K1C10_CANLF
ID K1C10_CANLF Reviewed; 568 AA.
AC Q6EIZ0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Keratin, type I cytoskeletal 10;
DE AltName: Full=Cytokeratin-10;
DE Short=CK-10;
DE AltName: Full=Epithelial keratin-10;
DE AltName: Full=Keratin-10;
DE Short=K10;
GN Name=KRT10 {ECO:0000303|PubMed:16147859};
GN Synonyms=KER10 {ECO:0000312|EMBL:AAQ83909.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ83909.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Blood {ECO:0000269|PubMed:16147859};
RX PubMed=16147859; DOI=10.1080/10425170500069932;
RA Minor J., Dunstan R., Guyon R., Andre C., Barnhart K., Credille K.;
RT "Comparative sequence analysis and radiation hybrid mapping of the canine
RT keratin 10 gene.";
RL DNA Seq. 16:89-95(2005).
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 -!- TISSUE SPECIFICITY: Expressed in skin. {ECO:0000269|PubMed:16147859}.
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; AY318944; AAQ83909.1; -; Genomic_DNA.
DR RefSeq; XP_013972065.1; XM_014116590.1.
DR AlphaFoldDB; Q6EIZ0; -.
DR SMR; Q6EIZ0; -.
DR STRING; 9615.ENSCAFP00000023577; -.
DR PaxDb; Q6EIZ0; -.
DR PRIDE; Q6EIZ0; -.
DR Ensembl; ENSCAFT00000025391; ENSCAFP00000023577; ENSCAFG00000016007.
DR Ensembl; ENSCAFT00030031038; ENSCAFP00030027077; ENSCAFG00030016765.
DR GeneID; 491006; -.
DR CTD; 3858; -.
DR VGNC; VGNC:42516; KRT10.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q6EIZ0; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
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:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR GO; GO:0018149; P:peptide cross-linking; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Disulfide bond; Intermediate filament; Keratin;
KW Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..568
FT /note="Keratin, type I cytoskeletal 10"
FT /id="PRO_0000257990"
FT DOMAIN 136..450
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..135
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..171
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 172..192
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 193..284
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 285..307
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 308..446
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 447..568
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 485..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT DISULFID 391
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P13645"
SQ SEQUENCE 568 AA; 57711 MW; 91CA555D41CE62CF CRC64;
MSVRYSSSKQ YSSSRSGGGG GGGGGSSFRI SSSKGSIGGG FSSGGFSGGS FSRGSSGGGC
FGGSSGGYGG LGGGFGGGNF GGGYGSSSFG GGYGGVSFGG GSFGGGSFGG GGFSGGSFGG
YGGGYGGDGG LLSGNEKVTM QNLNDRLASY LDKVRALEES NYELEGKIKE WYEKHGNSSQ
RAPRDYSKYY QTIEDLKNQI LNLTTDNANI LLQIDNARLA ADDFRLKYEN EVALRQSVEA
DINGLRRVLD ELTLTKADLE MQIESLTEEL AYLKKNHEEE MRDLQNVSTG DVNVEMNAAP
GVDLTELLNN MRNQYEQLAE QNRKDAEAWF NEKSKELTTE INSNIEQMSS HKSEITELRR
TVQGLEIELQ SQLALKQSLE GSLAETEGRY CVQLSQIQAQ ISSLEEQLQQ IRAETECQNA
EYQQLLDIKI RLENEIQTYR SLLEGEGSSG GGGYGGGRGG GSSGGGYGGS SGGGYGGSSG
GGGYGGGSSG GGGHIGGHSG GHSGSSGGGY GGGSSSGGGG YGGGSSGGGG SHGGSSGGGY
GGGSSSSGGH KSSSSGSVGE SSSKGPRY
