K2C7_POTTR
ID K2C7_POTTR Reviewed; 483 AA.
AC Q8HZR5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 73.
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:0000250|UniProtKB:P08729};
OS Potorous tridactylus (Potoroo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Potoroidae; Potorous.
OX NCBI_TaxID=9310;
RN [1] {ECO:0000312|EMBL:AAN64033.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney epithelium {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).
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 -!- PTM: Arg-20 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; AF509889; AAN64033.1; -; mRNA.
DR AlphaFoldDB; Q8HZR5; -.
DR SMR; Q8HZR5; -.
DR PRIDE; Q8HZR5; -.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Intermediate filament; Isopeptide bond; Keratin;
KW Methylation; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CHAIN 2..483
FT /note="Keratin, type II cytoskeletal 7"
FT /id="PRO_0000307637"
FT DOMAIN 108..420
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..107
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 14..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..143
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 144..161
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 162..253
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 254..277
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 278..416
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 417..483
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 360
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 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 20
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 20
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
SQ SEQUENCE 483 AA; 53286 MW; E3632B3267517BCE CRC64;
MSVQFSSQTF SSRSAAFPRR GGQGRLSSVS SRAGSVSQMG GFGSSSLYGL GSGRPRVSVG
FRSAYGGSSG GGFGARGAGL QEVTINQSLL APLNLEIDPQ IQQVRKEERE QIKTLNNKFA
SFIDKVRFLE QQNQMLETKW RLLQEQKSSK GSSLPAIFEA HIANLRRQLD GLQGDRGRLE
GELKNMQDVV EDFKNKYEGE INKRTAAENE FVVLKKDVDN AYMNKVELEA KVDGLTDEIN
FLRTLYEMEL NELQTQISDT SVVLSMDNSR SLDLDSIISE VKAQYEDIAN RSRAEAEYQY
QIKFETLQAQ AGKHGEDLRS TRNEISEMNR AIQRLQAEID NVKNQRTKLE ASIAEAEERG
ELALKDARAK QEELEAALQR SKQERARQVR EYQDLLNVKL ALDIEIATYR KLLEGEESRL
SGDGVGAVNI SVVNSVGGSL GGGVSLGGTM GGNALGFSSG TGSTIFKTYS TRTTSSSRRS
VRN
