ID   K1C23_MOUSE             Reviewed;         422 AA.
AC   Q99PS0;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Keratin, type I cytoskeletal 23;
DE   AltName: Full=Cytokeratin-23;
DE            Short=CK-23;
DE   AltName: Full=Keratin-23;
DE            Short=K23;
GN   Name=Krt23; Synonyms=Haik1, Krt1-23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11135429;
RX   DOI=10.1002/1098-2264(2000)9999:9999<::aid-gcc1070>3.3.co;2-n;
RA   Zhang J.-S., Wang L., Huang H., Nelson M., Smith D.I.;
RT   "Keratin 23 (K23), a novel acidic keratin, is highly induced by histone
RT   deacetylase inhibitors during differentiation of pancreatic cancer cells.";
RL   Genes Chromosomes Cancer 30:123-135(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF102849; AAK00051.1; -; mRNA.
DR   EMBL; BC019972; AAH19972.1; -; mRNA.
DR   CCDS; CCDS25382.1; -.
DR   RefSeq; NP_203537.1; NM_033373.1.
DR   AlphaFoldDB; Q99PS0; -.
DR   SMR; Q99PS0; -.
DR   STRING; 10090.ENSMUSP00000006969; -.
DR   iPTMnet; Q99PS0; -.
DR   PhosphoSitePlus; Q99PS0; -.
DR   PaxDb; 10090-ENSMUSP00000006969; -.
DR   ProteomicsDB; 269051; -.
DR   Antibodypedia; 1978; 320 antibodies from 29 providers.
DR   DNASU; 94179; -.
DR   Ensembl; ENSMUST00000006969.8; ENSMUSP00000006969.8; ENSMUSG00000006777.8.
DR   GeneID; 94179; -.
DR   KEGG; mmu:94179; -.
DR   UCSC; uc007liv.1; mouse.
DR   AGR; MGI:2148866; -.
DR   CTD; 25984; -.
DR   MGI; MGI:2148866; Krt23.
DR   VEuPathDB; HostDB:ENSMUSG00000006777; -.
DR   eggNOG; ENOG502QTH0; Eukaryota.
DR   GeneTree; ENSGT00940000161077; -.
DR   HOGENOM; CLU_012560_8_1_1; -.
DR   InParanoid; Q99PS0; -.
DR   OMA; SCILEWH; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; Q99PS0; -.
DR   TreeFam; TF332742; -.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 94179; 2 hits in 79 CRISPR screens.
DR   PRO; PR:Q99PS0; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q99PS0; Protein.
DR   Bgee; ENSMUSG00000006777; Expressed in otic placode and 100 other cell types or tissues.
DR   ExpressionAtlas; Q99PS0; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR   PANTHER; PTHR23239:SF44; KERATIN, TYPE I CYTOSKELETAL 23; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   Genevisible; Q99PS0; MM.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..422
FT                   /note="Keratin, type I cytoskeletal 23"
FT                   /id="PRO_0000063678"
FT   DOMAIN          72..382
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..71
FT                   /note="Head"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..107
FT                   /note="Coil 1A"
FT   REGION          108..125
FT                   /note="Linker 1"
FT   REGION          126..217
FT                   /note="Coil 1B"
FT   REGION          218..240
FT                   /note="Linker 12"
FT   REGION          241..378
FT                   /note="Coil 2"
FT   REGION          379..422
FT                   /note="Rod-like helical tail"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  48027 MW;  BD49C5215B5BB61E CRC64;
     MNSSHSFNQT YSASVHSLGS TRGRQGSCHR APSVHGGAGG VRISLSFTTP GCLPPGGSWG
     SGRSSPLLGG NGKATMQNLN DRLATYLEKV RALEEANSKL ETRILRWHQE REPSHRKDYS
     QYEENISRLQ EQIVDGKMAN AHIVVLIDNA RMAVDDFNLK FENEHSLKKD LEIEVEGLRK
     TLDDLTIVTT DLEQEVEGMR KELILMKKRH EQEMEENHLP SDFKVSVKVD TTPGEDLIKV
     LEDMRQEYEL IIKKKHQELD TWFREQSAAM AQEVASPAPV QGNQSDIHEL RRTFQALEID
     LQAQHSRKTA LENMLTETRA RYSCRLQDMQ QIISHYEEEL IQLRQDLERQ NNEHKVLLGI
     KTHLEKEIAT YRRLLEGDTE GTMDGSESRL KGSEASTIKA ITQESVNGRI VLSQVNEIQK
     HI
//