TBCD_CAEEL
ID TBCD_CAEEL Reviewed; 1163 AA.
AC Q19493;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tubulin-specific chaperone D {ECO:0000250|UniProtKB:Q9BTW9};
DE AltName: Full=Tubulin folding cofactor D homolog {ECO:0000312|WormBase:F16D3.4};
GN Name=tbcd-1 {ECO:0000312|WormBase:F16D3.4};
GN ORFNames=F16D3.4 {ECO:0000312|WormBase:F16D3.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAB01496.2, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB01496.2,
RC ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16054029; DOI=10.1016/j.devcel.2005.07.003;
RA Srayko M., Kaya A., Stamford J., Hyman A.A.;
RT "Identification and characterization of factors required for microtubule
RT growth and nucleation in the early C. elegans embryo.";
RL Dev. Cell 9:223-236(2005).
CC -!- FUNCTION: Tubulin-folding protein; involved in the first step of the
CC tubulin folding pathway (By similarity). Plays a role in microtubule
CC polymerization (PubMed:16054029). {ECO:0000250|UniProtKB:Q9BTW9,
CC ECO:0000269|PubMed:16054029}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC microtubule growth rate. {ECO:0000269|PubMed:16054029}.
CC -!- SIMILARITY: Belongs to the TBCD family. {ECO:0000305}.
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DR EMBL; BX284601; CAB01496.2; -; Genomic_DNA.
DR PIR; T21018; T21018.
DR RefSeq; NP_492270.1; NM_059869.3.
DR AlphaFoldDB; Q19493; -.
DR STRING; 6239.F16D3.4; -.
DR EPD; Q19493; -.
DR PaxDb; Q19493; -.
DR PeptideAtlas; Q19493; -.
DR EnsemblMetazoa; F16D3.4.1; F16D3.4.1; WBGene00008887.
DR UCSC; F16D3.4; c. elegans.
DR WormBase; F16D3.4; CE53738; WBGene00008887; tbcd-1.
DR eggNOG; KOG1943; Eukaryota.
DR GeneTree; ENSGT00390000017103; -.
DR HOGENOM; CLU_003043_0_0_1; -.
DR InParanoid; Q19493; -.
DR OrthoDB; 79003at2759; -.
DR PhylomeDB; Q19493; -.
DR PRO; PR:Q19493; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008887; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016328; C:lateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0034333; P:adherens junction assembly; IBA:GO_Central.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:WormBase.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033162; TBCD.
DR InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
DR PANTHER; PTHR12658; PTHR12658; 1.
DR Pfam; PF12612; TFCD_C; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 3: Inferred from homology;
KW Chaperone; Microtubule; Reference proteome.
FT CHAIN 1..1163
FT /note="Tubulin-specific chaperone D"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436250"
SQ SEQUENCE 1163 AA; 131654 MW; E9BE6F02252ACE4C CRC64;
MDEDAPVDES NEGIIGCLPS AVNIHHIEEI KELVDQLPII FKLENECDET AAEVNYLRYS
RLLHLYQEQP RLLDKWIPEI VANLVDLVTL IGIDVSKPRA MTPLSRESLK YLSDLCIVRG
SKTIVRLLPH QVHLLDPLLQ TLEYYETSQL SDHNQRNVLL MWLWIVVKNP FDLRRFDPTG
DPDNVITRIM NVALHYMKWD WNSSQASAAL VIAHCLSRTD GIPKVLSFLS RLLDSIKTHH
ENKKLLLADL ILLLAILKHV DRRVLTGHIG TIHEQLSFLY PIDEKKGGLI CKCLVKVVQR
IGLIALKPRT CSWSYNRGKR LLEGMLDDNE EYSDEPSFSN KVNSNQSCNN EIDKENQWND
GDELENSEIV EFALMHVLEA LSHSDTAVRW SAAKGVGRIT VRLPNFDLAT QVVGSIISSH
FGEVAEYSSW HSHGACLALA ELAHRGVLLP SLLEDIVPAL ELSLVFEDVM GRHQNGNQVR
DAACYAVWAL SRTYEPSMMA PYLQRLASAL LCGALFDRQV NLRRAASAAL QEMVGRQKNV
SHGIPLIQSV DYFAVTNRQK CYEHLCVPVA EYSTYSAIIL RHLITKKVVH WDEKIREQAA
ISLEKISEIR LENVSDDYYM EILDDFLKAS CETRISPFLR HGYLLASGHL IKGLTSRGMD
FSSKQTEIAW IPHILWPFCD MTTQPGALIR RTLCKFIQLV SASKKVLLLE KDKSEWLDVL
LQLITDPREI IRSLAKTAVG EFVMTYLMND EELIQKVKTR VIAAMTKCSD ESERIGMGMI
CESLNSEAVD YEMFESLCNT ILTPTSSDAK WALARQQTVF ALNRISVNSS TETFNRIGQK
CFETLYKAMT DYTTSANGDI GRFVREASMR AMSTILVDAK TEPPFLDEHV IKSAKYMVQQ
SAERISRTRE CACACLKSLV KCEITGRCLP HIDLLMNIYS EPMDFISDRT VFQLKPLLDL
GSEYYEQLIL GIVVSAGGLA EGTQKTAKQL LLDHQREICE NKPRFDHFLS TCADLFQRAR
KVNRIGNSFM QILPQIFGNL GIYEQCPETS ESIIEMVDTM KTIAVRSSMM SRQRLSIDSL
GELLNCGKKS TVYRSALTMI LDTLNSQQPV LRKSAAERLY EHLCCAEESD DEVLEVLATT
NWQDENDNVL KQAVAGISEK LIF
