K2C7_BOVIN
ID K2C7_BOVIN Reviewed; 466 AA.
AC Q29S21;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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:AAI13215.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI13215.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI13215.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAI13215.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC113214; AAI13215.1; -; mRNA.
DR RefSeq; NP_001039876.1; NM_001046411.1.
DR AlphaFoldDB; Q29S21; -.
DR SMR; Q29S21; -.
DR STRING; 9913.ENSBTAP00000021516; -.
DR PaxDb; Q29S21; -.
DR PeptideAtlas; Q29S21; -.
DR PRIDE; Q29S21; -.
DR Ensembl; ENSBTAT00000021516; ENSBTAP00000021516; ENSBTAG00000016165.
DR GeneID; 535697; -.
DR KEGG; bta:535697; -.
DR CTD; 3855; -.
DR VEuPathDB; HostDB:ENSBTAG00000016165; -.
DR VGNC; VGNC:30734; KRT7.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000161303; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; Q29S21; -.
DR OMA; QRSKQEM; -.
DR OrthoDB; 824246at2759; -.
DR TreeFam; TF317854; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016165; Expressed in parenchyma of mammary gland and 85 other tissues.
DR ExpressionAtlas; Q29S21; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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..466
FT /note="Keratin, type II cytoskeletal 7"
FT /id="PRO_0000307634"
FT DOMAIN 92..404
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..91
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 91..127
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 128..145
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 146..237
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 238..261
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 262..400
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 401..466
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 344
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 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 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 180
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08729"
SQ SEQUENCE 466 AA; 51578 MW; 4663001F60907BBD CRC64;
MSLHFGSQVF SSRSAAFPGR GTQVRLSSVR PGGFGSSSSL YGLGASRPRV AARSSYGAPV
GTGIRAVTIN QSLLTPLQVD IDPSIQQVRQ EEREQIKTLN NKFASFIDKV RFLEQQNKLL
ETKWALLQEQ KSAKSNRLPG IFEAQIAGLR KQLEALQLDG GRLEVELRNM QDVVEDFKNK
YEDEINHRTA AENEFVVLKK DVDVAYMNKV ELEAKVDTLN DEINFLRTLY EQELKELQSE
VSDTSVVLSM DNNRSLDLDS IIAEVKAQYE EIANRSRAEA EACYQTKFET LQAQAGKHGD
DLQNTRNEIA DMNRAVQRLQ AEIDSVKNQR SKLEAAIADA EQRGELAVKD ARAKQEDLEA
ALQKAKQDMT RQLREYQELM NVKLALDIEI ATYRKLLEGE ESRLTGDGVG AVNISVVSST
GGSGSLLTFG GTMGNNALRF SSGGGPGTLK AYSMRTTSAT SRSPRK
