ID A0A3Q2FVM4_CYPVA Unreviewed; 342 AA.
AC A0A3Q2FVM4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tubulin folding cofactor C {ECO:0000313|Ensembl:ENSCVAP00000011545.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000011545.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000011545.1}
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}.
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DR RefSeq; XP_015240047.1; XM_015384561.1.
DR AlphaFoldDB; A0A3Q2FVM4; -.
DR STRING; 28743.ENSCVAP00000011545; -.
DR Ensembl; ENSCVAT00000018551.1; ENSCVAP00000011545.1; ENSCVAG00000013831.1.
DR GeneID; 107090920; -.
DR KEGG; cvg:107090920; -.
DR CTD; 6903; -.
DR GeneTree; ENSGT00940000162058; -.
DR OMA; YFQHEIT; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000265020; 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 Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT DOMAIN 164..318
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 127..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 37734 MW; 500C06EAAE2275A1 CRC64;
MDAAEEISKA EEFSDKNASK IHERIVKRQQ LLAEGAERRK EARQKQTVAG ESSEVFLEAF
NAERAGLEQL LSGCLGAERT AVTRDLEQAA AKMAELQKLL NDSMMFLNQY EIRVAQSALQ
KLQASLSESR EQAMPKKKFT FRSRSKAAEK DSAAPPAAPP AAPPAVTEVD GAAASSQQPD
FSNISDQLLE KTSEEIQSRD VLLTHLTNCK VRLYGSPSTL HLKHLHGCEV LCGPVATSVF
VDHCTNSVLA FPCQQLRTHN TSDTQVYLHV TSRAIIEDCR GVGFAPFSWS YPTLDQDFSA
SGLDPNRNNW SQVDDFNWLA AGTPSPNWTV IPEADRKTTW DP
//
