K2C74_MOUSE
ID K2C74_MOUSE Reviewed; 495 AA.
AC Q6IFZ9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Keratin, type II cytoskeletal 74 {ECO:0000250|UniProtKB:Q7RT57};
DE AltName: Full=Keratin-74 {ECO:0000250|UniProtKB:Q7RT57};
DE Short=K74;
DE AltName: Full=Type-II keratin Kb37;
GN Name=Krt74 {ECO:0000312|MGI:MGI:3629975};
GN Synonyms=Kb37 {ECO:0000303|PubMed:15085952};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:DAA02231.1}
RP IDENTIFICATION.
RX PubMed=15085952; DOI=10.1078/0171-9335-00354;
RA Hesse M., Zimek A., Weber K., Magin T.M.;
RT "Comprehensive analysis of keratin gene clusters in humans and rodents.";
RL Eur. J. Cell Biol. 83:19-26(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=24714551; DOI=10.1371/journal.pone.0093607;
RA Raykova D., Klar J., Azhar A., Khan T.N., Malik N.A., Iqbal M., Tariq M.,
RA Baig S.M., Dahl N.;
RT "Autosomal recessive transmission of a rare KRT74 variant causes hair and
RT nail ectodermal dysplasia: allelism with dominant woolly
RT hair/hypotrichosis.";
RL PLoS ONE 9:E93607-E93607(2014).
CC -!- FUNCTION: Has a role in hair formation. Specific component of keratin
CC intermediate filaments in the inner root sheath (IRS) of the hair
CC follicle (By similarity). {ECO:0000250|UniProtKB:Q7RT57}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermis with a particularly strong
CC staining in the nail matrix, nail bed and hyponychium (at protein
CC level). {ECO:0000269|PubMed:24714551}.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC respectively). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AC104862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK003986; DAA02231.1; -; mRNA.
DR AlphaFoldDB; Q6IFZ9; -.
DR SMR; Q6IFZ9; -.
DR STRING; 10090.ENSMUSP00000085335; -.
DR iPTMnet; Q6IFZ9; -.
DR PhosphoSitePlus; Q6IFZ9; -.
DR jPOST; Q6IFZ9; -.
DR PaxDb; Q6IFZ9; -.
DR PeptideAtlas; Q6IFZ9; -.
DR PRIDE; Q6IFZ9; -.
DR ProteomicsDB; 269056; -.
DR MGI; MGI:3629975; Krt74.
DR eggNOG; ENOG502RNQG; Eukaryota.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; Q6IFZ9; -.
DR PhylomeDB; Q6IFZ9; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFZ9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6IFZ9; protein.
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 3: Inferred from homology;
KW Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..495
FT /note="Keratin, type II cytoskeletal 74"
FT /id="PRO_0000361694"
FT DOMAIN 106..419
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..105
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 106..141
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 142..160
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 161..252
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 253..276
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 277..415
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 416..495
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 449..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 357
FT /note="Stutter"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 54747 MW; 2B18AD0113BFE3F9 CRC64;
MASCHTAGHR TGLSSRSLYS LGGNQHTSYN VAGGSARGTR HSFGYGYGGG RGSGFANSMF
GSMALGANCP SVCLSGGIYQ VTVNKSLLAP LNVELDPEIQ KVRAQEREQI KALNDKFASF
IDKVRFLEQQ NQVLQTKWEL LQQLDLSNCR RNLEPVYEAH ISNLRKQLEM LSGERVRLDP
DLRKMRDVVE DYKKRYEVEI TQRTAAENEF VLLKKDADAA YTVKVELQDK VDSLDKDIKF
LKCLYDEEIS QLQTHASETS VILSMDNNRD LDLAGIIAEV RAHYEDIALK SKAEAEMLYQ
TKIQELQLAA GCYGDSLKHI RSEMLELDRL IQRIRCDIAN VKKQCSNLEM AIADAEQRGD
SALKDAWAKL DELEGALQQA KEELARMLCE YQELMGLKLS LDVEIATYRK LLEGEENRMS
GENPSSVSVS VISSSCGSCG YHPSSMISDS EAGNAVGSPS TPRNSQSKTR GSSVDPRDAQ
DESAAAAGTL ARKTT
