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Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Keratin-1) (K1) (Type-II keratin Kb1)

 K2C1_MOUSE              Reviewed;         637 AA.
P04104; Q149E0; Q9D2K8;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 4.
25-OCT-2017, entry version 155.
RecName: Full=Keratin, type II cytoskeletal 1;
AltName: Full=67 kDa cytokeratin;
AltName: Full=Cytokeratin-1;
Short=CK-1;
AltName: Full=Keratin-1;
Short=K1;
AltName: Full=Type-II keratin Kb1;
Name=Krt1; Synonyms=Krt2-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2581964;
Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C.,
Roop D.R.;
"Amino acid sequences of mouse and human epidermal type II keratins of
Mr 67,000 provide a systematic basis for the structural and functional
diversity of the end domains of keratin intermediate filament
subunits.";
J. Biol. Chem. 260:7142-7149(1985).
[2]
SEQUENCE REVISION.
Roop D.R.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 199-205; 208-219 AND 286-296, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
CITRULLINATION.
PubMed=11841545; DOI=10.1046/j.0022-202x.2001.01671.x;
Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H.,
Akiyama M., Iizuka H.;
"Sequential reorganization of cornified cell keratin filaments
involving filaggrin-mediated compaction and keratin 1 deimination.";
J. Invest. Dermatol. 118:282-287(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-24, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12; ARG-49; ARG-526; ARG-585
AND ARG-607, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[9]
VARIANT EHK PRO-194.
PubMed=16528356; DOI=10.1038/sj.jid.5700241;
McGowan K.A., Aradhya S., Fuchs H., de Angelis M.H., Barsh G.S.;
"A mouse keratin 1 mutation causes dark skin and epidermolytic
hyperkeratosis.";
J. Invest. Dermatol. 126:1013-1016(2006).
-!- FUNCTION: May regulate the activity of kinases such as PKC and SRC
via binding to integrin beta-1 (ITB1) and the receptor of
activated protein C kinase 1 (RACK1). In complex with C1QBP is a
high affinity receptor for kininogen-1/HMWK (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Keratin-1 is generally associated with keratin-10. Interacts with
ITGB1 in the presence of RACK1 and SRC, and with RACK1. Interacts
with C1QBP; the association represents a cell surface kininogen
receptor. Interacts with EPPK1; interaction is dependent of
higher-order structure of intermediate filament.
{ECO:0000250|UniProtKB:P04264}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
-!- PTM: Undergoes deimination of some arginine residues
(citrullination). {ECO:0000269|PubMed:11841545}.
-!- DISEASE: Note=Defects in Krt1 are a cause of epidermolytic
hyperkeratosis (EHK); also known as bullous congenital
ichthyosiform erythroderma (BIE). EHK is a hereditary skin
disorder characterized by intraepidermal blistering, a marked
thickening of the stratum corneum, pigmentation of the skin and
erosions at sites of trauma which are all present from birth.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; M10937; AAD05191.1; -; mRNA.
EMBL; AK019521; BAB31776.1; -; mRNA.
EMBL; BC117842; AAI17843.1; -; mRNA.
EMBL; BC117843; AAI17844.1; -; mRNA.
CCDS; CCDS37221.1; -.
PIR; A02951; KRMS2.
RefSeq; NP_032499.2; NM_008473.2.
UniGene; Mm.183137; -.
ProteinModelPortal; P04104; -.
SMR; P04104; -.
BioGrid; 201030; 11.
IntAct; P04104; 3.
MINT; MINT-1865848; -.
STRING; 10090.ENSMUSP00000023790; -.
iPTMnet; P04104; -.
PhosphoSitePlus; P04104; -.
SWISS-2DPAGE; P04104; -.
EPD; P04104; -.
MaxQB; P04104; -.
PaxDb; P04104; -.
PeptideAtlas; P04104; -.
PRIDE; P04104; -.
Ensembl; ENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
GeneID; 16678; -.
KEGG; mmu:16678; -.
UCSC; uc007xuc.1; mouse.
CTD; 3848; -.
MGI; MGI:96698; Krt1.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P04104; -.
KO; K07605; -.
OMA; EKCICCE; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P04104; -.
TreeFam; TF317854; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6805567; Keratinization.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
ChiTaRS; Krt1; mouse.
PRO; PR:P04104; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000046834; -.
CleanEx; MM_KRT1; -.
Genevisible; P04104; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0001533; C:cornified envelope; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0045095; C:keratin filament; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
GO; GO:0030280; F:structural constituent of epidermis; ISO:MGI.
GO; GO:0001867; P:complement activation, lectin pathway; ISO:MGI.
GO; GO:0061436; P:establishment of skin barrier; IMP:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032449; Keratin_2_1_tail.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
Pfam; PF16210; Keratin_2_tail; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Cell membrane; Citrullination; Coiled coil; Complete proteome;
Direct protein sequencing; Disease mutation; Intermediate filament;
Keratin; Membrane; Methylation; Phosphoprotein; Reference proteome.
CHAIN 1 637 Keratin, type II cytoskeletal 1.
/FTId=PRO_0000063710.
DOMAIN 188 501 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 187 Head.
REGION 188 223 Coil 1A.
REGION 224 243 Linker 1.
REGION 244 334 Coil 1B.
REGION 335 358 Linker 12.
REGION 359 497 Coil 2.
REGION 498 637 Tail.
COILED 180 328 {ECO:0000255}.
COILED 397 483 {ECO:0000255}.
COMPBIAS 13 159 Gly-rich.
COMPBIAS 522 621 Gly-rich.
SITE 452 452 Stutter.
MOD_RES 12 12 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 49 49 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 284 284 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 526 526 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 585 585 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 607 607 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VARIANT 194 194 S -> P (in EHK).
{ECO:0000269|PubMed:16528356}.
CONFLICT 99 99 G -> R (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 131 131 L -> S (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 147 147 R -> T (in Ref. 3; BAB31776).
{ECO:0000305}.
CONFLICT 150 151 SM -> GY (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 156 158 PPG -> SPS (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 165 165 I -> L (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 176 176 E -> K (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 214 214 Q -> K (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 261 261 D -> E (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 313 313 A -> R (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 321 321 D -> N (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 325 325 A -> T (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 352 353 SL -> QF (in Ref. 1; AAD05191).
{ECO:0000305}.
CONFLICT 428 428 S -> Y (in Ref. 3; BAB31776).
{ECO:0000305}.
CONFLICT 572 580 Missing (in Ref. 1; AAD05191).
{ECO:0000305}.
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


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