ID   K1C25_CAPHI             Reviewed;         450 AA.
AC   Q6R650;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
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;
DE   AltName: Full=Type I keratin intermediate filament IRSa1;
GN   Name=KRT25 {ECO:0000250|UniProtKB:Q7Z3Z0};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1] {ECO:0000312|EMBL:AAS00518.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yin J., Li J.Q., Zhou H.M.;
RL   Submitted (DEC-2003) 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; AY510111; AAS00518.1; -; mRNA.
DR   RefSeq; NP_001272695.1; NM_001285766.1.
DR   AlphaFoldDB; Q6R650; -.
DR   SMR; Q6R650; -.
DR   STRING; 9925.ENSCHIP00000014359; -.
DR   PRIDE; Q6R650; -.
DR   Ensembl; ENSCHIT00000022153; ENSCHIP00000014359; ENSCHIG00000015383.
DR   GeneID; 100861172; -.
DR   KEGG; chx:100861172; -.
DR   CTD; 147183; -.
DR   GeneTree; ENSGT00940000161994; -.
DR   OMA; KGWYEQF; -.
DR   OrthoDB; 805081at2759; -.
DR   Proteomes; UP000291000; Chromosome 19.
DR   Bgee; ENSCHIG00000015383; Expressed in skin of neck and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR   GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
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_0000312690"
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..24
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   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3Z0"
SQ   SEQUENCE   450 AA;  49423 MW;  084877188F3FFA90 CRC64;
     MSLRLPSGSR RASPRPTTGS LRLSGAGASF GAGNACSMPG IGSSFSCAFG SSSSGGNALG
     GNPCAGFTMN 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 SKDYAAGNMG NQMKDPIKAI
     VVKKVLEEVD QRSKILTTRL HSLEEKSQSN