K1C27_BOVIN
ID K1C27_BOVIN Reviewed; 460 AA.
AC Q0P5J6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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;
GN Name=KRT27 {ECO:0000250|UniProtKB:Q7Z3Y8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI19955.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI19955.1};
RC TISSUE=Fetal skin {ECO:0000312|EMBL:AAI19955.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC119954; AAI19955.1; -; mRNA.
DR RefSeq; NP_001069283.1; NM_001075815.1.
DR AlphaFoldDB; Q0P5J6; -.
DR SMR; Q0P5J6; -.
DR STRING; 9913.ENSBTAP00000040718; -.
DR PaxDb; Q0P5J6; -.
DR PRIDE; Q0P5J6; -.
DR Ensembl; ENSBTAT00000043127; ENSBTAP00000040718; ENSBTAG00000030548.
DR GeneID; 521074; -.
DR KEGG; bta:521074; -.
DR CTD; 342574; -.
DR VEuPathDB; HostDB:ENSBTAG00000030548; -.
DR VGNC; VGNC:30726; KRT27.
DR eggNOG; ENOG502SIHJ; Eukaryota.
DR GeneTree; ENSGT00940000161982; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q0P5J6; -.
DR OMA; SRVHTME; -.
DR OrthoDB; 805081at2759; -.
DR TreeFam; TF332742; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030548; Expressed in zone of skin and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031069; P:hair follicle morphogenesis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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_0000312699"
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 435..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 49907 MW; BB708B550A52C76A CRC64;
MSVRFSSASR RLGSCGGAGS VRLSGGGAGF 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
RNELTEMKRN LQTLEIELQS LLATKHSLEC SLTETEGNYC AQLAQIQAQI GALEEQLHQV
RTETEGQKLE YEQLLDIKVH LEKEIETYCR LIDGEDGSCA KSKGYGGPGH QIKDPSKATV
VKTIVEEIDP RGKVLSSRVH SVEEKSTKVN NVKSEQRVPS