K1C25_PANTR
ID K1C25_PANTR Reviewed; 450 AA.
AC A5A6N2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=Keratin-25A;
DE Short=K25A;
DE AltName: Full=Type I inner root sheath-specific keratin-K25irs1;
GN Name=KRT25; Synonyms=KRT25A;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1] {ECO:0000312|EMBL:BAF62405.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:BAF62405.1};
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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; AB222160; BAF62405.1; -; mRNA.
DR RefSeq; NP_001092033.1; NM_001098563.1.
DR AlphaFoldDB; A5A6N2; -.
DR SMR; A5A6N2; -.
DR STRING; 9598.ENSPTRP00000015562; -.
DR PaxDb; A5A6N2; -.
DR PRIDE; A5A6N2; -.
DR GeneID; 468237; -.
DR KEGG; ptr:468237; -.
DR CTD; 147183; -.
DR eggNOG; ENOG502SKJN; Eukaryota.
DR InParanoid; A5A6N2; -.
DR OrthoDB; 805081at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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 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_0000312693"
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..26
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; 49307 MW; D1663298C0AE380A CRC64;
MSLRLSSASR RSCPRPTTGS LRLSGGGTSF GTGNSCGISG IGSGFSCAFG GSSLGGNTAG
GNPCAGFTVN ERGLLSGNEK VTMQNLNDRL ASYLDSVHAL EEANADLEQK IKGWYEKFGP
GSCRGLDHDY SRYFPIIDDL KNQIIASTTS NANAVLQIDN ARLTADDFRL KYENELALHQ
SVEADVNGLR RVLDEITLCR TDLEIQYETL SEEMTYLKKN HKEEMQVLQC AAGGNVNVEM
NAAPGVDLTV LLNNMRAEYE ALAEQNRRDA EAWFNEKSAS LQQQISEDVG ATTSARNELT
EMKRTLQTLE IELQSLLATK HSLECSLTET ESNYCAQLAQ IQAQIGALEE QLHQVRTETE
GQKLEYEQLL DIKLHLEKEI ETYCLLIGGD DGACKSGGYK SKDYGSGNVG SQVKDSAKAI
VVKKVLEEVD QRSKILTTRL RSLEEKSQSN
