ID M3X6R2_FELCA Unreviewed; 344 AA.
AC M3X6R2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Tubulin folding cofactor C {ECO:0000313|Ensembl:ENSFCAP00000022314.3};
GN Name=TBCC {ECO:0000313|Ensembl:ENSFCAP00000022314.3,
GN ECO:0000313|VGNC:VGNC:65993};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000022314.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000022314.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022314.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000022314.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022314.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000022314.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022314.3};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state.
CC {ECO:0000256|ARBA:ARBA00026055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TBCC family.
CC {ECO:0000256|ARBA:ARBA00008848}.
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DR EMBL; AANG04003966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3X6R2; -.
DR STRING; 9685.ENSFCAP00000022314; -.
DR PaxDb; 9685-ENSFCAP00000022314; -.
DR Ensembl; ENSFCAT00000004146.4; ENSFCAP00000022314.3; ENSFCAG00000004145.4.
DR VGNC; VGNC:65993; TBCC.
DR eggNOG; KOG2512; Eukaryota.
DR GeneTree; ENSGT00940000162058; -.
DR HOGENOM; CLU_032612_2_1_1; -.
DR InParanoid; M3X6R2; -.
DR OMA; YFQHEIT; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000004145; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR006599; CARP_motif.
DR InterPro; IPR027684; TBCC.
DR InterPro; IPR031925; TBCC_N.
DR InterPro; IPR038397; TBCC_N_sf.
DR InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR Pfam; PF07986; TBCC; 1.
DR Pfam; PF16752; TBCC_N; 1.
DR SMART; SM00673; CARP; 2.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 169..321
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 38572 MW; DD7954F9F48826C1 CRC64;
METAACSAAA ANGAVGSQRD RSLVPERLQR REQERQLEVE RRKQKRQNQE VEEEKSDFFA
AAFARERAAV EELLEGGESM ERLEEAAARL QGLQKLVNDS VLFLAAYDLR QGQEALTRLQ
TTLAERRQEL QPKKRFAFKT RRKDAASAAK VDSAPGAPAA EGILASPPPL KEEGGIGSSW
VFGFSNVESQ VLEKRAEELH QRDVLLTELS KCTVRLYGNP NTLRLAKARS CTVLCGPVST
SVFLEDCSDC VLAVACQQLR VHTTRDTRIF LQVTSRAIVE DCSGIQFAPY TWSYPGIDKD
FEGSGLDRSK NNWNDVDDFN WLARDMASPN WSILPEEERM VQWD
//
