ID K2C5_BOVIN Reviewed; 601 AA.
AC Q5XQN5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 08-NOV-2023, entry version 98.
DE RecName: Full=Keratin, type II cytoskeletal 5;
DE AltName: Full=Cytokeratin-5;
DE Short=CK-5;
DE AltName: Full=Keratin-5;
DE Short=K5;
DE AltName: Full=Type-II keratin Kb5;
GN Name=KRT5 {ECO:0000250|UniProtKB:P13647};
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:0000305, ECO:0000312|EMBL:AAU95600.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT EBS LYS-478.
RC STRAIN=Friesian X Jersey {ECO:0000269|PubMed:15955091};
RX PubMed=15955091; DOI=10.1111/j.0022-202x.2005.23610.x;
RA Ford C.A., Stanfield A.M., Spelman R.J., Smits B., Ankersmidt-Udy A.E.,
RA Cottier K., Holloway H., Walden A., Al-Wahb M., Bohm E., Snell R.G.,
RA Sutherland G.T.;
RT "A mutation in bovine keratin 5 causing epidermolysis bullosa simplex,
RT transmitted by a mosaic sire.";
RL J. Invest. Dermatol. 124:1170-1176(2005).
CC -!- FUNCTION: Required for the formation of keratin intermediate filaments
CC in the basal epidermis and maintenance of the skin barrier in response
CC to mechanical stress (By similarity). Regulates the recruitment of
CC Langerhans cells to the epidermis, potentially by modulation of the
CC abundance of macrophage chemotactic cytokines, macrophage inflammatory
CC cytokines and CTNND1 localization in keratinocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q922U2}.
CC -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Heterodimer
CC with type I keratin KRT25 leading to the formation of keratin
CC intermediate filament (KIF) network (By similarity). Forms a
CC heterodimer (via 2B domains) with KRT14 (via 2B domains) (By
CC similarity). Interacts with TCHP (By similarity). Interacts with EPPK1
CC (By similarity). Interacts with AMELX (By similarity). Interacts with
CC PKP1 (via N-terminus) and PKP2 (By similarity).
CC {ECO:0000250|UniProtKB:P13647, ECO:0000250|UniProtKB:Q922U2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q922U2}.
CC -!- PTM: Phosphorylated by CDK1, AURKB and Rho-kinase, phosphorylation is
CC regulated by the cell cycle (By similarity). Thr-24 phosphorylation,
CC mediated by CDK1, peaks during prometaphase or metaphase cells with
CC phosphorylated filamentous structures evident throughout the cytoplasm
CC early mitosis (By similarity). CDK1 phosphorylates Thr-24 in mitotic
CC cells at the site of injury (By similarity).
CC {ECO:0000250|UniProtKB:Q922U2}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q922U2}.
CC -!- DISEASE: Note=Defects in KRT5 are a cause of epidermolysis bullosa
CC simplex [EBS]. EBS leads to loss of skin and mucosa from contact areas
CC and inflammation, due to separation of the epidermis from the dermis.
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AY740402; AAU95600.1; -; Genomic_DNA.
DR RefSeq; NP_001008663.1; NM_001008663.1.
DR AlphaFoldDB; Q5XQN5; -.
DR SMR; Q5XQN5; -.
DR IntAct; Q5XQN5; 1.
DR STRING; 9913.ENSBTAP00000021456; -.
DR PaxDb; 9913-ENSBTAP00000021456; -.
DR PeptideAtlas; Q5XQN5; -.
DR GeneID; 281268; -.
DR KEGG; bta:281268; -.
DR CTD; 3852; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR InParanoid; Q5XQN5; -.
DR OrthoDB; 4640531at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0045107; P:intermediate filament polymerization; ISS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45616:SF32; KERATIN, TYPE II CYTOSKELETAL 5; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Disease variant; Intermediate filament; Keratin;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..601
FT /note="Keratin, type II cytoskeletal 5"
FT /id="PRO_0000063726"
FT DOMAIN 169..482
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..168
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 169..204
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 205..223
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 224..316
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 317..339
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 340..478
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 479..601
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 576..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 420
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 24
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 152
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 167
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT VARIANT 478
FT /note="E -> K (in EBS)"
FT /evidence="ECO:0000269|PubMed:15955091"
SQ SEQUENCE 601 AA; 62937 MW; 62592254B22DE0A2 CRC64;
MSRQSTVSFR SGGGRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS LGGAYGAGGF
GSRSLYNLGG SKRISISASG GGFRNRFGAG AGGGYGFGGG AGSGFGFGGG AGGGGFGLGG
GAGFGGGFGG PGFPVCPPGG IQEVTVNQSL LTPLNLQIDP TIQRVRTEER EQIKTLNNKF
ASFIDKVRFL EQQNKVLDTK WALLQEQGTK TVRQNLEPLL EQYINNLRRQ LDGIVGERGR
LDSELRNMQD LVEDFKNKYE DEINKRTTAE NEFVMLKKDV DAAYMNKVEL EAKVDALMDE
INFMKMFFDA ELSQMQTHVS DTSVVLSMDN NRSLDLDSII AEVKAQYEDI ANRSRTEAES
WYQTKYEELQ QTAGRHGDDL RNTKHEISEM NRMIQRLRSE IDNVKKQCAN LQNAIADAEQ
RGELALKDAR SKLAELEDAL QKAKQDMARL LREYQELMNT KLALDVEIAT YRKLLEGEEC
RLSGEGVGPV NISVVTNTVS SGYGGGSGFG GGLGGGLGGG LGGGLGGGLG GGLGSGLGGG
GSSSFYSSSS GGVGLGGGLS VGGSGFSASS GRSLGFGSGG GSSSSVKFVS TTSSSRKSFK
S
//
