K1C23_MOUSE
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 03-AUG-2022, entry version 141.
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>3.0.co;2-w;
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}.
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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; Q99PS0; -.
DR PRIDE; Q99PS0; -.
DR ProteomicsDB; 269051; -.
DR Antibodypedia; 1978; 293 antibodies from 29 providers.
DR DNASU; 94179; -.
DR Ensembl; ENSMUST00000006969; ENSMUSP00000006969; ENSMUSG00000006777.
DR GeneID; 94179; -.
DR KEGG; mmu:94179; -.
DR UCSC; uc007liv.1; mouse.
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; SQDFKVN; -.
DR OrthoDB; 798081at2759; -.
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 74 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 tissues.
DR ExpressionAtlas; Q99PS0; baseline and differential.
DR Genevisible; Q99PS0; MM.
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 InterPro; IPR018039; IF_conserved.
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; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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
