K2C5_RAT
ID K2C5_RAT Reviewed; 576 AA.
AC Q6P6Q2; Q7TN97;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN Synonyms=Krt2-5 {ECO:0000312|EMBL:AAH62086.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ20893.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAQ20893.1};
RX PubMed=14551252; DOI=10.1091/mbc.e03-04-0226;
RA Kierszenbaum A.L., Rivkin E., Tres L.L.;
RT "Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to
RT the nucleus during shaping of the spermatid head.";
RL Mol. Biol. Cell 14:4628-4640(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-8; SER-16; SER-21;
RP SER-36; SER-60; SER-67; SER-71; SER-74 AND SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Expressed in the epidermis (at protein level) and
CC testis (within pachytene spermatocytes). {ECO:0000269|PubMed:14551252}.
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; AY342389; AAQ20893.1; -; mRNA.
DR EMBL; BC062086; AAH62086.1; -; mRNA.
DR RefSeq; NP_899162.1; NM_183333.1.
DR AlphaFoldDB; Q6P6Q2; -.
DR SMR; Q6P6Q2; -.
DR BioGRID; 266785; 2.
DR STRING; 10116.ENSRNOP00000011644; -.
DR iPTMnet; Q6P6Q2; -.
DR PhosphoSitePlus; Q6P6Q2; -.
DR jPOST; Q6P6Q2; -.
DR PaxDb; Q6P6Q2; -.
DR PRIDE; Q6P6Q2; -.
DR Ensembl; ENSRNOT00000011644; ENSRNOP00000011644; ENSRNOG00000050420.
DR GeneID; 369017; -.
DR KEGG; rno:369017; -.
DR CTD; 3852; -.
DR RGD; 727894; Krt5.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000160458; -.
DR InParanoid; Q6P6Q2; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q6P6Q2; -.
DR Reactome; R-RNO-446107; Type I hemidesmosome assembly.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6P6Q2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..576
FT /note="Keratin, type II cytoskeletal 5"
FT /id="PRO_0000063729"
FT DOMAIN 164..477
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..163
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 164..199
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 200..218
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 219..311
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 312..334
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 335..473
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 474..576
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 540..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 413
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 162
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT MOD_RES 527
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q922U2"
FT CONFLICT 114
FT /note="G -> R (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="E -> Q (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="S -> F (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="R -> L (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> Q (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="K -> N (in Ref. 1; AAQ20893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 61826 MW; 23A1C2C47405EE3B CRC64;
MSRQSSVSFR SGGSRSFSAA SAITPSVSRT TFSSVSRSGG GGGRVSLGGA YGAGGYGSRS
LYNVGGSKRI SFSSGGGSFR NQFGAGAGGG YGFGGGAGSG FGFGGGAGSG FGFGGGAGFG
GGYGGAGFPV CPPGGIQEVT VNQNLLTPLN LQIDPTIQRV RTEEREQIKT LNNKFASFID
KVRFLEQQNK VLDTKWTLLQ EQGTKTIKQN LDPLFEQYIN NLRRQLDGVM GERGRLDSEL
RNMQDLVEDY KNKYEDEINK RTTAENEFVM LKKDVDAAYM NKVELEAKVD ALMDEINFMK
MFFDAELSQM QTHVSDTSVV LSMDNNRSLD LDSIIAEVKA QYEDIANRSR TEAESWYQTK
YEELQQTAGR HGDDLRNTKH EISEMNRMIQ RLRSEIDNVK KQCANLQNAI AEAEQRGELA
LKDARNKLTE LEEALQKAKQ DMARLLREYQ ELMNTKLALD VEIATYRKLL EGEECRLSGE
GVGPVNISVV TNSLSSGYGG RSNIGYGSGL GSGIGGFASD IGPLLNRRGL GSGLSVGGSG
FSASSGQGGG FSSGGGSSSS VKFVSTTSSS RRSFKS
