TPC14_DANRE
ID TPC14_DANRE Reviewed; 595 AA.
AC E7F240;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Trafficking protein particle complex subunit 14;
DE AltName: Full=Microtubule-associated protein 11 {ECO:0000305};
GN Name=trappc14 {ECO:0000312|ZFIN:ZDB-GENE-111102-3};
GN Synonyms=map11 {ECO:0000312|ZFIN:ZDB-GENE-111102-3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=30715179; DOI=10.1093/brain/awz004;
RA Perez Y., Bar-Yaacov R., Kadir R., Wormser O., Shelef I., Birk O.S.,
RA Flusser H., Birnbaum R.Y.;
RT "Mutations in the microtubule-associated protein MAP11 (C7orf43) cause
RT microcephaly in humans and zebrafish.";
RL Brain 142:574-585(2019).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31467083; DOI=10.1074/jbc.ra119.008615;
RA Cuenca A., Insinna C., Zhao H., John P., Weiss M.A., Lu Q., Walia V.,
RA Specht S., Manivannan S., Stauffer J., Peden A.A., Westlake C.J.;
RT "The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for
RT preciliary vesicle tethering at the mother centriole during ciliogenesis.";
RL J. Biol. Chem. 294:15418-15434(2019).
CC -!- FUNCTION: Specific subunit of the TRAPP (transport protein particle) II
CC complex, a highly conserved vesicle tethering complex that functions in
CC late Golgi trafficking as a membrane tether (By similarity). TRAPP II
CC complex has also GEF activity toward RAB1A (By similarity). TRAPPC14 is
CC required for ciliogenesis (PubMed:30715179).
CC {ECO:0000250|UniProtKB:Q3TLI0, ECO:0000250|UniProtKB:Q8WVR3,
CC ECO:0000269|PubMed:30715179}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP II complex, which includes
CC at least TRAPPC1, TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC4, TRAPPC5,
CC TRAPPC6A/B, TRAPPC9, TRAPPC10 and TRAPPC14. TRAPPC9, TRAPPC10 and
CC TRAPPC14 are specific subunits of the TRAPP II complex. Interacts with
CC alpha-tubulin during mitosis. {ECO:0000250|UniProtKB:Q8WVR3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8WVR3}. Vesicle {ECO:0000250|UniProtKB:Q8WVR3}.
CC Midbody {ECO:0000250|UniProtKB:Q8WVR3}. Note=During mitosis, precedes
CC alpha-tubulin in gap formation of cell abscission at the midbody and is
CC co-localized with PLK1 at the edges of microtubules extensions of
CC daughter cells post cytokinesis abscission.
CC {ECO:0000250|UniProtKB:Q8WVR3}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein in early
CC embryos results in curved bodies and small eyes. Morphants exhibit
CC reduced ciliation in otic vesicles, neuromasts, and olfactory placodes
CC (PubMed:31467083). In a knockout model mutant animals show head to body
CC ratios lower than those of controls. They have decreased brain cell
CC proliferation rate at 24 hpf (PubMed:30715179).
CC {ECO:0000269|PubMed:30715179, ECO:0000269|PubMed:31467083}.
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DR EMBL; CR848737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001339329.2; XM_001339293.6.
DR AlphaFoldDB; E7F240; -.
DR STRING; 7955.ENSDARP00000102748; -.
DR PaxDb; E7F240; -.
DR PeptideAtlas; E7F240; -.
DR Ensembl; ENSDART00000109268; ENSDARP00000102748; ENSDARG00000078891.
DR GeneID; 100003958; -.
DR KEGG; dre:100003958; -.
DR CTD; 55262; -.
DR ZFIN; ZDB-GENE-111102-3; trappc14.
DR eggNOG; ENOG502QSBJ; Eukaryota.
DR GeneTree; ENSGT00390000014725; -.
DR HOGENOM; CLU_031637_0_0_1; -.
DR InParanoid; E7F240; -.
DR OMA; GEDDYMA; -.
DR OrthoDB; 536210at2759; -.
DR PhylomeDB; E7F240; -.
DR TreeFam; TF331500; -.
DR PRO; PR:E7F240; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000078891; Expressed in brain and 19 other tissues.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:1990071; C:TRAPPII protein complex; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR InterPro; IPR031626; TRAPPC14.
DR PANTHER; PTHR16096; PTHR16096; 1.
DR Pfam; PF15806; DUF4707; 1.
PE 3: Inferred from homology;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..595
FT /note="Trafficking protein particle complex subunit 14"
FT /id="PRO_0000446856"
FT REGION 84..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 66359 MW; 934D5DB8A5C73B7F CRC64;
MVLMMESQCE YFMYFPAVPI SDLSDPAKYR TLPRRSHLYL GETVRFLLVL RSQSASGSSD
GSCGSEQHSS RSWRELAGSL SAVASVSPGD SRQRTQPLYH DYHSSGDECV EDTDEDDAAE
AVGCPGRGGP RYRGFRECKP LLIHNNPGNG VREFRRAPVQ SPVDEPVVLS DEVIFPLTVS
LDKLPVNTLK VKIIVTVWKQ EEEKAEIQEH GYLSILQQKS PCQTFRQDLN TFKAQVSTTL
NVLPPPTVKC QQMTVSGRHL TVLKVLNGSS QEEVCVRDVK ILPNFNASYL PMMPDGSVLL
VDNVCHQSGE VAMASFYRMD SESSHLPSML SALEEQNFLF QLQLNNQPQD DSNEGLEVPL
VAVLQWSTSK LPFTNSIYTH YSLPSIRLDR PRFIMTASCP SAVRTRENFR VRYTLLNNLQ
DFLAVRLVWT PEGRGQKEDP AVNAVVCHSP LSNLGYCRKG STLSVSVAFQ ILRAGLFELS
QHMKLKLQFT ASVSNPPPDA RPLSRKNSPS SPAVRDILDR HQASLSLGRS QSFSHQQPSK
FHLTRTGSVM ERRAITPPVG SPVGRPLYLP PDRNILSLDK IAKRECKVLV LDSHN
