ID H2QZG8_PANTR Unreviewed; 1341 AA.
AC H2QZG8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MYO3B {ECO:0000313|Ensembl:ENSPTRP00000038973.5,
GN ECO:0000313|VGNC:VGNC:14316};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000038973.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000038973.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000038973.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
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DR EMBL; AACZ04058514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04058516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_525960.4; XM_525960.4.
DR PaxDb; 9598-ENSPTRP00000038973; -.
DR Ensembl; ENSPTRT00000050175.5; ENSPTRP00000038973.5; ENSPTRG00000012624.6.
DR GeneID; 470579; -.
DR CTD; 140469; -.
DR VGNC; VGNC:14316; MYO3B.
DR eggNOG; KOG0587; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000159309; -.
DR HOGENOM; CLU_000192_10_2_1; -.
DR InParanoid; H2QZG8; -.
DR OrthoDB; 1094820at2759; -.
DR TreeFam; TF326512; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012624; Expressed in cortex of kidney and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0032433; C:filopodium tip; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR GO; GO:0032426; C:stereocilium tip; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0030832; P:regulation of actin filament length; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR CDD; cd06639; STKc_myosinIIIB_N; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF1; MYOSIN-IIIB; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 27..293
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 343..1058
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 939..961
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1111..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 436..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1341 AA; 151599 MW; FBBF52E8D2652777 CRC64;
MKHLYGLFHY NPMMLGLESL PDPTDTWEII ETIGKGTYGK VYKVTNKRDG SLAAVKILDP
VSDMDEEIEA EYNILQFLPN HPNVVKFYGM FYKADHCVGG QLWLVLELCN GGSVTELVKG
LLRCGQRLDE AMISYILYGA LLGLQHLHNN RIIHRDVKGN NILLTTEGGV KLVDFGVSAQ
LTSTRLRRNT SVGTPFWMAP EVIACEQQYD SSYDARCDVW SLGITAIELG DGDPPLFDMH
PVKTLFKIPR NPPPTLLHPE NWCEEFNHFI SQCLIKDFER RPSVTHLLDH PFIKGVHGKV
LFLQKQLAKV LQDQKHQNPV AKTRHERMHT RRTYHVEDAE KYCLEDDLVN LEVLDEDTII
HQLQKRYADL LIYTYVGDIL IALNPFQNLS IYSPQFSRLY HGVKRASNPP HIFASADAAY
QCMVTLSKDQ CIVISGESGS GKTESAHLIV QHLTFLGKAN NQTLREKILQ VNSLVEAFGN
SCTAINDNSS RFGKYLEMMF TPTGVVMGAR ISEYLLEKSR VIKQAAGEKN FHIFYYIYAG
LHHQKKLSDF RLPEEKPPRY IADEAGRVMH DITSKESYRR QFEAIQHCFR IIGFTDKEVH
SVYRILAGIL NIGNIEFAAI SSQHQTDKSE VPNAEALQNA ASVLCISPEE LQEALTSHCV
VTRGETIIRA NTVDRAADVR DAISKALYGR LFSWIVNRIN TLLQPDKNIC SAGGGMNVGI
LDIFGFENFQ RNSFEQLCIN IANEQIQYYF NQHVFALEQM EYQNEGIDAI PVEYEDNRPL
LDMFLQKPLG LLALLDEESR FPQATDQTLV DKFEDNLRCK YFWRPKGVEL CFGIQHYAGK
VLYDASGVLE KNRDTLPADV VVVLRTSENK LLQQLFSIPL TKTGNLAQTR ARITVASRSL
PPHFSAGKAK VDTLEVIRHP EETTNMKRQT VASYFRYSLM DLLSKMVVGQ PHFVRCIKPN
DDREALQFSR ERVLAQLRST GILETVSIRR QGYSHRILFE EFVKRYYYLA FTAHQTPLAS
KESCVAILEK SRLDHWVLGK TKVFLKYYHV EQLNLLLREV IGRVVVLQAY TKGWLGARRY
KRVREKREKG AIAIQSAWRG YDARRKFKKI SNRRNESAAH NQAGDTSNQS GGPHSPVAAG
TRGSAEVQDC SEPGDHKVLR GSVHRRSHSQ AESNNGHTQS SSNSPAVTEK NGHSQAQSSP
KGCDISAGHA NKHSVSGTDL LSSRICHPAP DQQGLSLWGA PQKPGSENGL AQKHRTPRRR
CQQPKMLSSP EDTMYYNQLN GTLEYQGSKR KPRKLGQIKV LDGEDEYYKS LSPVDCIPEE
NNSAHPSFFS SSSKGDSFAP H
//
