K1C14_BOVIN
ID K1C14_BOVIN Reviewed; 93 AA.
AC P05785;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Keratin, type I cytoskeletal 14;
DE AltName: Full=Cytokeratin VII;
DE AltName: Full=Cytokeratin-14;
DE Short=CK-14;
DE AltName: Full=Cytokeratin-7;
DE AltName: Full=Keratin-14;
DE Short=K14;
DE Flags: Fragment;
GN Name=KRT14;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6209405; DOI=10.1016/0022-2836(84)90468-6;
RA Jorcano J.L., Rieger M., Franz J.K., Schiller D.L., Moll R., Franke W.W.;
RT "Identification of two types of keratin polypeptides within the acidic
RT cytokeratin subfamily I.";
RL J. Mol. Biol. 179:257-281(1984).
CC -!- FUNCTION: The nonhelical tail domain is involved in promoting KRT5-
CC KRT14 filaments to self-organize into large bundles and enhances the
CC mechanical properties involved in resilience of keratin intermediate
CC filaments in vitro. {ECO:0000250|UniProtKB:P02533}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a disulfide-linked heterodimer (via 2B domains) with
CC KRT5 (via 2B domains) (By similarity). Forms a heterodimer with KRT1;
CC the interaction is more abundant in the absence of KRT5 (By
CC similarity). Interacts with TRADD and with keratin filaments (By
CC similarity). Associates with other type I keratins (By similarity).
CC Interacts with EPPK1 (By similarity). Interacts with KLHL24 (By
CC similarity). {ECO:0000250|UniProtKB:P02533,
CC ECO:0000250|UniProtKB:Q61781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02533}. Nucleus
CC {ECO:0000250|UniProtKB:P02533}. Note=Expressed in both as a filamentous
CC pattern. {ECO:0000250|UniProtKB:P02533}.
CC -!- PTM: A disulfide bond is formed between rather than within filaments
CC and promotes the formation of a keratin filament cage around the
CC nucleus. {ECO:0000250|UniProtKB:Q61781}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:P02533}.
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X01461; CAA25695.1; -; mRNA.
DR PIR; S08613; S08613.
DR AlphaFoldDB; P05785; -.
DR SMR; P05785; -.
DR STRING; 9913.ENSBTAP00000036252; -.
DR PaxDb; P05785; -.
DR PeptideAtlas; P05785; -.
DR PRIDE; P05785; -.
DR eggNOG; ENOG502R8V7; Eukaryota.
DR InParanoid; P05785; -.
DR OrthoDB; 798081at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045110; P:intermediate filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Disulfide bond; Intermediate filament; Keratin;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN <1..93
FT /note="Keratin, type I cytoskeletal 14"
FT /id="PRO_0000063652"
FT DOMAIN <1..48
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..44
FT /note="Coil 2"
FT REGION 45..93
FT /note="Tail"
FT REGION 47..93
FT /note="Interaction with Type I keratins and keratin
FT filaments"
FT /evidence="ECO:0000250"
FT REGION 47..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61781"
FT NON_TER 1
SQ SEQUENCE 93 AA; 10722 MW; 70A999BB0A6B103A CRC64;
SVEEQLAQLR CEMEQQNQEY KILLDVKTRL EQEIATYRRL LEGEDAHLSS SQFSSGSQSS
RDVSSSRQVR TKVVDVHDGK VVFTHEQIVR TKN
