K1C9_RAT
ID K1C9_RAT Reviewed; 618 AA.
AC Q8CIS9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
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;
DE AltName: Full=Spermatid perinuclear ring manchette protein K9;
GN Name=Krt9; Synonyms=Krt1-9 {ECO:0000312|RGD:628785};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN05455.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAN05455.1};
RC TISSUE=Epidermis {ECO:0000269|PubMed:11071770}, and
RC Testis {ECO:0000269|PubMed:11071770};
RX PubMed=11071770; DOI=10.1006/dbio.2000.9911;
RA Mochida K., Rivkin E., Gil M., Kierszenbaum A.L.;
RT "Keratin 9 is a component of the perinuclear ring of the manchette of rat
RT spermatids.";
RL Dev. Biol. 227:510-519(2000).
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). May be involved in spermatid nuclear shaping and sperm
CC development. {ECO:0000250|UniProtKB:P35527,
CC ECO:0000269|PubMed:11071770}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the perinuclear ring of spermatid
CC manchettes within testis and in keratinocytes of the suprabasal layer
CC of footpad epidermis (at protein level). {ECO:0000269|PubMed:11071770}.
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; AY128946; AAN05455.1; -; mRNA.
DR RefSeq; NP_703206.1; NM_153476.1.
DR AlphaFoldDB; Q8CIS9; -.
DR SMR; Q8CIS9; -.
DR STRING; 10116.ENSRNOP00000019330; -.
DR GeneID; 266717; -.
DR KEGG; rno:266717; -.
DR UCSC; RGD:628785; rat.
DR CTD; 3857; -.
DR RGD; 628785; Krt9.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q8CIS9; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; Q8CIS9; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q8CIS9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:RGD.
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; IDA:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
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; PS00226; IF_ROD_1; 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..618
FT /note="Keratin, type I cytoskeletal 9"
FT /id="PRO_0000308373"
FT DOMAIN 138..450
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..137
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..173
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 174..192
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 193..284
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 285..307
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 308..446
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 447..609
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 449..618
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 31..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..618
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 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13645"
SQ SEQUENCE 618 AA; 63009 MW; B0140A0E34E2A28F CRC64;
MSFRQISSSF RSSSGSSCGG GGGRGASRGS MRSSFGRSSR AGGESRFGSS SGFGGGGFSA
CGTGGGGSFG SSYGGGYGRG FSAGSSSGMF GGSSRGCFGG GSGGGFGGGS GGGFGGGFGG
GFGGGSGGGE GSILNTNEKV VMQNLNSRLA SYMDKVQELE EDNANLEKQI QEWYSRKGNR
VFQKDYSHYY NTIEDLKDRI VDLTARNNKA LIDMDNTRMT LGDFRVKLEM EQSLPQGVDA
DINGLQKVLD DINMEKSDLE IQFDSLDDEL KALKKSHKEE MNQLTGLNDG DVNVEINVAP
STDLTQVLND MREEYEHLIS KNRQDIEQHY ESQMTQIEHQ LTNSGPEMET NMKQVSQLQH
SVQELNIELQ TQLTTKSALE KALEDTKNRY CGQLQQIREQ ISEMEAQLAQ VRAETECQNQ
EYGLLLSIKT RLEKEIETYR KLLEGGQQDF ESSGAGQIGF GSGKGGQRGS GGSYGGGSGD
SYEGESGGSY GGGSGGSHGG KSGGSYGGGS SSGGGSGGSY GGGSGGSHGG KSGGSHGGGS
GGSYGGGSGS GGESGGSYGG GSGGSHGGQK GGSGGSYEGG SGGSYGGGSG SGGGSGGSYG
GGNTRPSQSQ SSQIPRLR
