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K1C16_MOUSE
ID   K1C16_MOUSE             Reviewed;         469 AA.
AC   Q9Z2K1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Keratin, type I cytoskeletal 16;
DE   AltName: Full=Cytokeratin-16;
DE            Short=CK-16;
DE   AltName: Full=Keratin-16;
DE            Short=K16;
GN   Name=Krt16; Synonyms=Krt1-16;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=9822705; DOI=10.1074/jbc.273.48.32265;
RA   Porter R.M., Hutcheson A.M., Rugg E.L., Quinlan R.A., Lane E.B.;
RT   "cDNA cloning, expression, and assembly characteristics of mouse keratin
RT   16.";
RL   J. Biol. Chem. 273:32265-32272(1998).
RN   [2]
RP   INDUCTION, AND SUBUNIT.
RX   PubMed=8636216; DOI=10.1083/jcb.132.3.381;
RA   Paladini R.D., Takahashi K., Bravo N.S., Coulombe P.A.;
RT   "Onset of re-epithelialization after skin injury correlates with a
RT   reorganization of keratin filaments in wound edge keratinocytes: defining a
RT   potential role for keratin 16.";
RL   J. Cell Biol. 132:381-397(1996).
RN   [3]
RP   FUNCTION.
RX   PubMed=11029038; DOI=10.1091/mbc.11.10.3315;
RA   Wawersik M., Coulombe P.A.;
RT   "Forced expression of keratin 16 alters the adhesion, differentiation, and
RT   migration of mouse skin keratinocytes.";
RL   Mol. Biol. Cell 11:3315-3327(2000).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11408584; DOI=10.1091/mbc.12.6.1775;
RA   Peters B., Kirfel J., Bussow H., Vidal M., Magin T.M.;
RT   "Complete cytolysis and neonatal lethality in keratin 5 knockout mice
RT   reveal its fundamental role in skin integrity and in epidermolysis bullosa
RT   simplex.";
RL   Mol. Biol. Cell 12:1775-1789(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12445204; DOI=10.1046/j.1523-1747.2002.19518.x;
RA   Bernot K.M., Coulombe P.A., McGowan K.M.;
RT   "Keratin 16 expression defines a subset of epithelial cells during skin
RT   morphogenesis and the hair cycle.";
RL   J. Invest. Dermatol. 119:1137-1149(2002).
RN   [6]
RP   INTERACTION WITH TRADD.
RX   PubMed=16702408; DOI=10.1101/gad.1387406;
RA   Tong X., Coulombe P.A.;
RT   "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
RT   fashion.";
RL   Genes Dev. 20:1353-1364(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22336941; DOI=10.1038/jid.2012.6;
RA   Lessard J.C., Coulombe P.A.;
RT   "Keratin 16-null mice develop palmoplantar keratoderma, a hallmark feature
RT   of pachyonychia congenita and related disorders.";
RL   J. Invest. Dermatol. 132:1384-1391(2012).
RN   [9]
RP   FUNCTION.
RX   PubMed=24218583; DOI=10.1073/pnas.1309576110;
RA   Lessard J.C., Pina-Paz S., Rotty J.D., Hickerson R.P., Kaspar R.L.,
RA   Balmain A., Coulombe P.A.;
RT   "Keratin 16 regulates innate immunity in response to epidermal barrier
RT   breach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19537-19542(2013).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=26758872; DOI=10.1093/hmg/ddw001;
RA   Allen E.H., Courtney D.G., Atkinson S.D., Moore J.E., Mairs L.,
RA   Poulsen E.T., Schiroli D., Maurizi E., Cole C., Hickerson R.P., James J.,
RA   Murgatroyd H., Smith F.J., MacEwen C., Enghild J.J., Nesbit M.A.,
RA   Leslie Pedrioli D.M., McLean W.H., Moore C.B.;
RT   "Keratin 12 missense mutation induces the unfolded protein response and
RT   apoptosis in Meesmann epithelial corneal dystrophy.";
RL   Hum. Mol. Genet. 25:1176-1191(2016).
CC   -!- FUNCTION: Epidermis-specific type I keratin that plays a key role in
CC       skin (PubMed:22336941, PubMed:24218583). Acts as a regulator of innate
CC       immunity in response to skin barrier breach: required for some
CC       inflammatory checkpoint for the skin barrier maintenance
CC       (PubMed:24218583). {ECO:0000269|PubMed:11029038,
CC       ECO:0000269|PubMed:22336941, ECO:0000269|PubMed:24218583}.
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT16
CC       associates with KRT6 isomers (KRT6A or KRT6B) (PubMed:8636216).
CC       Interacts with TCHP (By similarity). Interacts with TRADD
CC       (PubMed:16702408). {ECO:0000250|UniProtKB:P08779,
CC       ECO:0000269|PubMed:16702408, ECO:0000269|PubMed:8636216}.
CC   -!- TISSUE SPECIFICITY: Expressed in the epithelia of the tongue, upper and
CC       lower palate, footpad, proximal nail fold and nail bed, penile spine,
CC       sweat gland ducts, and back epidermis (at protein level)
CC       (PubMed:12445204). Expressed in upper suprabasal layers of the corneal
CC       epithelium (at protein level) (PubMed:26758872). Expressed in internal
CC       stratified epithelia in the esophagus and vagina (at protein level)
CC       (PubMed:12445204). Expressed in transitional stratified squamous
CC       epithelia in the forestomach, anal canal, and nasal cavity (at protein
CC       level) (PubMed:12445204). Expressed in transitional epithelia of the
CC       ureter, bladder and urethra (at protein level) (PubMed:12445204). In
CC       mature hair follicles, expressed in the companion layer of the outer
CC       root sheath during anagen and in the club hair sheath during catagen
CC       and telogen (at protein level) (PubMed:12445204).
CC       {ECO:0000269|PubMed:12445204, ECO:0000269|PubMed:26758872}.
CC   -!- DEVELOPMENTAL STAGE: During embryonic development, initially localizes
CC       within early hair germs, but rapidly shifts to a subset of cells at the
CC       interface of basal and suprabasal cells above and around the hair germ
CC       (PubMed:12445204). Expressed in hair follicles and in most cells in the
CC       spinous layer at birth (PubMed:11408584). {ECO:0000269|PubMed:11408584,
CC       ECO:0000269|PubMed:12445204}.
CC   -!- INDUCTION: In response to epidermal stress such as wounding.
CC       {ECO:0000269|PubMed:8636216}.
CC   -!- DISRUPTION PHENOTYPE: Mice were born alive at approximately Mendelian
CC       ratios but increased postnatal mortality is observed. Surviving mice
CC       show oral lesions as well as palmoplantar keratoderma-like
CC       hyperkeratotic calluses on front and hind paws, which impair the
CC       ability to walk. {ECO:0000269|PubMed:22336941}.
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; AF053235; AAC79424.1; -; mRNA.
DR   CCDS; CCDS25414.1; -.
DR   RefSeq; NP_001300887.1; NM_001313958.1.
DR   RefSeq; NP_032496.1; NM_008470.1.
DR   AlphaFoldDB; Q9Z2K1; -.
DR   SMR; Q9Z2K1; -.
DR   BioGRID; 201021; 15.
DR   IntAct; Q9Z2K1; 2.
DR   MINT; Q9Z2K1; -.
DR   STRING; 10090.ENSMUSP00000007280; -.
DR   iPTMnet; Q9Z2K1; -.
DR   PhosphoSitePlus; Q9Z2K1; -.
DR   CPTAC; non-CPTAC-3796; -.
DR   jPOST; Q9Z2K1; -.
DR   PaxDb; Q9Z2K1; -.
DR   PRIDE; Q9Z2K1; -.
DR   ProteomicsDB; 269162; -.
DR   Antibodypedia; 3602; 650 antibodies from 37 providers.
DR   DNASU; 16666; -.
DR   Ensembl; ENSMUST00000007280; ENSMUSP00000007280; ENSMUSG00000053797.
DR   GeneID; 16666; -.
DR   KEGG; mmu:16666; -.
DR   UCSC; uc007lkq.2; mouse.
DR   CTD; 3868; -.
DR   MGI; MGI:96690; Krt16.
DR   VEuPathDB; HostDB:ENSMUSG00000053797; -.
DR   eggNOG; ENOG502QTM6; Eukaryota.
DR   GeneTree; ENSGT00940000154602; -.
DR   HOGENOM; CLU_012560_8_1_1; -.
DR   InParanoid; Q9Z2K1; -.
DR   OMA; GHQTRPI; -.
DR   OrthoDB; 798081at2759; -.
DR   PhylomeDB; Q9Z2K1; -.
DR   TreeFam; TF332742; -.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 16666; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q9Z2K1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9Z2K1; protein.
DR   Bgee; ENSMUSG00000053797; Expressed in lip and 38 other tissues.
DR   ExpressionAtlas; Q9Z2K1; baseline and differential.
DR   Genevisible; Q9Z2K1; MM.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR   GO; GO:0007568; P:aging; ISO:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR   GO; GO:0042633; P:hair cycle; ISO:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:MGI.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0031424; P:keratinization; IDA:UniProtKB.
DR   GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0051546; P:keratinocyte migration; IDA:UniProtKB.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
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; Immunity; Innate immunity; Intermediate filament; Keratin;
KW   Reference proteome.
FT   CHAIN           1..469
FT                   /note="Keratin, type I cytoskeletal 16"
FT                   /id="PRO_0000063663"
FT   DOMAIN          113..424
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..112
FT                   /note="Head"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..148
FT                   /note="Coil 1A"
FT   REGION          149..166
FT                   /note="Linker 1"
FT   REGION          167..258
FT                   /note="Coil 1B"
FT   REGION          259..281
FT                   /note="Linker 12"
FT   REGION          282..420
FT                   /note="Coil 2"
FT   REGION          421..469
FT                   /note="Tail"
FT   REGION          422..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  51606 MW;  13B8028CF28B64D5 CRC64;
     MATCSRQFTS SSSMKGSCGI GGGSSRMSSI LAGGSCRAPS TCGGMSVTSS RFSSGGVCGI
     GGGYGGSFSS SSFGGGLGSG FGGRFDGFGG GFGAGLGGGL GGGIGDGLLV GSEKVTMQNL
     NDRLATYLDK VRALEEANRD LEVKIRDWYQ RQRPTEIKDY SPYFKTIEDL KSKIIIATQE
     NAQFTLQIDN ARLAADDFRT KYENELFLRQ SVEGDINGLR KVLDELTLSR ADLEMQIENL
     REELAFLKKN HEEEMLALRG QTGGDVNVEM DAAPGVDLSR ILNEMRDQYE QMAEKNRRDV
     EAWFLRKTEE LNKEVASNSD LIQSNRSEVA ELRRVFQGLE IELQSQLSMK ASLENSLEET
     KGRYCMQLSQ IQGLISSVEE QLAQLRCEME QQSQEYNILL DVKTRLEQEI ATYRRLLDGE
     NIHSSSQHSS GQSYSSREVF SSSSRQPRSI LKEQGSTSFS QSQSQSSRD
 
 
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