RQCWKRQPED RPTFEQLHGY L
//
