ID   K1C27_CAPHI             Reviewed;         460 AA.
AC   Q6R649;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Keratin, type I cytoskeletal 27;
DE   AltName: Full=Cytokeratin-27;
DE            Short=CK-27;
DE   AltName: Full=Keratin-27;
DE            Short=K27;
DE   AltName: Full=Type I inner root sheath-specific keratin-K25irs3;
DE   AltName: Full=Type I keratin intermediate filament C29;
GN   Name=KRT27 {ECO:0000250|UniProtKB:Q7Z3Y8};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1] {ECO:0000312|EMBL:AAS00519.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yin J., Li J.Q., Zhou H.M.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for the proper assembly of type I and type II
CC       keratin protein complexes and formation of keratin intermediate
CC       filaments in the inner root sheath (irs).
CC       {ECO:0000250|UniProtKB:Q9Z320}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Interacts with KRT6A to form filaments (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Z320, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z320}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AY510112; AAS00519.1; -; mRNA.
DR   RefSeq; NP_001272648.1; NM_001285719.1.
DR   AlphaFoldDB; Q6R649; -.
DR   SMR; Q6R649; -.
DR   STRING; 9925.ENSCHIP00000029335; -.
DR   PRIDE; Q6R649; -.
DR   GeneID; 100861382; -.
DR   KEGG; chx:100861382; -.
DR   CTD; 342574; -.
DR   OrthoDB; 805081at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..460
FT                   /note="Keratin, type I cytoskeletal 27"
FT                   /id="PRO_0000312700"
FT   DOMAIN          84..399
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..83
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          84..119
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          120..141
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          142..233
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          234..256
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          257..395
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          396..460
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          429..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  49961 MW;  66AAB9DC7D07DE85 CRC64;
     MSVRFSSASR RLGSCGGAGS VRLSSGGAGF GVGSTGSVPG FGSGFTCAFG GSSSAGSYSG
     GLGGGSASCT AFTGNEHGLL SGNEKVTMQN LNDRLASYLD NVRALEEANA DLEQKIKGWY
     EKFGPGSCRG LDHDYSRYFT VIDDLRNQII SATTSNANIV LQNDNARLTA DDFRLKFENE
     QALHQSVDAD VSSLRRVLDE LTLCRTDLEI QLETLSEELA YLKKNHEEEM KALQCAAGGN
     VNVEMNAAPG VDLTVLLNNM RAEYEALAEQ NRRDAEAWFN EKSASLQQQI SDDAGATTSA
     RNELTEMKRT LQTLEIELQS LLATKHSLEC SLTETEGNYC AQLAQIQAQI GALEEQLHQV
     RTETEGQKLE YEQLLDIKVH LEKEIETYCR LIDGEDGSCT KSKGYGGPGN QIKDPSKATV
     VKTIVEEIDP RGKVPSSRVH TVEEKSTKVN NMKSEQRVPS