TPC14_MOUSE
ID TPC14_MOUSE Reviewed; 580 AA.
AC Q3UTZ3; E9Q2V5; Q8JZV2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Trafficking protein particle complex subunit 14;
DE AltName: Full=Microtubule-associated protein 11 {ECO:0000305};
GN Name=Trappc14 {ECO:0000312|MGI:MGI:2385896};
GN Synonyms=Map11 {ECO:0000312|MGI:MGI:2385896};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-580.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. TRAPPC14 is dispensable
CC for TRAPPII complex integrity but mediates RAB3IP preciliary vesicle
CC trafficking to the mother centriole during ciliogenesis. Modulates YAP1
CC activity as transcriptional regulator. {ECO:0000250|UniProtKB:Q8WVR3}.
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. Interacts with RAB3IP (via the N-terminal
CC region); this interaction mediates RAB3IP association with the TRAPP II
CC complex. Interacts with TRAPPC10. Interacts with FBF1.
CC {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. Colocalizes with RAB3IP on
CC preciliary vesicles. {ECO:0000250|UniProtKB:Q8WVR3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37034.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK138960; BAE23836.1; -; mRNA.
DR EMBL; AC159257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037034; AAH37034.1; ALT_INIT; mRNA.
DR CCDS; CCDS39343.2; -.
DR RefSeq; NP_694801.2; NM_153161.3.
DR AlphaFoldDB; Q3UTZ3; -.
DR IntAct; Q3UTZ3; 1.
DR STRING; 10090.ENSMUSP00000046898; -.
DR iPTMnet; Q3UTZ3; -.
DR PhosphoSitePlus; Q3UTZ3; -.
DR EPD; Q3UTZ3; -.
DR MaxQB; Q3UTZ3; -.
DR PaxDb; Q3UTZ3; -.
DR PRIDE; Q3UTZ3; -.
DR ProteomicsDB; 357059; -.
DR Antibodypedia; 16406; 90 antibodies from 17 providers.
DR Ensembl; ENSMUST00000048421; ENSMUSP00000046898; ENSMUSG00000036948.
DR GeneID; 231807; -.
DR KEGG; mmu:231807; -.
DR UCSC; uc009afe.2; mouse.
DR CTD; 55262; -.
DR MGI; MGI:2385896; Trappc14.
DR VEuPathDB; HostDB:ENSMUSG00000036948; -.
DR eggNOG; ENOG502QSBJ; Eukaryota.
DR GeneTree; ENSGT00390000014725; -.
DR HOGENOM; CLU_031637_0_0_1; -.
DR InParanoid; Q3UTZ3; -.
DR OMA; AHIGRRE; -.
DR OrthoDB; 536210at2759; -.
DR PhylomeDB; Q3UTZ3; -.
DR TreeFam; TF331500; -.
DR BioGRID-ORCS; 231807; 0 hits in 72 CRISPR screens.
DR ChiTaRS; BC037034; mouse.
DR PRO; PR:Q3UTZ3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UTZ3; protein.
DR Bgee; ENSMUSG00000036948; Expressed in granulocyte and 81 other tissues.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR InterPro; IPR031626; TRAPPC14.
DR PANTHER; PTHR16096; PTHR16096; 1.
DR Pfam; PF15806; DUF4707; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..580
FT /note="Trafficking protein particle complex subunit 14"
FT /id="PRO_0000280345"
FT REGION 95..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVR3"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVR3"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVR3"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVR3"
FT CONFLICT 23
FT /note="A -> T (in Ref. 1; BAE23836)"
SQ SEQUENCE 580 AA; 62750 MW; A6BBBE4923699498 CRC64;
MESQCDYSMY FPAVPLPPRA ELAGDPGRYR ALPRRNHLYL GETVRFLLVL RCRGSVGAGV
GGGAGLASRG AWTELATSLA ALASVSAGGA LPGCGSAGDQ DADPPGGGDP GGGGLFRGCS
PLLTHGQGPA TSGGATTLPV EEPIVSTDEV IFPLTVSLDR LPPGTPKAKI VVTVWKREVE
APEVRDQGYL RLLQTRSPGE TFRGEQSAFK AQVSTLLTLL PPPVLKCRQF TVAGKHLTVL
KVLNSSSQEE ISIWDIRILP NFNASYLPVM PDGSVLLVDN VCHQSGEVSM GSFCRLPGTS
GYFPCPLSAL EEHNFLFQLR GGEQPPPGAK EGLEVPLIAV VQWSTPKLPF TQSIYTHYRL
PSVRLDRPCF VMTASCESPV RTYERFTVTY TLLNNLQDFL AVRLVWTPEH AQAGKQLCEE
ERRAMQAALD SIVCHTPLNN LGFSRKGSAL TFSVAFQALR TGLFELSQHM KLKLQFTASV
SHPPPEARPL SRKSSPSSPA VRDLVERHQA SLGRSQSFSH QQPSRSHLMR SGSVMERRAI
TPPVASPVGR PLYLPPDKAV LSLDKIAKRE CKVLVVEPVK
