ID   K1C25_SHEEP             Reviewed;         450 AA.
AC   Q9BGM5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
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   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:AAK00222.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Corriedale {ECO:0000312|EMBL:AAK00222.1};
RX   PubMed=11168812; DOI=10.1046/j.1523-1747.2001.00215.x;
RA   Bawden C.S., McLaughlan C., Nesci A., Rogers G.;
RT   "A unique type I keratin intermediate filament gene family is abundantly
RT   expressed in the inner root sheaths of sheep and human hair follicles.";
RL   J. Invest. Dermatol. 116:157-166(2001).
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   -!- TISSUE SPECIFICITY: Expressed in skin and wool follicle. Expression
CC       localized to the inner root sheath of wool follicle.
CC       {ECO:0000269|PubMed:11168812}.
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; AF227759; AAK00222.1; -; mRNA.
DR   RefSeq; NP_001009739.1; NM_001009739.1.
DR   AlphaFoldDB; Q9BGM5; -.
DR   SMR; Q9BGM5; -.
DR   STRING; 9940.ENSOARP00000016210; -.
DR   PRIDE; Q9BGM5; -.
DR   GeneID; 443079; -.
DR   KEGG; oas:443079; -.
DR   CTD; 147183; -.
DR   eggNOG; ENOG502SKJN; Eukaryota.
DR   OrthoDB; 805081at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; 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   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_0000312695"
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;  49313 MW;  8F924BA92D3BB1D6 CRC64;
     MSLRLPSGSR RAGPRPTTGS LRLSGAGASF GAGNACSMPG IGSSFSCAFG SSSSGGNALG
     GNPCAGFTMN EGGLLSGNEK VTMQNLNDRL ASYLENVRAL EEANADLEQK IKGWYEKFGP
     GSCRGLDHDY SRYLPIIEDL KNQIIASTTS NANAVLQIDN ARLTADVFRL KYENELALHQ
     SVESDVNGLR RVLDVITLCR TDLEIQYETL SEELTYLKKN HKEEMQVLQC AAGGNVNVEM
     NAAPGVDLTV LLNNMRAEYE ALAEQNRRDA EAWFNEKSAS LQQQITEDVG ATTSARNELT
     EMKRNLQTLE IELQSLLATK HSLECSLTET EGNYCAQLAQ VQAQIGALEE QLHQVRTETE
     GQKLEYEQLL DIKVHLEKEI ETYCLLIGGD DGACKSGGYK SKDYAAGNMG NQMKDPIRAI
     VVKKVLEEVD QRSKVLTTRL HSLEEKSQSN