GenomeNet

Database: UniProt
Entry: A0A3Q1C8U9_AMPOC
LinkDB: A0A3Q1C8U9_AMPOC
Original site: A0A3Q1C8U9_AMPOC 
ID   A0A3Q1C8U9_AMPOC        Unreviewed;       338 AA.
AC   A0A3Q1C8U9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Tubulin folding cofactor C {ECO:0000313|Ensembl:ENSAOCP00000016626.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000016626.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000016626.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
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   AlphaFoldDB; A0A3Q1C8U9; -.
DR   STRING; 80972.ENSAOCP00000016626; -.
DR   Ensembl; ENSAOCT00000025649.1; ENSAOCP00000016626.1; ENSAOCG00000021589.1.
DR   GeneTree; ENSGT00940000162058; -.
DR   OMA; YFQHEIT; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT   DOMAIN          160..314
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   COILED          15..49
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   338 AA;  37699 MW;  F974A9C2FC8F32A8 CRC64;
     MSFVDTGVTG GSGAARLQER LQKRHQARIE DAERRREAKE SRSVAEEEVQ YFSRSFSRER
     ADIEELLASC CGAERSLVTQ NLEEATDRTT QLQKFLNDSL MFLTQYELRQ AQAALQKLQT
     SLTETREGAL PKKKFTFRAR TKAAGKVSAA GTPPPAAASP ADPGVMAVDG ASEQCGFSNV
     RDELLIKTAE EIQKQDVLLT HLSNCRVRLI GSPSTLHLKN IDSCEILCGP VSSSVFIDQC
     RNSTLAFPCQ QLRTHNTSDT QVYLHVTSRA IIEDCWGLSF APFSWSYPTL EEDFAVSGLD
     RQRNNWREVD DFNWLAAGTP SPNWTVLPEA DRKTSWDS
//
DBGET integrated database retrieval system