K2C7_PANTR
ID K2C7_PANTR Reviewed; 469 AA.
AC A5A6N0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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:0000312|EMBL:BAF62403.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1] {ECO:0000312|EMBL:BAF62403.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:BAF62403.1};
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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; AB222158; BAF62403.1; -; mRNA.
DR RefSeq; NP_001104284.1; NM_001110814.1.
DR AlphaFoldDB; A5A6N0; -.
DR SMR; A5A6N0; -.
DR STRING; 9598.ENSPTRP00000008481; -.
DR PaxDb; A5A6N0; -.
DR PRIDE; A5A6N0; -.
DR GeneID; 466983; -.
DR KEGG; ptr:466983; -.
DR CTD; 3855; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR InParanoid; A5A6N0; -.
DR OrthoDB; 824246at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Intermediate filament; Isopeptide bond; Keratin;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CHAIN 2..469
FT /note="Keratin, type II cytoskeletal 7"
FT /id="PRO_0000307636"
FT DOMAIN 91..403
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..90
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 90..126
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 127..144
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 145..236
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 237..260
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 261..399
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 400..469
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 343
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 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
SQ SEQUENCE 469 AA; 51414 MW; 66DD245C9DA2DBD9 CRC64;
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA VRSAYGGPVG
AGIREVTINQ SLLAPLRLDA DPSLQRVRQE EREQIKTLNN KFASFIDKVR FLEQQNKLLE
TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG QLEALQVDGG RLEAELQSMQ DVVEDFKNKY
EDEINRRAAA ENEFVVLKKD VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI
SDTSVVLSMD NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD
LRNTRNEISE MNRAIQRLQA EIDNIKDQRA KLEAAIAEAE ERGELALKDA RAKQEELEAA
LQRAKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE SRLAGDGVGA VNISVMNSTG
GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG PLKAYSIRTA SASRRSARN
