K22E_RAT
ID K22E_RAT Reviewed; 685 AA.
AC Q6IG02;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Keratin, type II cytoskeletal 2 epidermal;
DE AltName: Full=Cytokeratin-2e;
DE Short=CK-2e;
DE AltName: Full=Epithelial keratin-2e;
DE AltName: Full=Keratin-2 epidermis;
DE AltName: Full=Keratin-2e;
DE Short=K2e;
DE AltName: Full=Type-II keratin Kb2;
GN Name=Krt2 {ECO:0000250|UniProtKB:P35908};
GN Synonyms=Kb2 {ECO:0000312|RGD:1303297},
GN Krt2a {ECO:0000250|UniProtKB:P35908};
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:DAA02228.1}
RP IDENTIFICATION.
RX PubMed=15085952; DOI=10.1078/0171-9335-00354;
RA Hesse M., Zimek A., Weber K., Magin T.M.;
RT "Comprehensive analysis of keratin gene clusters in humans and rodents.";
RL Eur. J. Cell Biol. 83:19-26(2004).
CC -!- FUNCTION: Probably contributes to terminal cornification. Associated
CC with keratinocyte activation, proliferation and keratinization (By
CC similarity). Required for maintenance of corneocytes and keratin
CC filaments in suprabasal keratinocytes in the epidermis of the ear,
CC potentially via moderation of expression and localization of keratins
CC and their partner proteins (By similarity). Plays a role in the
CC establishment of the epidermal barrier on plantar skin (By similarity).
CC {ECO:0000250|UniProtKB:P35908, ECO:0000250|UniProtKB:Q3TTY5}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Associates with KRT10. {ECO:0000250|UniProtKB:Q3TTY5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35908}.
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; AABR03055962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK003983; DAA02228.1; -; mRNA.
DR RefSeq; NP_001008899.1; NM_001008899.1.
DR AlphaFoldDB; Q6IG02; -.
DR SMR; Q6IG02; -.
DR STRING; 10116.ENSRNOP00000050471; -.
DR iPTMnet; Q6IG02; -.
DR PhosphoSitePlus; Q6IG02; -.
DR jPOST; Q6IG02; -.
DR PaxDb; Q6IG02; -.
DR PRIDE; Q6IG02; -.
DR GeneID; 406228; -.
DR KEGG; rno:406228; -.
DR UCSC; RGD:1303297; rat.
DR CTD; 3849; -.
DR RGD; 1303297; Krt2.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q6IG02; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q6IG02; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IG02; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR GO; GO:0031424; P:keratinization; ISO:RGD.
DR GO; GO:0032980; P:keratinocyte activation; ISO:RGD.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0051546; P:keratinocyte migration; ISO:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR GO; GO:0045684; P:positive regulation of epidermis development; 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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..685
FT /note="Keratin, type II cytoskeletal 2 epidermal"
FT /id="PRO_0000283764"
FT DOMAIN 197..511
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..196
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..232
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 233..251
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 252..343
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 344..367
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 368..507
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 508..685
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 532..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 449
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 22
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TTY5"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 52
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TTY5"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35908"
FT MOD_RES 554
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TTY5"
FT MOD_RES 588
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TTY5"
FT MOD_RES 603
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 653
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
SQ SEQUENCE 685 AA; 69127 MW; F6F8C0D770C6DF01 CRC64;
MSCQISCKSR RGGGGGGGGG FRGFSSGSAV VSGGSRRSTS GFSCLSRHGG GRGGSGGGGF
GSQSLVGLGG YKSISSSVAG YGGGFGGRSY GGFGGGSGFG GSGGFGGGSG FGGGRGFGGG
SGFGGGSGFG GGSGFGGGSG FGGGGFGGGR FGGGPGGFGG PGGFPGGGIH EVSVNQSLLQ
PLDVKVDPEI QNVKSQEREQ IKTLNNKFAS FIDTVRFLEQ QNQVLHTKWE LLQQLDVGTR
TTNLDPVFQA YIGILKKQVD RLTAERNSQD SELNNMQDLV EDFKKKYEDE INKRTSAEND
FVTIKKDVDS CYMDKTELQA KMEMLTQEVD FLRTLYDTEL SQLQQNVTDT NVILSMDNNR
NLDLDSIIAE VQSQYEIIAH KSKAESEELY HSKANEELQV TAVKHGDSLK EIKMEISELN
RTIQRLQGEI SHVKKQCKGV QDSIADAEQR GEHAIKDARG KLTDLEEALQ QGRENLARLL
RDYQELMNVK LALDVEIATY RKLLEGEECR MSGDFSDNVS VSVTSSTISS SVASKAGFGS
GGQSSGGRGS YGGRGGGSTY GSGGRSSGVR GSGSGSGGGG YSSGGGSRGG SGGGGYSTGG
GSRGGSSSGG GGYSSGGGSR GDSSSGGGSR GGSGGGSRGG SGGGGYSSGG GSRGGSSSGG
AVSGSERGGS GSGEGCGSGV TFSFR
