K1C9_CANLF
ID K1C9_CANLF Reviewed; 786 AA.
AC O18740;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Keratin, type I cytoskeletal 9;
DE AltName: Full=Cytokeratin-9;
DE Short=CK-9;
DE AltName: Full=Keratin-9;
DE Short=K9;
GN Name=KRT9 {ECO:0000312|EMBL:AAC26971.1};
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:AAC26971.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-308.
RX PubMed=9720175; DOI=10.1046/j.1365-2052.1998.00297.x;
RA Lachaume P., Hitte C., Jouquand S., Priat C., Galibert F.;
RT "Identification and analysis of the dog keratin 9 (KRT9) gene.";
RL Anim. Genet. 29:173-177(1998).
CC -!- FUNCTION: May serve an important special function either in the mature
CC palmar and plantar skin tissue or in the morphogenetic program of the
CC formation of these tissues. Plays a role in keratin filament assembly
CC (By similarity). {ECO:0000250|UniProtKB:P35527}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively). {ECO:0000305}.
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; AF000949; AAC26971.1; -; Genomic_DNA.
DR AlphaFoldDB; O18740; -.
DR SMR; O18740; -.
DR STRING; 9615.ENSCAFP00000039054; -.
DR PaxDb; O18740; -.
DR PRIDE; O18740; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; O18740; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; ISS:UniProtKB.
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 3: Inferred from homology;
KW Coiled coil; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..786
FT /note="Keratin, type I cytoskeletal 9"
FT /id="PRO_0000308371"
FT DOMAIN 137..449
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..136
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..172
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 173..191
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 192..283
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 284..306
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 307..445
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 446..760
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 447..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT VARIANT 308
FT /note="N -> G"
FT /evidence="ECO:0000269|PubMed:9720175"
SQ SEQUENCE 786 AA; 76354 MW; 272AB5425DD09535 CRC64;
MNCRQFLSSH CSRDSSGGGG GSKMFSCNRS SFSGASGGGG RFSSSRSFGG GSSGACGRGG
GGSFGSSYGG GSGGGFSAGS FGGHSRGFSG GSGGGFGGGF GGGFGGFSGG SGGGFGGPGG
FGSGFDSGAG GILGADEKTT MQDLNSRLAS YLDKVQALED ANKELESKIR EWYDKQGSRT
FHRDYSPYYD TIEDLKNQIV NITADNNKTL LDLDNTRMTL DDIRMKCDIE NNLRLAVNAD
INGLRKVLDD LTMQKSDLEM HYESLQEELI ALKKNHEDEM SQLTGQNSGD VNVEMNAAPG
RDLTKILNDM REEYERISAK NRKDIEEQYE TQMSQMEQEV MSSGQEMESN HKEVTQLRHS
IQEMEIELQS QLSKKSALEK SLEDTKNHYC GQLQQLQEQI RSLEGQITEI RGEIECQNQE
YSLLLNIKTR LEQEIKTYRS LLEGGQEDFE SHESGQSHFG SGGSRQQGGI GGSHGRGSRG
GSGGSYGGGS SSGGGSGGSH GGGSGGSYGG GSSSGGGSGG RGGSGGSYGG GSGSGGGSSG
SYGGGSSSGG GSGGSHGGGS GGSYGGGSSS GGGSGGRGGS GGSYGGGSGS GGGRGGGCEE
GSGSGGRSGG SYGGGSGSGG GSSCSYGGGS SSGGGSGGSY GGGSSSGGGS GGKGGSGCSY
SGGSSSGGGS GGSYGGGSSS GRGSGGRGGS AGSYGGGSGS GGGRGGGCEE GSGSGGRSGG
SYGGGSGSGG RSGGSYGGGS GSGGGSGGSY GGGSGSKGGS GRSSQVQSSS SKSGECDDTQ
GYHIQY
