ID Q66J04_XENLA Unreviewed; 639 AA.
AC Q66J04;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE SubName: Full=MGC83727 protein {ECO:0000313|EMBL:AAH81120.1};
GN Name=MGC83727 {ECO:0000313|EMBL:AAH81120.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH81120.1};
RN [1] {ECO:0000313|EMBL:AAH81120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocytes {ECO:0000313|EMBL:AAH81120.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC081120; AAH81120.1; -; mRNA.
DR RefSeq; NP_001087707.1; NM_001094238.1.
DR AlphaFoldDB; Q66J04; -.
DR IntAct; Q66J04; 1.
DR DNASU; 447531; -.
DR AGR; Xenbase:XB-GENE-865718; -.
DR OrthoDB; 2939922at2759; -.
DR Bgee; 447531; Expressed in egg cell and 19 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20839; C1_PKD1_rpt1; 1.
DR CDD; cd01239; PH_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF9; SERINE_THREONINE-PROTEIN KINASE D1; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 112..162
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 236..286
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 378..497
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 537..639
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 306..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 639 AA; 71408 MW; 30E4DC8ED06F7F5F CRC64;
MSAPPVIRPP SPAGTGLSLQ IQIGLSREPV LLPEPGELSL GAVREMACSI VDQKFPECGF
YGMYDKILLF RHDPNSENIL QLVKSEADIQ EGDLIEVVLS ASATFEDFQI RPHALFVHSY
RAPAFCDHCG EMLWGLVRQG LKCEGCGLNY HKRCAFKIPN NCSGVRKRRL SNVSLTGLSS
IRTLSVESFP STPDEPLLQK SPSESFVGRH SRSGSQLHIG RPIKLDKFFL TKVKVPHTFV
IHSYTRPTVC QHCKKLLKGL FRQGLQCKDC KFNCHKRCAP RVPHNCLGED AINGDLTDVM
MEEGRDDYEN RPDMDMDESP TTDSEGSISG CRSENGEMQE ADQDQDASDR TISPSASNNI
PLMRVVQSVK HTKRKSSSVM KEGWMVHYTS KDPMRKRHYW RLDSKCITLF QNDTGSKYYK
EIPLSEILSL EPAKDLSLLC PGANPHCFEI TTANLVYYVG ENLPLPVAPE MGNIMLTSGA
GLDVARMWEI AIQHALMPVN PKGANDGSIQ HRDISISISV SNCQVQENVD ISSVYQIFPD
EVLGSGQFGI VYGGKHRKTG RDVAIKIIDK LRFPTKQESQ LRNEVAILQN LHHQGVVNLE
CMFETPERVF VVMEKLHGDM LEMILSSEKD GYQTVLLNS
//
