K2C1_MOUSE
ID K2C1_MOUSE Reviewed; 637 AA.
AC P04104; Q149E0; Q9D2K8;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Keratin, type II cytoskeletal 1;
DE AltName: Full=67 kDa cytokeratin;
DE AltName: Full=Cytokeratin-1;
DE Short=CK-1;
DE AltName: Full=Keratin-1;
DE Short=K1;
DE AltName: Full=Type-II keratin Kb1;
GN Name=Krt1; Synonyms=Krt2-1;
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=2581964; DOI=10.1016/s0021-9258(18)88900-1;
RA Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C.,
RA Roop D.R.;
RT "Amino acid sequences of mouse and human epidermal type II keratins of Mr
RT 67,000 provide a systematic basis for the structural and functional
RT diversity of the end domains of keratin intermediate filament subunits.";
RL J. Biol. Chem. 260:7142-7149(1985).
RN [2]
RP SEQUENCE REVISION.
RA Roop D.R.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 199-205; 208-219 AND 286-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH KRT14, INTERACTION WITH KRT14, AND
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 [7]
RP CITRULLINATION.
RX PubMed=11841545; DOI=10.1046/j.0022-202x.2001.01671.x;
RA Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H.,
RA Akiyama M., Iizuka H.;
RT "Sequential reorganization of cornified cell keratin filaments involving
RT filaggrin-mediated compaction and keratin 1 deimination.";
RL J. Invest. Dermatol. 118:282-287(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, AND
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=24751727; DOI=10.1038/jid.2014.197;
RA Fischer H., Langbein L., Reichelt J., Praetzel-Wunder S., Buchberger M.,
RA Ghannadan M., Tschachler E., Eckhart L.;
RT "Loss of keratin K2 expression causes aberrant aggregation of K10,
RT hyperkeratosis, and inflammation.";
RL J. Invest. Dermatol. 134:2579-2588(2014).
RN [10]
RP INTERACTION WITH PLEC AND KRT10.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12; ARG-49; ARG-526; ARG-585 AND
RP ARG-607, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP VARIANT EHK PRO-194.
RX PubMed=16528356; DOI=10.1038/sj.jid.5700241;
RA McGowan K.A., Aradhya S., Fuchs H., de Angelis M.H., Barsh G.S.;
RT "A mouse keratin 1 mutation causes dark skin and epidermolytic
RT hyperkeratosis.";
RL J. Invest. Dermatol. 126:1013-1016(2006).
CC -!- FUNCTION: May regulate the activity of kinases such as PKC and SRC via
CC binding to integrin beta-1 (ITB1) and the receptor of activated protein
CC C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor
CC for kininogen-1/HMWK (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins
CC (PubMed:24940650, PubMed:11408584). Heterodimer with KRT10
CC (PubMed:24940650). Two heterodimers of KRT1 and KRT10 form a
CC heterotetramer (By similarity). Forms a heterodimer with KRT14; the
CC interaction is more abundant in the absence of KRT5 (PubMed:11408584).
CC Interacts with PLEC isoform 1C, when in a heterodimer with KRT10
CC (PubMed:24940650). Interacts with ITGB1 in the presence of RACK1 and
CC SRC, and with RACK1 (By similarity). Interacts with C1QBP; the
CC association represents a cell surface kininogen receptor (By
CC similarity). Interacts with EPPK1; interaction is dependent of higher-
CC order structure of intermediate filament (By similarity).
CC {ECO:0000250|UniProtKB:P04264, ECO:0000269|PubMed:11408584,
CC ECO:0000269|PubMed:24940650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04264}.
CC Cytoplasm {ECO:0000250|UniProtKB:P04264}.
CC -!- TISSUE SPECIFICITY: Expressed in the infundibular regions of the ear,
CC the interfollicular epidermis of the back, in the interscale regions
CC containing hair follicles in the tail, and in the soles of the footpads
CC (at protein level). {ECO:0000269|PubMed:24751727}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the skin at birth.
CC {ECO:0000269|PubMed:11408584}.
CC -!- PTM: Undergoes deimination of some arginine residues (citrullination).
CC {ECO:0000269|PubMed:11841545}.
CC -!- DISEASE: Note=Defects in Krt1 are a cause of epidermolytic
CC hyperkeratosis (EHK); also known as bullous congenital ichthyosiform
CC erythroderma (BIE). EHK is a hereditary skin disorder characterized by
CC intraepidermal blistering, a marked thickening of the stratum corneum,
CC pigmentation of the skin and erosions at sites of trauma which are all
CC present from birth.
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; M10937; AAD05191.1; -; mRNA.
DR EMBL; AK019521; BAB31776.1; -; mRNA.
DR EMBL; BC117842; AAI17843.1; -; mRNA.
DR EMBL; BC117843; AAI17844.1; -; mRNA.
DR CCDS; CCDS37221.1; -.
DR PIR; A02951; KRMS2.
DR RefSeq; NP_032499.2; NM_008473.2.
DR AlphaFoldDB; P04104; -.
DR SMR; P04104; -.
DR BioGRID; 201030; 20.
DR ComplexPortal; CPX-5871; Keratin-1 - Keratin-10 dimer complex.
DR IntAct; P04104; 2.
DR STRING; 10090.ENSMUSP00000023790; -.
DR iPTMnet; P04104; -.
DR PhosphoSitePlus; P04104; -.
DR SWISS-2DPAGE; P04104; -.
DR EPD; P04104; -.
DR jPOST; P04104; -.
DR MaxQB; P04104; -.
DR PaxDb; P04104; -.
DR PeptideAtlas; P04104; -.
DR PRIDE; P04104; -.
DR ProteomicsDB; 268942; -.
DR Antibodypedia; 3686; 1237 antibodies from 40 providers.
DR DNASU; 16678; -.
DR Ensembl; ENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
DR GeneID; 16678; -.
DR KEGG; mmu:16678; -.
DR UCSC; uc007xuc.1; mouse.
DR CTD; 3848; -.
DR MGI; MGI:96698; Krt1.
DR VEuPathDB; HostDB:ENSMUSG00000046834; -.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR GeneTree; ENSGT00940000162175; -.
DR HOGENOM; CLU_012560_6_0_1; -.
DR InParanoid; P04104; -.
DR OMA; IRMSGEC; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P04104; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16678; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Krt1; mouse.
DR PRO; PR:P04104; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P04104; protein.
DR Bgee; ENSMUSG00000046834; Expressed in lip and 82 other tissues.
DR Genevisible; P04104; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:MGI.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032449; Keratin_2_1_tail.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR Pfam; PF16210; Keratin_2_tail; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
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 Cell membrane; Citrullination; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disease variant; Intermediate filament; Keratin;
KW Membrane; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..637
FT /note="Keratin, type II cytoskeletal 1"
FT /id="PRO_0000063710"
FT DOMAIN 188..501
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..187
FT /note="Head"
FT REGION 188..223
FT /note="Coil 1A"
FT REGION 224..243
FT /note="Linker 1"
FT REGION 244..334
FT /note="Coil 1B"
FT REGION 335..358
FT /note="Linker 12"
FT REGION 359..497
FT /note="Coil 2"
FT REGION 498..637
FT /note="Tail"
FT REGION 505..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..328
FT /evidence="ECO:0000255"
FT COILED 397..483
FT /evidence="ECO:0000255"
FT COMPBIAS 505..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 452
FT /note="Stutter"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 284
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 526
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 585
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 607
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 194
FT /note="S -> P (in EHK)"
FT /evidence="ECO:0000269|PubMed:16528356"
FT CONFLICT 99
FT /note="G -> R (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="L -> S (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> T (in Ref. 3; BAB31776)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..151
FT /note="SM -> GY (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..158
FT /note="PPG -> SPS (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> L (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> K (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="Q -> K (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="D -> E (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> R (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> N (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="A -> T (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..353
FT /note="SL -> QF (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="S -> Y (in Ref. 3; BAB31776)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..580
FT /note="Missing (in Ref. 1; AAD05191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 65606 MW; D2016D15066FD0A5 CRC64;
MSLQCSSRSL CRGGGGSRNF SSGSAGLVSF QRRSTSSSMR RSGGGGGGRF SGGGFCGSSG
SGFGSKSLMN LGGGRSISKS VAGGGGSFCG GFGGGSYGGG GFGGGSYGGG GFGGGSFGGG
GFGGSGFGGG LGGGGGFGSG GGFGGGRFGS MGPVCPPGGI QEVTINQSLL QPLNVEVDPQ
IQKVKSQERE QIKSLNDKFA SFIDKVRFLE QQNQVLQTKW ELLQQVDTTT RTQNLDPFFE
NYISILRRKV DSLKSDQSRM DSELKNMQDL VEEYRTKYED EINKRTNAEN EFVTIKKDVD
SAYMTKVELQ AKADALQQDI DFFSALYQME MSQMQTQISE TNVVLSMDNN RSLDLDGIIS
EVKAQYDSIC QRSKAEAETF YQSKYEELQI TAGKHGDSVR NTKMEISELN RMIQRLRSEI
DGCKKQISQI QQNINDAEQR GEKALKDAQN KLNEIEDALS QCKEDLARLL RDFQELMNTK
LALDMEIATY KKLLEGEEIR MSGECTPNVS VSVSTSHTSM SGSSSRGGGS GGGRYGGGGS
YGGGSGGGSY GGSSGGGGSG GSYGGGSGGG SYGGGSGGGS SGSHRGGSGG GGGSSGGSYG
GSSGGGRGGS SSGGGGVKSS GSSTVKFVST SYSRGTK
