TBCK_CHICK
ID TBCK_CHICK Reviewed; 893 AA.
AC Q5F361;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=TBC domain-containing protein kinase-like protein;
GN Name=TBCK {ECO:0000250|UniProtKB:Q8TEA7}; ORFNames=RCJMB04_32m11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAH65423.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAH65423.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAH65423.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Involved in the modulation of mTOR signaling and expression
CC of mTOR complex components. Involved in the regulation of cell
CC proliferation and growth. Involved in the control of actin-cytoskeleton
CC organization. {ECO:0000250|UniProtKB:Q8TEA7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TEA7}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8TEA7}.
CC Midbody {ECO:0000250|UniProtKB:Q8TEA7}. Note=Mainly localized in the
CC cytoplasm during interphase. During metaphase, TBCK accumulates at the
CC mitotic spindle. At the end of mitosis, it is detected at the midbody.
CC {ECO:0000250|UniProtKB:Q8TEA7}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH65423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ851789; CAH65423.1; ALT_INIT; mRNA.
DR RefSeq; NP_001012595.1; NM_001012577.1.
DR AlphaFoldDB; Q5F361; -.
DR SMR; Q5F361; -.
DR STRING; 9031.ENSGALP00000017170; -.
DR PaxDb; Q5F361; -.
DR GeneID; 422534; -.
DR KEGG; gga:422534; -.
DR CTD; 93627; -.
DR VEuPathDB; HostDB:geneid_422534; -.
DR eggNOG; KOG1093; Eukaryota.
DR InParanoid; Q5F361; -.
DR PhylomeDB; Q5F361; -.
DR PRO; PR:Q5F361; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..893
FT /note="TBC domain-containing protein kinase-like protein"
FT /id="PRO_0000273280"
FT DOMAIN 1..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 466..651
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 790..889
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ SEQUENCE 893 AA; 100453 MW; E40C85C13AF6EC62 CRC64;
MFPLRDTEMG ASTFFASALP HDVCGSNGLP LTPNSIKILG RFQILKTITH PRLCQYVDIT
RGKHERLVVA AEHCENSLED LLREGKLVSS SRILCIAYEV LQGLQYMNKH GMVHRALSPR
NILLDRKGHV KLAKFGLYHM TAQGVDVDFP IGYPSYLAPE VIAQGMVKPS DHTQCEKPLP
SGPKSDLWSL GIILFELCVG RKLFQTLEIA ERLKFVITLG YVDDIVTVLA EEHGCLDIIK
DLSENVITLL KKCLTFQPSK RPTPEELMHD HLFSEVSLTY PPFHKPAGLF SSSPRCADLT
LPEDISQLCK DEDNDYLAER SIEEVYYLWC LAGGDLEKEL VNKEIIRSKP PVCTLPNFVL
EDGESFGQGR DRSSLLDDTT VTLSLCQLRN RLKDVGGEAF YPLLEDDQST LPHSNSSSEL
SAAANLPLII RERDTEYQLN RIVLFDRLLK AYPYKKNQIW KEARVDIPPL LRGITWAALL
GVEGAIQAKY DAIDKDTPIP TDRQIEVDIP RCHQYDELLS SPEGHAKFRR VLKAWVVSHP
DLVYWQGLDS LCAPFLYLNF NNEALAYACM SAFIPKYLYN FFLKDNSHVI QEYLTVFSQM
IAFHDPELSN HLNEIGFIPD LYAIPWFLTM FTHVFPLHKI FHLWDTLLLG NSSFPFCIGV
AILQQLRDRL LANGFNECIL LFSDLPEIDI ERCVRESINL FRWTPKSATY RQYAQPPRQA
NESNGTRSSM SCFSVDYQEA PRGDLSRDSI KLDDLKAEVS PRISAEDLID LCELTGPSHS
KTPIKKTKSS KPKLLVVDIR NSEDFNRGHI SGSINVPFAS AFTAEGDLIQ CPATATLQSF
KGRVVVIVGN AVKNTAAFAA HLVKSKYPRV CILDGGINKI KPTGLLTVPS PQI