K1C15_SHEEP
ID K1C15_SHEEP Reviewed; 453 AA.
AC O77727;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Keratin, type I cytoskeletal 15;
DE AltName: Full=Cytokeratin-15;
DE Short=CK-15;
DE AltName: Full=Keratin-15;
DE Short=K15;
GN Name=KRT15 {ECO:0000312|EMBL:CAA06944.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA06944.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Spleen {ECO:0000312|EMBL:CAA06944.1};
RX PubMed=9806795; DOI=10.1006/excr.1998.4217;
RA Whitbread L.A., Powell B.C.;
RT "Expression of the intermediate filament keratin gene, K15, in the basal
RT cell layers of epithelia and the hair follicle.";
RL Exp. Cell Res. 244:448-459(1998).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with NOD2 (By similarity). {ECO:0000250|UniProtKB:P19012,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the basal cell layers of several
CC stratified epithelia including esophagus, tongue, stomach, epidermis
CC and hair follicle. In the hair follicle, expression is detected mainly
CC in the basal layer of the outer root sheath (ORS), except just above
CC the follicle bulb where it occurs throughout its thickness. Low
CC expression levels are seen in the single layer of ORS cells around the
CC base of the follicle which increases in the palisade-like cells of the
CC bulb. Also expressed in the basal cells of the sebaceous glands, and
CC expression in the epidermis occurs in a punctate pattern.
CC {ECO:0000269|PubMed:9806795}.
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; AJ006277; CAA06944.1; -; Genomic_DNA.
DR AlphaFoldDB; O77727; -.
DR SMR; O77727; -.
DR STRING; 9940.ENSOARP00000018244; -.
DR PRIDE; O77727; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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; Intermediate filament; Isopeptide bond; Keratin;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..453
FT /note="Keratin, type I cytoskeletal 15"
FT /id="PRO_0000063660"
FT DOMAIN 103..415
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..102
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 103..138
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 139..157
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 158..249
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 250..269
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 270..411
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 412..453
FT /note="Tail"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61414"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFV3"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04695"
SQ SEQUENCE 453 AA; 48770 MW; E90D5239DA45015A CRC64;
MATTLLQTSS STFGGSSTRG GSLLAGGGGF GGGSLYGGGG SRTISASSAR FVSSGSAGGY
GGGFGGGAGS GYGGGFGGGF GGGFGSGFGD FGGGDGGLLS GNEKITMQNL NDRLASYLEK
VRALEEANAD LEVKIRDWYQ RQSPTSPERD YSPYFKTTDE LRDKILAAAI DNSRVILEID
NARLAADDFR LKYENEMALR QSVEADINGL RRVLDELTLT KTDLEMQIES LNEELAYLKK
NHEEEMKEFS NQLAGQVNVE MDAAPGVDLT RVLSEMREQY EAMAEKNRRD AEAWFFSKTE
ELNKEVASNT EMIQTSKSEI TDLRRTIQGL EIELQSQLSM KAGLESTLAE TDGRYAAQLQ
QIQGLISSIE AQLSELRSEM EAQNQEYKML LDIKTRLEQE IATYHSLLEG QDARMAGIGT
GEASLGGGGG GKVRINVEES VDGKVVSSRK REI
