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Keratin, type I cytoskeletal 25 (Cytokeratin-25) (CK-25) (Keratin-25) (K25) (Keratin-25A) (K25A) (Type I inner root sheath-specific keratin-K25irs1)

 K1C25_HUMAN             Reviewed;         450 AA.
Q7Z3Z0;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 115.
RecName: Full=Keratin, type I cytoskeletal 25;
AltName: Full=Cytokeratin-25;
Short=CK-25;
AltName: Full=Keratin-25;
Short=K25;
AltName: Full=Keratin-25A;
Short=K25A;
AltName: Full=Type I inner root sheath-specific keratin-K25irs1;
Name=KRT25 {ECO:0000312|HGNC:HGNC:30839};
Synonyms=KRT25A {ECO:0000312|EMBL:CAD91904.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:CAD91904.1}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Scalp {ECO:0000312|EMBL:CAD91904.1};
PubMed=15617563; DOI=10.1111/j.1432-0436.2004.07209006.x;
Rogers M.A., Winter H., Langbein L., Bleiler R., Schweizer J.;
"The human type I keratin gene family: characterization of new hair
follicle specific members and evaluation of the chromosome 17q21.2
gene domain.";
Differentiation 72:527-540(2004).
[2] {ECO:0000312|EMBL:EAW60676.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=16874310; DOI=10.1038/sj.jid.5700494;
Langbein L., Rogers M.A., Praetzel-Wunder S., Helmke B.,
Schirmacher P., Schweizer J.;
"K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4)
represent the type I inner root sheath keratins of the human hair
follicle.";
J. Invest. Dermatol. 126:2377-2386(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
VARIANT ARWH3 PRO-317.
PubMed=26160856; DOI=10.1136/jmedgenet-2015-103255;
Ansar M., Raza S.I., Lee K., Irfanullah X., Shahi S., Acharya A.,
Dai H., Smith J.D., Shendure J., Bamshad M.J., Nickerson D.A.,
Santos-Cortez R.L., Ahmad W., Leal S.M.;
"A homozygous missense variant in type I keratin KRT25 causes
autosomal recessive woolly hair.";
J. Med. Genet. 52:676-680(2015).
[6]
VARIANT ARWH3 LEU-238, CHARACTERIZATION OF VARIANT ARWH3 LEU-238,
FUNCTION, AND SUBUNIT.
PubMed=26902920; DOI=10.1016/j.jid.2016.01.037;
Zernov N.V., Skoblov M.Y., Marakhonov A.V., Shimomura Y.,
Vasilyeva T.A., Konovalov F.A., Abrukova A.V., Zinchenko R.A.;
"Autosomal recessive hypotrichosis with woolly hair caused by a
mutation in the keratin 25 gene expressed in hair follicles.";
J. Invest. Dermatol. 136:1097-1105(2016).
-!- FUNCTION: Essential for the proper assembly of type I and type II
keratin protein complexes and formation of keratin intermediate
filaments in the inner root sheath (irs) (By similarity). Plays a
role in the cytoskeleton organization (PubMed:26902920).
{ECO:0000250|UniProtKB:Q8VCW2, ECO:0000269|PubMed:26902920}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins
(PubMed:26902920). Interacts with KRT6A to form filaments (By
similarity). {ECO:0000250|UniProtKB:Q8VCW2,
ECO:0000269|PubMed:26902920, ECO:0000305}.
-!- INTERACTION:
Q3SY84:KRT71; NbExp=4; IntAct=EBI-11980019, EBI-2952676;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VCW2}.
-!- TISSUE SPECIFICITY: Strongly expressed in skin and scalp, and weak
expression observed in thymus and tongue. In the hair follicle,
expressed in Henle layer, Huxley layer and in the inner root
sheath cuticle of the hair follicle. Expression extends from the
bulb region up to the point of differentiation into the three
layers. Also present in the medulla of beard hair (at protein
level). {ECO:0000269|PubMed:15617563,
ECO:0000269|PubMed:16874310}.
-!- DISEASE: Woolly hair autosomal recessive 3 (ARWH3) [MIM:616760]: A
hair shaft disorder characterized by fine and tightly curled hair.
Compared to normal curly hair that is observed in some
populations, woolly hair grows slowly and stops growing after a
few inches. Under light microscopy, woolly hair shows some
structural anomalies, including trichorrhexis nodosa and tapered
ends. Some individuals may present with hypotrichosis.
{ECO:0000269|PubMed:26160856, ECO:0000269|PubMed:26902920}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa). {ECO:0000305}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ564204; CAD91904.1; -; mRNA.
EMBL; CH471152; EAW60676.1; -; Genomic_DNA.
CCDS; CCDS11373.1; -.
RefSeq; NP_853512.1; NM_181534.3.
UniGene; Hs.55412; -.
ProteinModelPortal; Q7Z3Z0; -.
SMR; Q7Z3Z0; -.
IntAct; Q7Z3Z0; 22.
STRING; 9606.ENSP00000310573; -.
iPTMnet; Q7Z3Z0; -.
PhosphoSitePlus; Q7Z3Z0; -.
SwissPalm; Q7Z3Z0; -.
BioMuta; KRT25; -.
DMDM; 74723316; -.
PaxDb; Q7Z3Z0; -.
PeptideAtlas; Q7Z3Z0; -.
PRIDE; Q7Z3Z0; -.
DNASU; 147183; -.
Ensembl; ENST00000312150; ENSP00000310573; ENSG00000204897.
GeneID; 147183; -.
KEGG; hsa:147183; -.
UCSC; uc002hve.3; human.
CTD; 147183; -.
DisGeNET; 147183; -.
EuPathDB; HostDB:ENSG00000204897.6; -.
GeneCards; KRT25; -.
H-InvDB; HIX0027280; -.
HGNC; HGNC:30839; KRT25.
HPA; HPA053977; -.
HPA; HPA058943; -.
MalaCards; KRT25; -.
MIM; 616646; gene.
MIM; 616760; phenotype.
neXtProt; NX_Q7Z3Z0; -.
OpenTargets; ENSG00000204897; -.
PharmGKB; PA134977088; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00900000140820; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; Q7Z3Z0; -.
KO; K07604; -.
OMA; EGACKSG; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; Q7Z3Z0; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GenomeRNAi; 147183; -.
PRO; PR:Q7Z3Z0; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000204897; -.
CleanEx; HS_KRT25; -.
Genevisible; Q7Z3Z0; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0007568; P:aging; IDA:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
GO; GO:0042633; P:hair cycle; IDA:UniProtKB.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0031424; P:keratinization; TAS:Reactome.
InterPro; IPR001664; IF.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Disease mutation;
Hypotrichosis; Intermediate filament; Keratin; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 450 Keratin, type I cytoskeletal 25.
/FTId=PRO_0000312691.
DOMAIN 79 394 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 78 Head. {ECO:0000255}.
REGION 79 114 Coil 1A. {ECO:0000255}.
REGION 115 136 Linker 1. {ECO:0000255}.
REGION 137 228 Coil 1B. {ECO:0000255}.
REGION 229 251 Linker 12. {ECO:0000255}.
REGION 252 390 Coil 2. {ECO:0000255}.
REGION 391 450 Tail. {ECO:0000255}.
COMPBIAS 25 77 Gly-rich. {ECO:0000255}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 54 54 S -> L (in dbSNP:rs12951399).
/FTId=VAR_049786.
VARIANT 238 238 V -> L (in ARWH3; reduces keratin
intermediate filamen formation; impairs
cytoskeleton assembly;
dbSNP:rs879253749).
{ECO:0000269|PubMed:26902920}.
/FTId=VAR_076303.
VARIANT 317 317 L -> P (in ARWH3; dbSNP:rs766783183).
{ECO:0000269|PubMed:26160856}.
/FTId=VAR_076304.
SEQUENCE 450 AA; 49318 MW; 12AB5BF74BA426FF CRC64;
MSLRLSSASR RSCPRPTTGS LRLYGGGTSF GTGNSCGISG IGSGFSSAFG GSSSGGNTGG
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 SQVKDPAKAI
VVKKVLEEVD QRSKILTTRL HSLEEKSQSN


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