TCHP_MOUSE
ID TCHP_MOUSE Reviewed; 497 AA.
AC Q3TVW5; Q80ZV6; Q8C459; Q9CTP0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Trichoplein keratin filament-binding protein;
DE Short=Protein TCHP;
DE AltName: Full=Mitochondrial protein with oncostatic activity;
DE Short=Mitostatin;
GN Name=Tchp {ECO:0000312|MGI:MGI:1925082};
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] {ECO:0000305, ECO:0000312|EMBL:BAE35503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE35503.1};
RC TISSUE=Embryonic spinal cord {ECO:0000312|EMBL:BAC38735.1},
RC Osteoclast {ECO:0000312|EMBL:BAE35503.1}, and
RC Retina {ECO:0000312|EMBL:BAB32251.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH43048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 229-497 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH43048.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH43048.1}, and
RC Retina {ECO:0000312|EMBL:AAH47930.1};
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 TISSUE SPECIFICITY.
RX PubMed=15731013; DOI=10.1242/jcs.01667;
RA Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
RA Usukura J., Inagaki M.;
RT "Identification of trichoplein, a novel keratin filament-binding protein.";
RL J. Cell Sci. 118:1081-1090(2005).
CC -!- FUNCTION: Tumor suppressor which has the ability to inhibit cell growth
CC and be pro-apoptotic during cell stress. May act as a 'capping' or
CC 'branching' protein for keratin filaments in the cell periphery. May
CC regulate K8/K18 filament and desmosome organization mainly at the
CC apical or peripheral regions of simple epithelial cells (By
CC similarity). Is a negative regulator of ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9BT92}.
CC -!- SUBUNIT: Interacts specifically with keratin proteins including, KRT5,
CC KRT6A, KRT8, KRT14, KRT16 and KRT18. Interacts with KCTD17 (By
CC similarity). {ECO:0000250|UniProtKB:Q9BT92}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Mitochondrion
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3TVW5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3TVW5-2; Sequence=VSP_052475;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including brain,
CC liver, small intestine, large intestine, lung and heart. Found
CC concentrated in tubular structures within hepatocytes, and in the
CC apical cortical region and desmosomes of the apical junctional domain
CC in enterocytes of the small intestine. In the hair follicle, localized
CC at the outer root sheath. Also expressed in blood vessels (at protein
CC level). {ECO:0000269|PubMed:15731013}.
CC -!- PTM: Ubiquitinated. Ubiquitination by the BCR(KCTD17) E3 ubiquitin
CC ligase complex results in proteasomal degradation, and induces
CC ciliogenesis. {ECO:0000250|UniProtKB:Q9BT92}.
CC -!- SIMILARITY: Belongs to the TCHP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK020912; BAB32251.1; -; mRNA.
DR EMBL; AK083027; BAC38735.1; -; mRNA.
DR EMBL; AK159947; BAE35503.1; -; mRNA.
DR EMBL; BC043048; AAH43048.1; -; mRNA.
DR EMBL; BC047930; AAH47930.1; ALT_INIT; mRNA.
DR CCDS; CCDS51624.1; -. [Q3TVW5-1]
DR RefSeq; NP_084268.2; NM_029992.2. [Q3TVW5-1]
DR RefSeq; XP_006530573.1; XM_006530510.3.
DR AlphaFoldDB; Q3TVW5; -.
DR SMR; Q3TVW5; -.
DR BioGRID; 218956; 4.
DR IntAct; Q3TVW5; 1.
DR MINT; Q3TVW5; -.
DR STRING; 10090.ENSMUSP00000092009; -.
DR iPTMnet; Q3TVW5; -.
DR PhosphoSitePlus; Q3TVW5; -.
DR EPD; Q3TVW5; -.
DR MaxQB; Q3TVW5; -.
DR PaxDb; Q3TVW5; -.
DR PRIDE; Q3TVW5; -.
DR ProteomicsDB; 263023; -. [Q3TVW5-1]
DR ProteomicsDB; 263024; -. [Q3TVW5-2]
DR Ensembl; ENSMUST00000094441; ENSMUSP00000092009; ENSMUSG00000002486. [Q3TVW5-1]
DR GeneID; 77832; -.
DR KEGG; mmu:77832; -.
DR UCSC; uc008yzx.1; mouse. [Q3TVW5-1]
DR CTD; 84260; -.
DR MGI; MGI:1925082; Tchp.
DR VEuPathDB; HostDB:ENSMUSG00000002486; -.
DR eggNOG; ENOG502QVSH; Eukaryota.
DR GeneTree; ENSGT01010000222818; -.
DR HOGENOM; CLU_042533_1_0_1; -.
DR InParanoid; Q3TVW5; -.
DR OMA; QNSHYFR; -.
DR OrthoDB; 675049at2759; -.
DR PhylomeDB; Q3TVW5; -.
DR TreeFam; TF329032; -.
DR BioGRID-ORCS; 77832; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q3TVW5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3TVW5; protein.
DR Bgee; ENSMUSG00000002486; Expressed in spermatocyte and 168 other tissues.
DR ExpressionAtlas; Q3TVW5; baseline and differential.
DR Genevisible; Q3TVW5; MM.
DR GO; GO:0045179; C:apical cortex; ISS:HGNC-UCL.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030057; C:desmosome; IDA:MGI.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR InterPro; IPR043596; CFAP53/TCHP.
DR InterPro; IPR026773; TCHP.
DR InterPro; IPR043597; TPH_dom.
DR PANTHER; PTHR31183; PTHR31183; 1.
DR PANTHER; PTHR31183:SF2; PTHR31183:SF2; 1.
DR Pfam; PF13868; TPH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Mitochondrion; Reference proteome; Tumor suppressor;
KW Ubl conjugation.
FT CHAIN 1..497
FT /note="Trichoplein keratin filament-binding protein"
FT /id="PRO_0000292610"
FT REGION 72..457
FT /note="Interaction with keratin proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT REGION 167..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..424
FT /note="Trichohyalin/plectin homology domain"
FT /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT REGION 441..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..140
FT /evidence="ECO:0000255"
FT COILED 166..271
FT /evidence="ECO:0000255"
FT COILED 327..479
FT /evidence="ECO:0000255"
FT COMPBIAS 482..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 441..497
FT /note="AERQGQEWEAARQEEEEEEEARQAEEHSNALLQQEAKTMAEKGYQPKLHGHL
FT RIAWD -> GPKGKGGLAGHYRTELGRGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052475"
FT CONFLICT 109
FT /note="G -> S (in Ref. 1; BAE35503)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..232
FT /note="KEME -> LWVS (in Ref. 2; AAH47930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 60642 MW; E6731294EA6E1CD7 CRC64;
MALPTLPSYW SSRKHMDLRQ RQHQQEDQFR QQWEQNSRYF RTWDIHNSKQ IEWSSKISYQ
RSMHAYHCEK MKEEKRKILE LRRERLRELL LEEQDLLAAE LDELRLSMGL REQRLREQHQ
DLKSAREEQR KLIAERLLYE HWKKNNPKLR ELELDLHKKH VINSWATQKE EKKQQEATEK
QENKRLENQY AAARREAEAR MRVEEERRQL EGRLQAEALR QQMEELKQKE MEATKLKKEQ
ENLLRQRWEL ERLEEERRQM AALRRKTELG RFLKHQYNAQ LNRRTQEIQE ELEVDGRILQ
ALLEKEGELQ QVELARREQA RADAAWMKQV IEEQLQLEKA REAELQQLLR EEAKEMWEKR
EAEWAREQVA RDRLMSEVLT GRQQQILEKI EQNRRAQEET LKHREKLIRS LEEGKQLAQR
AKEESEELKL ARKQELEAQV AERQGQEWEA ARQEEEEEEE ARQAEEHSNA LLQQEAKTMA
EKGYQPKLHG HLRIAWD
