TBCC_PONAB
ID TBCC_PONAB Reviewed; 346 AA.
AC Q5R5J7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Tubulin-specific chaperone C;
DE AltName: Full=Tubulin-folding cofactor C;
DE Short=CFC;
GN Name=TBCC;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin-folding protein; involved in the final step of the
CC tubulin folding pathway. {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Detected
CC predominantly in the photoreceptor connecting cilium. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR EMBL; CR860861; CAH92969.1; -; mRNA.
DR RefSeq; NP_001126753.1; NM_001133281.1.
DR AlphaFoldDB; Q5R5J7; -.
DR BMRB; Q5R5J7; -.
DR SMR; Q5R5J7; -.
DR STRING; 9601.ENSPPYP00000019357; -.
DR PRIDE; Q5R5J7; -.
DR GeneID; 100173755; -.
DR KEGG; pon:100173755; -.
DR CTD; 6903; -.
DR eggNOG; KOG2512; Eukaryota.
DR InParanoid; Q5R5J7; -.
DR OrthoDB; 1618114at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
DR Gene3D; 1.20.58.1250; -; 1.
DR Gene3D; 2.160.20.70; -; 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; PTHR15139; 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 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..346
FT /note="Tubulin-specific chaperone C"
FT /id="PRO_0000285108"
FT DOMAIN 171..323
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15814"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15814"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15814"
SQ SEQUENCE 346 AA; 39330 MW; 03E3027C25533B37 CRC64;
MESVSCSAAP VRSGDMESQR DMSLVPERLQ RREQERQLEV ERRKQKRQNQ EVEKENSHFF
AATFARERAA VEELLERAES VERLEEAASR LQGLQKLIND SVFFLAAYDL RQGQEALARL
QAALAERRRE LQPKKRFAFK TRGKDAASCT KVDAAPGIPP AVESIQDSPL PKKAEGDLGS
SWLCGFSNLE SQVLEKRASE LHQRDVLLTE LSNCTVRLYG NPNTLRLTKA HSCKLLCGPV
STSVFLEDCS DCVLAVACQQ LRIHSTKDTR IFLQVTSRAI VEDCSGIQFA PYTWSYPEID
KDFESSGLDR SKNNWNDVDD FNWLARDMAS PNWCILPEEE RNIQWD
