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TCPQ_MACFA
ID   TCPQ_MACFA              Reviewed;         548 AA.
AC   Q4R5J0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=T-complex protein 1 subunit theta;
DE            Short=TCP-1-theta;
DE   AltName: Full=CCT-theta;
GN   Name=CCT8; ORFNames=QflA-12463, QtsA-14677;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex, and Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC       molecular chaperone complex that assists the folding of proteins upon
CC       ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1,
CC       thereby regulating telomere maintenance. As part of the TRiC complex
CC       may play a role in the assembly of BBSome, a complex involved in
CC       ciliogenesis regulating transports vesicles to the cilia. The TRiC
CC       complex plays a role in the folding of actin and tubulin.
CC       {ECO:0000250|UniProtKB:P50990}.
CC   -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC       heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC       rings, 12 to 16 nm in diameter. Interacts with PACRG (By similarity).
CC       Interacts with DNAAF4 (By similarity). {ECO:0000250|UniProtKB:P42932,
CC       ECO:0000250|UniProtKB:P50990}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50990}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:P42932}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AB168763; BAE00870.1; -; mRNA.
DR   EMBL; AB169553; BAE01635.1; -; mRNA.
DR   RefSeq; NP_001270137.1; NM_001283208.1.
DR   AlphaFoldDB; Q4R5J0; -.
DR   SMR; Q4R5J0; -.
DR   STRING; 9541.XP_005548924.1; -.
DR   GeneID; 101864979; -.
DR   CTD; 10694; -.
DR   VEuPathDB; HostDB:ENSMFAG00000035602; -.
DR   eggNOG; KOG0362; Eukaryota.
DR   Proteomes; UP000233100; Chromosome 3.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd03341; TCP1_theta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012721; Chap_CCT_theta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02346; chap_CCT_theta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cell projection; Chaperone; Cilium; Cytoplasm;
KW   Cytoskeleton; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CHAIN           2..548
FT                   /note="T-complex protein 1 subunit theta"
FT                   /id="PRO_0000273200"
FT   REGION          529..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         30
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         318
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         400
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         466
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         505
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        224
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        254
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        260
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        459
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        534
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
FT   CROSSLNK        539
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P50990"
SQ   SEQUENCE   548 AA;  59516 MW;  CC60BC88240D7B29 CRC64;
     MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL
     EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR
     IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDVDEV SSLLRTSIMS KQYGNEVFLA
     KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA
     VYSCPFDGTI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM
     ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV CLSEVGDTQV
     VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
     KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL
     DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
     DWDDDQND
 
 
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