K22E_CANLF
ID K22E_CANLF Reviewed; 633 AA.
AC Q6EIZ1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; Synonyms=K2E {ECO:0000312|EMBL:AAQ83908.1}, KRT2A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000312|EMBL:AAQ83908.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis {ECO:0000269|PubMed:15627753};
RX PubMed=15627753; DOI=10.1159/000081527;
RA Credille K.M., Guyon R., Andre C., Murphy K., Tucker K., Barnhart K.F.,
RA Dunstan R.W.;
RT "Comparative sequence analysis and radiation hybrid mapping of two
RT epidermal type II keratin genes in the dog: keratin 1 and keratin 2e.";
RL Cytogenet. Genome Res. 108:328-332(2005).
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; AY318943; AAQ83908.1; -; mRNA.
DR STRING; 9612.ENSCAFP00000010729; -.
DR PaxDb; Q6EIZ1; -.
DR PRIDE; Q6EIZ1; -.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q6EIZ1; -.
DR Proteomes; UP000002254; 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:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Intermediate filament; Keratin; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..633
FT /note="Keratin, type II cytoskeletal 2 epidermal"
FT /id="PRO_0000283762"
FT DOMAIN 190..503
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..189
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 190..225
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 226..244
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 245..336
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 337..360
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 361..499
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 500..633
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 518..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 441
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3TTY5"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35908"
FT MOD_RES 588
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 612
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
SQ SEQUENCE 633 AA; 64567 MW; 445D509166A23CB1 CRC64;
MSCQISCKSR IGGGGGFRSF SSGSAVVSGG SRRSTRSFSC LSRHGGGGGG AGGGGFGSRS
LVGLGGTKSI SISVAGGGGS FGSGGGFGGR GGGFGGGSGF GGGSGFGGGG FGGGGFGGGS
GFGGGGFGGG GFGGGRFGGG GGLGGFGGPG GFGPGGFPGG GIHEVSINES LLQPLNVKVD
PEIQNVKSQE REQIKTLNNK FASFIDKVRF LEQQNQVLQT KWELLQQLDV STRTTNLEPI
FQAYIAKLKK YVDTLSAERT SQGSELNNMQ DLVEDFKKKY EDEINKRTAA ENDFVTLKKD
VDNNYMTKVE LQAKTDVLTQ ELEFIKFLFD XELSQMQTQI SETNVTLSMD NNRSLDLDSI
ISEVKAQYEE IAQKSKAEAE ALYHSKYEEL QVTAGKHGDS LKEVKMEISE LNRMIQRLQG
EIAHVKKQCK SVQEAIAEAE QKGEHAVKDA QGKLSDLEEA LQQAREDLAG LLRDYQELMN
VKLALDVEIA TYRKLLEGEE CRMSGDLSSN VTVSVTSSSM SSSMTSRGGF GGYGSGGRGS
SSGGGGFSSG SGSYSSGGRG SSSRGGGGGG YGSGGGSGGK YSSGGGSRGG SGSGGGYGSS
SGGGYGSGGG SRGGFSSQKG GSGSGSSVTF SFR
