ID   TCHP_PONAB              Reviewed;         498 AA.
AC   Q5RE49;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
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:0000250|UniProtKB:Q9BT92};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH89958.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:CAH89958.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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, 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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR857688; CAH89958.1; -; mRNA.
DR   RefSeq; NP_001124920.1; NM_001131448.1.
DR   AlphaFoldDB; Q5RE49; -.
DR   SMR; Q5RE49; -.
DR   STRING; 9601.ENSPPYP00000005637; -.
DR   PRIDE; Q5RE49; -.
DR   GeneID; 100171790; -.
DR   KEGG; pon:100171790; -.
DR   CTD; 84260; -.
DR   eggNOG; ENOG502QVSH; Eukaryota.
DR   InParanoid; Q5RE49; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Apoptosis; Cell membrane; Cilium biogenesis/degradation; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Membrane; Mitochondrion; Reference proteome;
KW   Tumor suppressor; Ubl conjugation.
FT   CHAIN           1..498
FT                   /note="Trichoplein keratin filament-binding protein"
FT                   /id="PRO_0000292611"
FT   REGION          73..498
FT                   /note="Interaction with keratin proteins"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT   REGION          168..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..425
FT                   /note="Trichohyalin/plectin homology domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT   REGION          386..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..39
FT                   /evidence="ECO:0000255"
FT   COILED          66..353
FT                   /evidence="ECO:0000255"
FT   COILED          380..479
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        389..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  61170 MW;  236B7C8520C4191A CRC64;
     MALPTLPFYW CSQQRLNQQL ARQREQEARL RQQWEQNSRY FRMSDICSSK QAEWSSKTSY
     QRSMHAYQRE KMKEEKRRSL EARREKLRQL MREEQDLLAR ELEELRLSMN LQERRIREQH
     RKLKSAREEQ RKLIAEQLLY EHWKKNNPKL REMELDLHQK HVINSWETQK EEKKQQEATA
     EEENKRYENE YERAQREALE RMKAEEERRQ LEDKLQAEAL LQQMEELKLK EVEATKLKKE
     QENLLKQRWE LERLEEERKQ MEAFRQKAEL GRFLRHQYNA QLNRRTQQIQ EELEADRRIL
     QALLEKEDES QRLHLARREQ VIADAAWMKQ AIEEQLQLER AREAELQMLL REEAKEMWEK
     REAEWARERS ARDRLMSEVL TGRQQQIQEK IEQNRRAQEE SLKHREQLIR NLEEARESAR
     REKEENEELK SARKQELEAQ VAERQLQAWE ADQQEKEEEE EARRVEQLSD ALLQQEAETM
     AEQGYRPKPY GHPKIAWN