K1C10_BOVIN
ID K1C10_BOVIN Reviewed; 526 AA.
AC P06394;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Keratin, type I cytoskeletal 10;
DE AltName: Full=Cytokeratin VIB;
DE AltName: Full=Cytokeratin-10;
DE Short=CK-10;
DE AltName: Full=Cytokeratin-6B;
DE AltName: Full=Keratin-10;
DE Short=K10;
GN Name=KRT10;
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 [GENOMIC DNA].
RX PubMed=2416562; DOI=10.1002/j.1460-2075.1985.tb03924.x;
RA Rieger M., Jorcano J.L., Franke W.W.;
RT "Complete sequence of a bovine type I cytokeratin gene: conserved and
RT variable intron positions in genes of polypeptides of the same cytokeratin
RT subfamily.";
RL EMBO J. 4:2261-2267(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-526.
RC TISSUE=Epidermis;
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: Plays a role in the establishment of the epidermal barrier on
CC plantar skin (By similarity). Involved in the maintenance of cell layer
CC development and keratin filament bundles in suprabasal cells of the
CC epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Heterodimer with KRT1 (By similarity). Two heterodimers of KRT1 and
CC KRT10 form a heterotetramer (By similarity). The KRT10 subunit in the
CC heterotetramer is probably disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P02535, ECO:0000250|UniProtKB:P13645}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P13645}. Cell surface
CC {ECO:0000250|UniProtKB:P13645}. Cytoplasm
CC {ECO:0000250|UniProtKB:P02535}.
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}.
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; X02870; CAA26626.1; -; Genomic_DNA.
DR PIR; A02941; KRBOVI.
DR RefSeq; NP_776802.1; NM_174377.1.
DR AlphaFoldDB; P06394; -.
DR SMR; P06394; -.
DR IntAct; P06394; 1.
DR STRING; 9913.ENSBTAP00000017140; -.
DR PaxDb; P06394; -.
DR PeptideAtlas; P06394; -.
DR PRIDE; P06394; -.
DR GeneID; 281888; -.
DR KEGG; bta:281888; -.
DR CTD; 3858; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; P06394; -.
DR OrthoDB; 798081at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0045684; P:positive regulation of epidermis development; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
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 PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Disulfide bond; Intermediate filament; Keratin;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..526
FT /note="Keratin, type I cytoskeletal 10"
FT /id="PRO_0000063641"
FT DOMAIN 127..441
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..126
FT /note="Head"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..162
FT /note="Coil 1A"
FT REGION 163..183
FT /note="Linker 1"
FT REGION 184..275
FT /note="Coil 1B"
FT REGION 276..298
FT /note="Linker 12"
FT REGION 299..437
FT /note="Coil 2"
FT REGION 438..526
FT /note="Tail"
FT REGION 458..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 379
FT /note="Stutter"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT DISULFID 382
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT CONFLICT 467..488
FT /note="SSGGYGGGSSSGGGHGGSSGGS -> PAAATAAEVQRWRPRRSFRRQ (in
FT Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..503
FT /note="SSGGGHGGGS -> PVAVARRRK (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 54848 MW; BF6B53C809FBDA48 CRC64;
MSVRYSSSKQ YSSSRSGGGG GGGSSLRISS SKGSLGGGYS SGGFSGGSFS RGSSAGGCFG
GSSSIYGGGL GSGFGGGYGS SFGGSYGGSF GGGYGGGGFG GGSFGGGSFG GGLGGGFGDG
GLISGNQKIT MQNLNDRLAS YLDKVRALEE SNYELEVKIK EWYEKYGNSR QREPRDYSKY
YQTIDDLKNQ IFNLTTDNAN ILIQVDNARL AADDFRLKYE NEVTLRQSVE ADINGLRRVL
DELTLTKTDL EMQIESLTEE LAYLKKNHEE EMRDLQNVST GDVNVEMNAA PGVDLTELLN
NMRSQYEQLA EKNRRDAEAW FNEKSKELTT EINSNLEQVS SHKSEITELR RTIQGLEIEL
QSQLALKQSL EASLAETEGR YCVQLSQIQS QISSLEEQLQ QIRAETECQN AEYQQLLDIK
IRLENEIQTY RSLLEGEGSS GGGSYGGGRG YGGSSGGGGG GYGGGSSSGG YGGGSSSGGG
HGGSSGGSYG GGSSSGGGHG GGSSSGGHKS TTTGSVGESS SKGPRY
