TPC12_MOUSE
ID TPC12_MOUSE Reviewed; 797 AA.
AC Q8K2L8; E9QLQ6; Q8BX27;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Trafficking protein particle complex subunit 12 {ECO:0000305};
DE AltName: Full=Tetratricopeptide repeat protein 15 {ECO:0000250|UniProtKB:Q8WVT3};
DE Short=TPR repeat protein 15 {ECO:0000250|UniProtKB:Q8WVT3};
GN Name=Trappc12 {ECO:0000312|MGI:MGI:2445089};
GN Synonyms=Ttc15 {ECO:0000250|UniProtKB:Q8WVT3};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-797.
RC STRAIN=C57BL/6J;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; THR-130 AND
RP SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; THR-130;
RP SER-309 AND SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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: Component of the TRAPP complex, which is involved in
CC endoplasmic reticulum to Golgi apparatus trafficking at a very early
CC stage. Also plays a role in chromosome congression, kinetochore
CC assembly and stability and controls the recruitment of CENPE to the
CC kinetochores. {ECO:0000250|UniProtKB:Q8WVT3}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12. Interacts with CENPE. {ECO:0000250|UniProtKB:Q8WVT3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000250|UniProtKB:Q8WVT3}. Nucleus
CC {ECO:0000250|UniProtKB:Q8WVT3}. Note=Mainly localizes to structures
CC resembling the Golgi and a small amount is found in the nucleus.
CC {ECO:0000250|UniProtKB:Q8WVT3}.
CC -!- PTM: Phosphorylated as the cells enter mitosis but is dephosphorylated
CC at or before the onset of anaphase. The phosphorylated form recruits
CC CENPE to kinetochores more efficiently than the non-phosphorylated
CC form. {ECO:0000250|UniProtKB:Q8WVT3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33585.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC136986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024077; AAH24077.1; -; mRNA.
DR EMBL; BC030887; AAH30887.1; -; mRNA.
DR EMBL; AK049172; BAC33585.1; ALT_INIT; mRNA.
DR CCDS; CCDS25854.1; -.
DR RefSeq; NP_001154882.1; NM_001161410.1.
DR RefSeq; NP_848926.3; NM_178811.4.
DR AlphaFoldDB; Q8K2L8; -.
DR SMR; Q8K2L8; -.
DR BioGRID; 229916; 13.
DR ComplexPortal; CPX-4766; TRAPP III complex.
DR STRING; 10090.ENSMUSP00000020954; -.
DR iPTMnet; Q8K2L8; -.
DR PhosphoSitePlus; Q8K2L8; -.
DR EPD; Q8K2L8; -.
DR jPOST; Q8K2L8; -.
DR MaxQB; Q8K2L8; -.
DR PaxDb; Q8K2L8; -.
DR PeptideAtlas; Q8K2L8; -.
DR PRIDE; Q8K2L8; -.
DR ProteomicsDB; 258821; -.
DR Antibodypedia; 26298; 68 antibodies from 15 providers.
DR Ensembl; ENSMUST00000020954; ENSMUSP00000020954; ENSMUSG00000020628.
DR Ensembl; ENSMUST00000168129; ENSMUSP00000127752; ENSMUSG00000020628.
DR GeneID; 217449; -.
DR KEGG; mmu:217449; -.
DR UCSC; uc007nfw.2; mouse.
DR CTD; 51112; -.
DR MGI; MGI:2445089; Trappc12.
DR VEuPathDB; HostDB:ENSMUSG00000020628; -.
DR eggNOG; KOG2796; Eukaryota.
DR GeneTree; ENSGT00390000002448; -.
DR HOGENOM; CLU_014917_0_0_1; -.
DR InParanoid; Q8K2L8; -.
DR OMA; FNAQCLK; -.
DR OrthoDB; 1142416at2759; -.
DR PhylomeDB; Q8K2L8; -.
DR TreeFam; TF320881; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 217449; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Trappc12; mouse.
DR PRO; PR:Q8K2L8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K2L8; protein.
DR Bgee; ENSMUSG00000020628; Expressed in rostral migratory stream and 230 other tissues.
DR ExpressionAtlas; Q8K2L8; baseline and differential.
DR Genevisible; Q8K2L8; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030008; C:TRAPP complex; ISO:MGI.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0048208; P:COPII vesicle coating; IC:ComplexPortal.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; ISS:UniProtKB.
DR GO; GO:0090234; P:regulation of kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW ER-Golgi transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transport.
FT CHAIN 1..797
FT /note="Trafficking protein particle complex subunit 12"
FT /id="PRO_0000106402"
FT REPEAT 607..640
FT /note="TPR 1"
FT REPEAT 642..675
FT /note="TPR 2"
FT REPEAT 682..715
FT /note="TPR 3"
FT REPEAT 716..749
FT /note="TPR 4"
FT REGION 1..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVT3"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 241
FT /note="T -> M (in Ref. 2; AAH24077/AAH30887)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="V -> I (in Ref. 3; BAC33585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 797 AA; 87694 MW; C384660A9BB7E5FA CRC64;
METAKDGEQS PSEASPSAQA GPENIPEPMS REEESQPLYH EETIDLGGDE FASEENEPTS
EGSHNFGDKL NEHMMESVLI SDSPNNSEGD VGDLGCLQDV GEPPRGATDH RLPSSTDKEV
VDTLSNGSET DGDDTPRDIS DMTPDSRASL KEDSTQEDVT SMPALENAAT EEVGPKDSLA
PREEQTSEVS SNQSSSKDEP LPVCTIFSQA TATPSQPHLF LQDGFESQMV KSPSFSSTSE
TSAKTPPPMV QPSPSLSTFF GDTMSSNSLA SDFFDSFTTS TFISVSNPNA GSPVPEKLSS
LTAPVGEKSP DSTSPSYSTR MDRSESGVSR APLDVPESPK PFSQIQAVFA GSDDPFATAL
SMSEMDRRND AWLPSQATRE VLMSVATQQY GTVFIDKENL TMPGLKFDNI QGDAVKDLML
RFLGEKAAAK RQVLNASSVE QSFVGLKQLI SCRNWRAAVD LCGRLLTAHG QGYGKNGLPT
SHTTDSLQLW FVRLALLVKL GLFQNAEMEF EPFGNLDQPD LYYEYYPHVY PGRRGSMVPF
SMRILHAELQ QYLGNPQESL DRLHRVKTVC SKILANLEQG LAEDGGLSSV TQESRQASVQ
LWRSRLGRVL YSMANCLLLM KDYVLAVDAY LTVIKYYPEQ EPQLLSGIGR ILLQIGDIKT
AEKYFQDVEK VTQKLDGLQG KIMVLMNRAF LYLGQNNFAE AHKFFTEILR MDPTNAVANN
NAAVCLLYLG KLKDSLRQLE AMVQQDPRHY LHESVLFNLT TMYELESSRS MQKKQSLLEA
VASKEGDSFN TQCLKLA
