K1C9_MOUSE
ID K1C9_MOUSE Reviewed; 743 AA.
AC Q6RHW0; A2A4G3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Keratin, type I cytoskeletal 9;
DE AltName: Full=Cytokeratin-9;
DE Short=CK-9;
DE AltName: Full=Keratin-9;
DE Short=K9;
GN Name=Krt9 {ECO:0000312|MGI:MGI:96696};
GN Synonyms=K9 {ECO:0000312|EMBL:AAR89518.1},
GN Krt1-9 {ECO:0000312|MGI:MGI:96696};
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:0000312|EMBL:AAR89518.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAR89518.1};
RX PubMed=16015579; DOI=10.1002/mrd.20335;
RA Rivkin E., Eddy E.M., Willis W.D., Goulding E.H., Suganuma R.,
RA Yanagimachi R., Kierszenbaum A.L.;
RT "Sperm tail abnormalities in mutant mice with neo(r) gene insertion into an
RT intron of the keratin 9 gene.";
RL Mol. Reprod. Dev. 72:259-271(2005).
RN [2]
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).
CC -!- FUNCTION: May serve an important special function either in the mature
CC palmar and plantar skin tissue or in the morphogenetic program of the
CC formation of these tissues. Plays a role in keratin filament assembly
CC (By similarity). Plays an essential role in the correct development of
CC sperm. {ECO:0000250|UniProtKB:P35527, ECO:0000269|PubMed:16015579}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in footpad epidermis and testis (at
CC protein level). {ECO:0000269|PubMed:16015579}.
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; AY497550; AAR89518.1; -; mRNA.
DR EMBL; GL456158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25412.1; -.
DR RefSeq; NP_957707.2; NM_201255.2.
DR AlphaFoldDB; Q6RHW0; -.
DR SMR; Q6RHW0; -.
DR BioGRID; 223461; 5.
DR IntAct; Q6RHW0; 1.
DR STRING; 10090.ENSMUSP00000055255; -.
DR iPTMnet; Q6RHW0; -.
DR PhosphoSitePlus; Q6RHW0; -.
DR EPD; Q6RHW0; -.
DR PaxDb; Q6RHW0; -.
DR PRIDE; Q6RHW0; -.
DR ProteomicsDB; 269054; -.
DR Antibodypedia; 1544; 209 antibodies from 28 providers.
DR DNASU; 107656; -.
DR Ensembl; ENSMUST00000059707; ENSMUSP00000055255; ENSMUSG00000051617.
DR GeneID; 107656; -.
DR KEGG; mmu:107656; -.
DR UCSC; uc007lkn.1; mouse.
DR CTD; 3857; -.
DR MGI; MGI:96696; Krt9.
DR VEuPathDB; HostDB:ENSMUSG00000051617; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR GeneTree; ENSGT00940000162894; -.
DR HOGENOM; CLU_012560_8_3_1; -.
DR InParanoid; Q6RHW0; -.
DR OMA; TNEKSAM; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q6RHW0; -.
DR TreeFam; TF332742; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 107656; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q6RHW0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6RHW0; protein.
DR Bgee; ENSMUSG00000051617; Expressed in undifferentiated genital tubercle and 10 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..743
FT /note="Keratin, type I cytoskeletal 9"
FT /id="PRO_0000308372"
FT DOMAIN 131..443
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..130
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..166
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 167..185
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 186..277
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 278..300
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 301..439
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 440..709
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 440..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
FT CONFLICT 226
FT /note="S -> T (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> N (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> P (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="R -> Q (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="Q -> H (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="M -> V (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="S -> T (in Ref. 1; AAR89518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 72495 MW; C1A44B4FE65A4B5A CRC64;
MSCRQSSSSF WSSSSSCGGG GGRGGSGGSM RSSFSRSSRA GGGGGGRFNS SSGFSGGGFS
ACGGGGGGSF GSSYGGGYGG GFSTGSYSGM FGGGSGGGFG GGSGGGFGGG SGGGFGGGSG
GGEGGILNTN EKIVMQNLNS RLASYMEKVL ELEESNTAME KQIQDWYSKR GPKVFQKDNT
HYYDTIEDLK DRIVDLTVRN NKTLVDIDNT RMTMDDFRVK LEMEQSLRQG VEGDINGLKK
VLDDLVMAKS DLEILLDSLE DEKNALTKNH KEEMSQLTGQ NDGDVNVEIN VAPSTDLTRV
LNDMREEYEQ LISKNRQDIE QHYESKMTQI EQQMTNSGQE MESNMKQVSQ LQHTIQELNV
ELQTQLTTKS ALEKALEDTK NRYCGQLQQI QEQISELEAQ LAEIRAETEC QSQEYSILLS
IKTRLEKEIE TYRELLEGGQ QDFESSGAGQ IGFGSGKGRQ RGSGGSYGGG SGGSYGGGSG
GSYGGGSGGS YGGGSGGSYG GGSGGSHGGK SGGSHGGGSG GSYGGESGGS HGGGSGGSYG
GGSGGSHGGK SGGGYGGGSS SGGGSGGSYG GGSGGSHGGG SGGSYGGGSG GSHGGKSGGG
YGGGSSSGGG SGGSYGGGSG GSHGGKSGGS YGGGSGGSYG GGSGGSHGGK SGGGYGGGSS
SGGGSGGSYG GGSGGSHGGK SGGSYGGGSS SGGGSGGSYG GGSGSGGGSG GSYGGGNRRP
SQSQSSSKSA DCDDDSQEHK MRY
