K1C25_BOVIN
ID K1C25_BOVIN Reviewed; 450 AA.
AC Q0P5J4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Keratin, type I cytoskeletal 25;
DE AltName: Full=Cytokeratin-25;
DE Short=CK-25;
DE AltName: Full=Keratin-25;
DE Short=K25;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs1;
GN Name=KRT25 {ECO:0000250|UniProtKB:Q7Z3Z0};
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] {ECO:0000312|EMBL:AAI19959.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI19959.1};
RC TISSUE=Fetal skin {ECO:0000312|EMBL:AAI19959.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the proper assembly of type I and type II
CC keratin protein complexes and formation of keratin intermediate
CC filaments in the inner root sheath (irs) (By similarity). Plays a role
CC in the cytoskeleton organization (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000250|UniProtKB:Q8VCW2}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Heterodimer
CC with type II keratin KRT5 leading to the formation of keratin
CC intermediate filament (KIF) network. Interacts with KRT6A to form
CC filaments. {ECO:0000250|UniProtKB:Q7Z3Z0, ECO:0000250|UniProtKB:Q8VCW2,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VCW2}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; BC119958; AAI19959.1; -; mRNA.
DR RefSeq; NP_001068991.1; NM_001075523.1.
DR AlphaFoldDB; Q0P5J4; -.
DR SMR; Q0P5J4; -.
DR STRING; 9913.ENSBTAP00000040707; -.
DR PaxDb; Q0P5J4; -.
DR PeptideAtlas; Q0P5J4; -.
DR PRIDE; Q0P5J4; -.
DR Ensembl; ENSBTAT00000043116; ENSBTAP00000040707; ENSBTAG00000030542.
DR GeneID; 511540; -.
DR KEGG; bta:511540; -.
DR CTD; 147183; -.
DR VEuPathDB; HostDB:ENSBTAG00000030542; -.
DR VGNC; VGNC:30724; KRT25.
DR eggNOG; ENOG502SKJN; Eukaryota.
DR GeneTree; ENSGT00940000161994; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q0P5J4; -.
DR OMA; KGWYEQF; -.
DR OrthoDB; 805081at2759; -.
DR TreeFam; TF332742; -.
DR Reactome; R-BTA-6805567; Keratinization.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030542; Expressed in zone of skin and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..450
FT /note="Keratin, type I cytoskeletal 25"
FT /id="PRO_0000312689"
FT DOMAIN 79..394
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..78
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..114
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 115..136
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 137..228
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 229..251
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 252..390
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 391..450
FT /note="Tail"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3Z0"
SQ SEQUENCE 450 AA; 49313 MW; D2D3CE42F7F22CE4 CRC64;
MSLRLPSGSR RASPRPTTGS LRLSSGGASF GAGNACSMPG IGSSFSCAFG GSSSGGNALG
GNPCAGFTVN EGGLLSGNEK VTMQNLNDRL ASYLENVRAL EEANADLEQK IKGWYEKFGP
GSCRGLDHDY SRYFPIIEDL KNQIIASTTS NANAVLQIDN ARLTADDFRL KYENELALHQ
SVESDVNGLR RVLDEITLCR TDLEIQYETL SEELTYLKKN HKEEMQVLQC AAGGNVNVEM
NAAPGVDLTV LLNNMRAEYE ALAEQNRRDA EAWFNEKSAS LQQQITEDVG ATTSARNELT
EMKRNLQTLE IELQSLLATK HSLECSLTET EGNYCAQLAQ IQAQIGALEE QLHQVRTETE
GQKLEYEQLL DIKVHLEKEI ETYCLLIGGD DGACKSGGYK SKDYGAGNVG NQMKDPVKAI
VVKKVLEEVD QRSKILTPRL HSLEEKSQSN
