ID   TCHP_DANRE              Reviewed;         499 AA.
AC   Q1RM03; Q502P3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Trichoplein keratin filament-binding protein;
DE            Short=Protein TCHP;
GN   Name=tchp {ECO:0000312|EMBL:AAI15205.1,
GN   ECO:0000312|ZFIN:ZDB-GENE-060421-3368}; ORFNames=zgc:136634;
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] {ECO:0000312|EMBL:CAM15569.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larva {ECO:0000312|EMBL:AAH95618.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a 'capping' or 'branching' protein for keratin
CC       filaments in the cell periphery. May regulate K8/K18 filament and
CC       desmosome organization mainly at the apical or peripheral regions of
CC       simple epithelial cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BT92}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCHP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH95618.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 264.; Evidence={ECO:0000305};
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DR   EMBL; BX323811; CAM15569.1; -; Genomic_DNA.
DR   EMBL; BC095618; AAH95618.1; ALT_SEQ; mRNA.
DR   EMBL; BC115204; AAI15205.1; -; mRNA.
DR   RefSeq; NP_001035433.1; NM_001040343.1.
DR   AlphaFoldDB; Q1RM03; -.
DR   SMR; Q1RM03; -.
DR   STRING; 7955.ENSDARP00000051613; -.
DR   PaxDb; Q1RM03; -.
DR   PRIDE; Q1RM03; -.
DR   Ensembl; ENSDART00000051614; ENSDARP00000051613; ENSDARG00000035605.
DR   GeneID; 678595; -.
DR   KEGG; dre:678595; -.
DR   CTD; 84260; -.
DR   ZFIN; ZDB-GENE-060421-3368; tchp.
DR   eggNOG; ENOG502QVSH; Eukaryota.
DR   GeneTree; ENSGT01050000245079; -.
DR   HOGENOM; CLU_042533_1_0_1; -.
DR   InParanoid; Q1RM03; -.
DR   OMA; QNSHYFR; -.
DR   OrthoDB; 675049at2759; -.
DR   PhylomeDB; Q1RM03; -.
DR   TreeFam; TF329032; -.
DR   PRO; PR:Q1RM03; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000035605; Expressed in testis and 20 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
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   Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..499
FT                   /note="Trichoplein keratin filament-binding protein"
FT                   /id="PRO_0000292612"
FT   REGION          46..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..499
FT                   /note="Interaction with keratin proteins"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT   REGION          169..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..426
FT                   /note="Trichohyalin/plectin homology domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT92"
FT   COILED          12..38
FT                   /evidence="ECO:0000255"
FT   COILED          71..133
FT                   /evidence="ECO:0000255"
FT   COILED          168..306
FT                   /evidence="ECO:0000255"
FT   COILED          359..484
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        46..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        261..263
FT                   /note="MME -> ISD (in Ref. 2; AAH95618)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  62351 MW;  49B2771596B68D5B CRC64;
     MALPTLSAHW PSRVRTLEQQ LVRQREQEAR LRRQWEQHSQ YFREQDVRSS KQAQWSSRQS
     FHRSMSAFQR DRMREEKQRK LEERRERLRT MLQEERDQLE AELRNIHPDR DTLARQLVEK
     TDALRSAREE RRKNLAQELL REHWKQNNSQ LRKVESELHK DHIVSQWQVQ QQEKKQADER
     TQEEKQRFEN EYERTRQEAL ERMRKEEENR KWEEKKRAEE LLKQMEELKL REQEAERLKQ
     EQETLMSKRW ELEKLEDERK MMEESRRKTE FGRFLTRQYR AQLKRRAQQV QEELEADRKI
     LAALLEGELD EQRFHKARRE RAVADAAWMK RVIEEQLQLE REREAEFDIL YREEAQRVWE
     KREAEWEKER RARERLMREV LAGRQQQLQE RMQENRLARE ESLQRREELL QQLEQDRLTL
     RLEKEQQEGL RTARIQEIDN QVEQRRKEQW EQQQTLEQEE AQEREELRLQ EEELRLETDR
     MIRQGFQERI HSRPRSAWT