K2C7_MOUSE
ID K2C7_MOUSE Reviewed; 457 AA.
AC Q9DCV7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Keratin, type II cytoskeletal 7;
DE AltName: Full=Cytokeratin-7;
DE Short=CK-7;
DE AltName: Full=Keratin-7;
DE Short=K7;
DE AltName: Full=Type-II keratin Kb7;
GN Name=Krt7 {ECO:0000312|MGI:MGI:96704};
GN Synonyms=Krt2-7 {ECO:0000312|MGI:MGI:96704};
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] {ECO:0000305, ECO:0000312|EMBL:AAN64034.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAN64034.1};
RC TISSUE=Mammary gland {ECO:0000269|PubMed:12359226};
RX PubMed=12359226; DOI=10.1016/s0006-291x(02)02288-x;
RA Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B.,
RA McLean W.H.I.;
RT "Cloning of human, murine, and marsupial keratin 7 and a survey of K7
RT expression in the mouse.";
RL Biochem. Biophys. Res. Commun. 297:818-827(2002).
RN [2] {ECO:0000312|EMBL:BAB22099.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22099.1};
RC TISSUE=Amnion {ECO:0000312|EMBL:BAE27526.1},
RC Kidney {ECO:0000312|EMBL:BAB22099.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAE23275.1};
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 [3] {ECO:0000312|EMBL:AAH30403.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH30403.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH30403.1};
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 [4]
RP PROTEIN SEQUENCE OF 368-387, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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 -!- FUNCTION: Blocks interferon-dependent interphase and stimulates DNA
CC synthesis in cells. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit
CC EIF3S10. Interacts with GPER1 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in most simple epithelia tested including
CC liver, lactating mammary gland, lung, kidney, stomach, duodenum, colon,
CC oviduct, uterus, pancreas, epididymis, prostate, preputial gland and
CC mesothelium, and in most stratified epithelia tested including dorsal
CC skin, paw/toe, tail, tongue, cervix, forestomach, and bladder. Also
CC expressed in Henle layer of the inner root sheath of whisker follicle.
CC {ECO:0000269|PubMed:12359226}.
CC -!- PTM: Arg-15 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250|UniProtKB:P08729}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AF509888; AAN64032.1; -; mRNA.
DR EMBL; AF509890; AAN64034.1; -; Genomic_DNA.
DR EMBL; AK002434; BAB22099.1; -; mRNA.
DR EMBL; AK137217; BAE23275.1; -; mRNA.
DR EMBL; AK146914; BAE27526.1; -; mRNA.
DR EMBL; BC030403; AAH30403.1; -; mRNA.
DR CCDS; CCDS27851.1; -.
DR RefSeq; NP_149064.1; NM_033073.3.
DR AlphaFoldDB; Q9DCV7; -.
DR SMR; Q9DCV7; -.
DR BioGRID; 225484; 4.
DR IntAct; Q9DCV7; 3.
DR MINT; Q9DCV7; -.
DR STRING; 10090.ENSMUSP00000069900; -.
DR iPTMnet; Q9DCV7; -.
DR PhosphoSitePlus; Q9DCV7; -.
DR jPOST; Q9DCV7; -.
DR PaxDb; Q9DCV7; -.
DR PeptideAtlas; Q9DCV7; -.
DR PRIDE; Q9DCV7; -.
DR ProteomicsDB; 268946; -.
DR Antibodypedia; 1535; 2533 antibodies from 57 providers.
DR DNASU; 110310; -.
DR Ensembl; ENSMUST00000068904; ENSMUSP00000069900; ENSMUSG00000023039.
DR GeneID; 110310; -.
DR KEGG; mmu:110310; -.
DR UCSC; uc007xtd.2; mouse.
DR CTD; 3855; -.
DR MGI; MGI:96704; Krt7.
DR VEuPathDB; HostDB:ENSMUSG00000023039; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000161303; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; Q9DCV7; -.
DR OMA; QRSKQEM; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q9DCV7; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 110310; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Krt7; mouse.
DR PRO; PR:Q9DCV7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DCV7; protein.
DR Bgee; ENSMUSG00000023039; Expressed in urinary bladder urothelium and 187 other tissues.
DR ExpressionAtlas; Q9DCV7; baseline and differential.
DR Genevisible; Q9DCV7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 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 Acetylation; Coiled coil; Direct protein sequencing; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CHAIN 2..457
FT /note="Keratin, type II cytoskeletal 7"
FT /id="PRO_0000307635"
FT DOMAIN 85..397
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..84
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 84..120
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 121..138
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 139..230
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 231..254
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 255..393
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 394..457
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 337
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 15
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 15
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
SQ SEQUENCE 457 AA; 50709 MW; D6AD866E4949DEF8 CRC64;
MSIHFSSRST AYPGRGAQVR LSSGRASFGS RSLYGLGSSR PRVAVRSAYG GPVGAGIREI
TINQSLLAPL SVDIDPTIQQ VRQEEREQIK TLNNKFASFI DKVRFLEQQN KMLETKWALL
QEQKSAKSSQ LPRIFEAQIA GLRQQLETLQ LDGGRLEVEL RNMQDVVEDF KNKYEEEINR
RTAAENEFVL LKKDVDAAYT NKVELEAKAD SLQDEINFLK TLHETELAEL QSQISDTSVV
LSMDNSRSLD LDGIIADVKA QYEEMANHSR AEAEAWYQTK FETLQAQAGK HGDDLRNTRN
EIAEMNRSIQ RLQAEIDTLK NQRAKLESSI AEAEEQGELA IKDAHAKQGE LEAALQKAKQ
DVARQLREYQ ELLNTKLALD IEIATYRKLL EGEESRLSGD GMGPVNISVV NSTGGNGGKL
IFGGTMGSNA LSFSGGPGAL RAYSIKTTST TRRGTHN
