K2C1B_MOUSE
ID K2C1B_MOUSE Reviewed; 572 AA.
AC Q6IFZ6;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Keratin, type II cytoskeletal 1b;
DE AltName: Full=Cytokeratin-1B;
DE Short=CK-1B;
DE AltName: Full=Embryonic type II keratin-1;
DE AltName: Full=Keratin-77;
DE Short=K77;
DE AltName: Full=Type-II keratin Kb39;
GN Name=Krt77; Synonyms=Krt1b;
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}
RP PROTEIN SEQUENCE OF 187-198, 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 [3] {ECO:0000305, ECO:0000312|EMBL:DAA05633.1}
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION, AND CITRULLINATION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:DAA05633.1};
RC TISSUE=Epidermis {ECO:0000312|EMBL:DAA05633.1};
RX PubMed=15619433; DOI=10.1016/j.jdermsci.2004.07.003;
RA Senshu T., Ishida-Yamamoto A., Takahashi H., Iizuka H.;
RT "Prediction of a coding sequence for a novel type II keratin from N-
RT terminal sequences of mouse epidermal proteins site-specifically deiminated
RT in embryonic development.";
RL J. Dermatol. Sci. 37:41-48(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA02234.1}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Pancreas;
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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-81; ARG-99; ARG-526 AND ARG-542,
RP 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).
CC -!- TISSUE SPECIFICITY: Expressed in stratified epithelia.
CC {ECO:0000269|PubMed:15085952}.
CC -!- PTM: Undergoes deimination of some arginine residues (citrullination).
CC {ECO:0000269|PubMed:15619433}.
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; CAAA01098975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01098987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK005256; DAA05633.1; -; mRNA.
DR EMBL; BK003993; DAA02234.1; -; mRNA.
DR CCDS; CCDS27865.1; -.
DR RefSeq; NP_001003667.1; NM_001003667.1.
DR AlphaFoldDB; Q6IFZ6; -.
DR SMR; Q6IFZ6; -.
DR BioGRID; 240430; 17.
DR STRING; 10090.ENSMUSP00000085311; -.
DR iPTMnet; Q6IFZ6; -.
DR PhosphoSitePlus; Q6IFZ6; -.
DR jPOST; Q6IFZ6; -.
DR PaxDb; Q6IFZ6; -.
DR PRIDE; Q6IFZ6; -.
DR ProteomicsDB; 269146; -.
DR Antibodypedia; 51312; 609 antibodies from 23 providers.
DR DNASU; 406220; -.
DR Ensembl; ENSMUST00000087996; ENSMUSP00000085311; ENSMUSG00000067594.
DR GeneID; 406220; -.
DR KEGG; mmu:406220; -.
DR UCSC; uc007xud.1; mouse.
DR CTD; 374454; -.
DR MGI; MGI:3588209; Krt77.
DR VEuPathDB; HostDB:ENSMUSG00000067594; -.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR GeneTree; ENSGT00940000162397; -.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; Q6IFZ6; -.
DR OMA; VGSVCHA; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q6IFZ6; -.
DR TreeFam; TF317854; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 406220; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Krt77; mouse.
DR PRO; PR:Q6IFZ6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6IFZ6; protein.
DR Bgee; ENSMUSG00000067594; Expressed in mammary bud and 47 other tissues.
DR ExpressionAtlas; Q6IFZ6; baseline and differential.
DR Genevisible; Q6IFZ6; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005856; C: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 Citrullination; Coiled coil; Direct protein sequencing;
KW Intermediate filament; Keratin; Methylation; Reference proteome.
FT CHAIN 1..572
FT /note="Keratin, type II cytoskeletal 1b"
FT /id="PRO_0000063712"
FT DOMAIN 167..480
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..166
FT /note="Head"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..202
FT /note="Coil 1A"
FT REGION 203..221
FT /note="Linker 1"
FT REGION 222..313
FT /note="Coil 1B"
FT REGION 314..337
FT /note="Linker 12"
FT REGION 338..476
FT /note="Coil 2"
FT REGION 477..568
FT /note="Tail"
FT REGION 495..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 420
FT /note="Stutter"
FT MOD_RES 81
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 99
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 526
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 542
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 572 AA; 61359 MW; 4D6A8BEC8E250096 CRC64;
MSRQFSSQSA FSSRSRRAYS SRSSSGFGGG RQALVSVSQS RRYGGDYGGG FSSRSLYSLG
GSKSIFGNLV GRSASGFCQS RGPGGGFGGG IGGGIGGGRG FGGGGFGGGY GGGGRFGGGF
GGAGFGFGGF GPSYPPGGIH EVTINQSLLE PLHLEVDPEI QRVKTQEREQ IKTLNNKFAS
FIDKVRFLEQ QNQVLQTKWE LLQQVNTSTR TSSLEPVFEE FISQLQRQVD VLTTEQLRQN
TEIRNMQDVV EDYKNKYEDE INKRTNAEND FVVLKKDVDA AFMGKSDLQS KVDTLYGEIN
FLKYLFDTEL SQIQTHVSDT NVILSMDNNR SLDLDSIIDA VRAQYEIIAQ KSKDEAEALY
QTKYQELQIT AGKHGDDLKN SKMEISELNR NIQRLRAEIA NIKKQVEGMH GLISDAEERG
ERALQNAKQK LQDMEEALQQ AKEDLAKLLR DYQAMLGAKL SLDVEIATYR QLLEGEESRM
SGALQSQVSI SVQSSQVTIG GGGGGSGSYS GSSRGGGGGG GGTGSRGGGG GGGGSSYVSS
SRSATKYGSG GGSSRTQILQ TSTHSSRRHV VE
