K2C8_BOVIN
ID K2C8_BOVIN Reviewed; 478 AA.
AC P05786; Q3SYX7;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Keratin, type II cytoskeletal 8;
DE AltName: Full=Cytokeratin-8;
DE Short=CK-8;
DE AltName: Full=Cytokeratin-A;
DE AltName: Full=Keratin-8;
DE Short=K8;
DE AltName: Full=Type-II keratin Kb8;
GN Name=KRT8;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-478, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Urinary bladder;
RX PubMed=2422084; DOI=10.1111/j.1432-0436.1986.tb00788.x;
RA Magin T.M., Jorcano J.L., Franke W.W.;
RT "Cytokeratin expression in simple epithelia. II. cDNA cloning and sequence
RT characteristics of bovine cytokeratin A (no. 8).";
RL Differentiation 30:254-264(1986).
CC -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC to dystrophin at the costameres of striated muscle. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Forms a heterodimer with KRT18 (By similarity). Associates
CC with KRT20 (By similarity). Interacts with PNN (By similarity). When
CC associated with KRT19, interacts with DMD (By similarity). Interacts
CC with TCHP (By similarity). Interacts with APEX1 (By similarity).
CC Interacts with GPER1 (By similarity). Interacts with EPPK1 (By
CC similarity). {ECO:0000250|UniProtKB:P05787,
CC ECO:0000250|UniProtKB:P11679, ECO:0000250|UniProtKB:Q10758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q10758}.
CC -!- TISSUE SPECIFICITY: Expressed in bladder, liver, exocervix and (in very
CC low amounts) esophagus. {ECO:0000269|PubMed:2422084}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early embryonal epithelia.
CC {ECO:0000269|PubMed:2422084}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
CC solubility, and decreases stability by inducing proteasomal degradation
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
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; BC103339; AAI03340.1; -; mRNA.
DR EMBL; K03532; AAA30598.1; -; mRNA.
DR EMBL; X12877; CAA31370.1; -; mRNA.
DR PIR; A25004; A25004.
DR RefSeq; NP_001028782.1; NM_001033610.1.
DR AlphaFoldDB; P05786; -.
DR SMR; P05786; -.
DR STRING; 9913.ENSBTAP00000001108; -.
DR PaxDb; P05786; -.
DR PeptideAtlas; P05786; -.
DR PRIDE; P05786; -.
DR GeneID; 281269; -.
DR KEGG; bta:281269; -.
DR CTD; 3856; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR InParanoid; P05786; -.
DR OrthoDB; 824246at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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 Acetylation; Coiled coil; Cytoplasm; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..478
FT /note="Keratin, type II cytoskeletal 8"
FT /id="PRO_0000063739"
FT DOMAIN 98..409
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..97
FT /note="Head"
FT REGION 16..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..133
FT /note="Coil 1A"
FT REGION 134..150
FT /note="Linker 1"
FT REGION 151..242
FT /note="Coil 1B"
FT REGION 243..266
FT /note="Linker 12"
FT REGION 267..405
FT /note="Coil 2"
FT REGION 268..389
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250"
FT REGION 406..478
FT /note="Tail"
FT SITE 349
FT /note="Stutter"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 23
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 48
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 81
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 108
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 235
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 302
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 332
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11679"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05787"
FT CONFLICT 254
FT /note="E -> S (in Ref. 2; AAA30598)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="E -> R (in Ref. 2; AAA30598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53627 MW; 9CDA9DE5CDE9BC35 CRC64;
MSIRVTQKSY KVSTSAPRSF SSRSYTSGPG SRISSSAFSR VGSSSSFRGG LGTGMSMAGS
YGGAPGLGGI TAVTVNQSLL SPLKLEVDPN IQAVRTQEKE QIKTLNNKFA SFIDKVRHLE
QQNKVLETKW NLLQQQKTAR SNIDNMFESY INNLRRQLET LAQEKLKLEV ELGNMQGLVE
DFKTKYEDEI QKRTDMENEF VIIKKDVDEA YMNKVELESR LEGLTDEINF YRQLYEEEIR
EMQSQISDTS VVLEMDNNRN LDLDGIIAEV KAQYEEIANR SRAEAEAMYQ IKYEELQTLA
GKHGDDLRRT KTEISEMNRN INRLQAEIEG LKGQRASLEA AIADAEQRGE MAVKDAQAKL
AELEAALRNA KQDMARQLRE YQELMNVKLA LDVEIATYRK LLEGEESRLE SGMQNMSIHT
KTTSGYAGGL TSSYGTPGFN YSLSPGSFSR TSSKPVVVKK IETRDGKLVS ESSDVLSK
