ID A9VD25_MONBE Unreviewed; 1365 AA.
AC A9VD25;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=MONBRDRAFT_12702 {ECO:0000313|EMBL:EDQ84568.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ84568.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ84568.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CH991584; EDQ84568.1; -; Genomic_DNA.
DR RefSeq; XP_001750595.1; XM_001750543.1.
DR STRING; 81824.A9VD25; -.
DR EnsemblProtists; EDQ84568; EDQ84568; MONBRDRAFT_12702.
DR GeneID; 5895889; -.
DR KEGG; mbr:MONBRDRAFT_12702; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; A9VD25; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF550; FIBROBLAST GROWTH FACTOR RECEPTOR HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00084; Sushi; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00032; CCP; 3.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM01411; Ephrin_rec_like; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50923; SUSHI; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 887..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..223
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 284..340
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 785..820
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 822..866
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 942..1208
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 975
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 810..819
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 826..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 856..865
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1365 AA; 143556 MW; ECEEF93E594A2E9B CRC64;
MRVVNTTKSV ARGPSWRTIF LFRGGISDDN CYANSDSCGS NTACTFTGHD AYVCNCKSGY
YDVHSGTRGS YSCSAWSSCS SSQYQTSSPS AVVDRGCSSC SVLTCSNGAY RTGCGYGSSG
TCRTCDSCST TTSTTTSTTT STTTSTTTST TTTTTTTTTI LQCEPLTAPM DGNAQFEVHG
GISMAFFSCN AGFNMLGNPE LYCRYNEEEG AAQWSAPVPT CQGTLCDVDV DVNVVESSAT
NGGRYPSTLT SFCRSGYTPS GGDTRRTCST SGTYMGTPLT CVPVSCGDVP SDGATPNATT
ATYGDAVAYT CPAGTHMTGD AVLTCTASGA FSALPPSCVP CPINTAQAQS GHAETSCEPC
GANMATTSLG SHACSCDVNY IVSNGACQAC PSGFAKAGIA NTTSCPLVNL GVSYTLSVSA
AMATEEMAGD LEDALGAALS AVVAGDPIDT VAVTLIQEQT SATSLVSLAL GVTTSQRDSA
CCALQTVASG DFSSQLEELG WDDVATTFFS RSNCDGVLCG AACPAGSTLK DGWCVISELT
CPDGFAVVGD ACVSEEGNVR CPDGAISTLV NGSIVCTWAV VCPSPDHVYD PERGCFAPDT
CAAGEELTAE YYCIQSVKDC GDGFIYNKSL VTRENRANIR AGCQDINECA TSTSPCSSDT
MCVNTAGGFT CECIDDSLQY NAVLMSCVDP NACVTPPAIA ALGINYFVNG NGACVSDTYV
CNIVNSVYDP EIVTRNNLAL AGFKPCVASN SNCTVSGPSD AVVSCVCATG YSGDAQTGAN
SIGCQNYCNP NPCQFGGECE VSRRGARCKC AVGLSGPTCS ILDAACDGRC NGHGTCTPGA
ASPDLDPATS EYECECDEGF AGTDCEVDTV GSGTSQGSTA SDASTSMVIG GAAGGAILLL
LLLVLILFRR KQKPVTPTTS EDLYAVLEVR DADIWEVERQ FVRLGEKLGN GAFGEVFRAW
IRNRHSGEER GCAAKTLKPG APFEERQDFL SEMTVMKEIG AHPNVIGIIG HCLREEPYIL
LVELADLGNL RDYLRECRAS RSKPQSLHVS QMVDFCLQIA SGMAFLEQKN VIHRDLAARN
VLVGKKLECK ISDFGLARNI EGEEYKTTAT KLPVKWMAPE SLADRIYTTK SDVWSFGVTM
WEIFSLGGTP YKEYRNGDVF NLLEKGYRLP TPRQAPAEAD AIARMCWSLE AEDRPTFGEL
VDLLTDMIKE KNFSTAVPEA DSEELYESIA DLSDESEGSG IRAPARGSSG VGVWMGADMY
ESRFGGDDIY DNEANGQMLS EGPLMANKVF RANESKNAEG PIYEVAGPAT TGRLGPMAVY
DFPVANDTSG RRATVYDRHA QPAPSIDLQS SDATIYDFAL DDMEI
//
