K2C5_PANTR
ID K2C5_PANTR Reviewed; 592 AA.
AC A5A6M8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
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;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
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: 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).
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 during early mitosis (By similarity). CDK1 phosphorylates Thr-24 in
CC mitotic cells at the site of injury (By similarity).
CC {ECO:0000250|UniProtKB:Q922U2}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q922U2}.
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; AB222156; BAF62401.1; -; mRNA.
DR RefSeq; NP_001266996.1; NM_001280067.1.
DR AlphaFoldDB; A5A6M8; -.
DR SMR; A5A6M8; -.
DR PRIDE; A5A6M8; -.
DR GeneID; 100615215; -.
DR KEGG; ptr:100615215; -.
DR CTD; 3852; -.
DR InParanoid; A5A6M8; -.
DR OrthoDB; 824246at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0045107; P:intermediate filament polymerization; ISS:UniProtKB.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
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 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 Coiled coil; Cytoplasm; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..592
FT /note="Keratin, type II cytoskeletal 5"
FT /id="PRO_0000356826"
FT DOMAIN 170..483
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..169
FT /note="Head"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..205
FT /note="Coil 1A"
FT REGION 206..224
FT /note="Linker 1"
FT REGION 225..317
FT /note="Coil 1B"
FT REGION 318..340
FT /note="Linker 12"
FT REGION 341..479
FT /note="Coil 2"
FT REGION 480..592
FT /note="Tail"
FT REGION 568..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 421
FT /note="Stutter"
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 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6Q2"
FT MOD_RES 153
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 168
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
SQ SEQUENCE 592 AA; 62538 MW; 4EC68886890D89BD CRC64;
MSRQSSVSFR SGGSRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS LGGACGVGGY
GSRSLYNLGG SKWISISTSG GSFRNRFGAG AGAGGGYGFG GGAGSGFGFG GGAGGGFGLG
GGAGFGGGYG GPGFPVCPPG GIQEVTVNQS LLTPLNLQID PSIQRVRTEE REQIKTLNNK
FASFIDKVRF LEQQNKVLDT KWTLLQEQGT KTVRQNLEPL FEQYINNLRR QLDSIVGERG
RLDSELRNMQ DLVEDFKNKY EDEINKRTTA ENEFVMLKKD VDAAYMNKVE LEAKVDALMD
EINFMKMFFD AELSQMQTHV SDTSVVLSMD NNRNLDLDSI IAEVKAQYEE IANRSRTEAE
SWYQTKYEEL QQTAGRHGDD LRNTKHEISE MNRMIQRLRA EIDNVKKQCA NLQNAIADAE
QRGELALKDA RNKLAELEEA LQKAKQDMAR LLREYQELMN TKLALDVEIA TYRKLLEGEE
CRLSGEGVGP VNISVVTSSV SSGYGSGSGY GGGLGGGLGG GLGGSLAGGG SGSYYSSSSG
GVGLGGGLSV GGSGFSASSG RGLGVGFGSG GGSSSSVKFV STTSSSRKSF KS
