DESM_BOVIN
ID DESM_BOVIN Reviewed; 470 AA.
AC O62654; A2VDU8; O62655;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Desmin;
GN Name=DES;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Holstein; TISSUE=Muscle;
RA Chikuni K., Tanabe R., Muroya S.;
RT "Desmin structure as related to meat tenderness.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Muscle-specific type III intermediate filament essential for
CC proper muscular structure and function. Plays a crucial role in
CC maintaining the structure of sarcomeres, inter-connecting the Z-disks
CC and forming the myofibrils, linking them not only to the sarcolemmal
CC cytoskeleton, but also to the nucleus and mitochondria, thus providing
CC strength for the muscle fiber during activity. In adult striated muscle
CC they form a fibrous network connecting myofibrils to each other and to
CC the plasma membrane from the periphery of the Z-line structures. May
CC act as a sarcomeric microtubule-anchoring protein: specifically
CC associates with detyrosinated tubulin-alpha chains, leading to buckled
CC microtubules and mechanical resistance to contraction. Contributes to
CC the transcriptional regulation of the NKX2-5 gene in cardiac progenitor
CC cells during a short period of cardiomyogenesis and in cardiac side
CC population stem cells in the adult. Plays a role in maintaining an
CC optimal conformation of nebulette (NEB) on heart muscle sarcomeres to
CC bind and recruit cardiac alpha-actin. {ECO:0000250|UniProtKB:P17661,
CC ECO:0000250|UniProtKB:P31001}.
CC -!- SUBUNIT: Homomer. Interacts with DST. Interacts with MTM1. Interacts
CC with EPPK1; interaction is dependent of higher-order structure of
CC intermediate filament. Interacts with CRYAB. Interacts with NEB (via
CC nebulin repeats 160-164). Interacts (via rod region) with NEBL (via
CC nebulin repeats 1-5). Interacts with ASB2; the interaction targets DES
CC for proteasomal degradation (By similarity).
CC {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P17661}. Cytoplasm
CC {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P17661}. Nucleus {ECO:0000250|UniProtKB:P31001}.
CC Note=Localizes in the intercalated disks which occur at the Z line of
CC cardiomyocytes. Localizes in the nucleus exclusively in differentiating
CC cardiac progenitor cells and premature cardiomyocytes.
CC {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
CC -!- PTM: ADP-ribosylation prevents ability to form intermediate filaments.
CC {ECO:0000250|UniProtKB:P48675}.
CC -!- PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1 and
CC phosphorylation at Ser-60 by AURKB contribute to efficient separation
CC of desmin intermediate filaments during mitosis.
CC {ECO:0000250|UniProtKB:P31001}.
CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 leads to
CC proteasomal degradation. {ECO:0000250|UniProtKB:P31001}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AB011675; BAA25135.1; -; Genomic_DNA.
DR EMBL; AB011673; BAA25133.1; -; mRNA.
DR EMBL; BC133410; AAI33411.1; -; mRNA.
DR RefSeq; NP_001075044.1; NM_001081575.1.
DR AlphaFoldDB; O62654; -.
DR SMR; O62654; -.
DR STRING; 9913.ENSBTAP00000007041; -.
DR PaxDb; O62654; -.
DR PeptideAtlas; O62654; -.
DR PRIDE; O62654; -.
DR Ensembl; ENSBTAT00000007041; ENSBTAP00000007041; ENSBTAG00000005353.
DR GeneID; 280765; -.
DR KEGG; bta:280765; -.
DR CTD; 1674; -.
DR VEuPathDB; HostDB:ENSBTAG00000005353; -.
DR VGNC; VGNC:28013; DES.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000155522; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; O62654; -.
DR OMA; TMSQSYS; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Reactome; R-BTA-390522; Striated Muscle Contraction.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000005353; Expressed in laryngeal cartilage and 102 other tissues.
DR GO; GO:0097512; C:cardiac myofibril; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0060538; P:skeletal muscle organ development; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
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 ADP-ribosylation; Cell membrane; Coiled coil; Cytoplasm;
KW Intermediate filament; Membrane; Methylation; Muscle protein; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02542"
FT CHAIN 2..470
FT /note="Desmin"
FT /id="PRO_0000063769"
FT DOMAIN 108..416
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..108
FT /note="Head"
FT REGION 109..141
FT /note="Coil 1A"
FT REGION 142..151
FT /note="Linker 1"
FT REGION 152..252
FT /note="Coil 1B"
FT REGION 253..268
FT /note="Linker 12"
FT REGION 268..415
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT REGION 269..287
FT /note="Coil 2A"
FT REGION 288..295
FT /note="Linker 2"
FT REGION 296..412
FT /note="Coil 2B"
FT REGION 413..470
FT /note="Tail"
FT REGION 438..453
FT /note="Interaction with CRYAB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT SITE 354
FT /note="Stutter"
FT MOD_RES 7
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 12
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 16
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 17
FT /note="Phosphothreonine; by AURKB and ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 28
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 32
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 37
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 37
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 58
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 60
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 77
FT /note="Phosphothreonine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
SQ SEQUENCE 470 AA; 53532 MW; B642D20280B3FD54 CRC64;
MSQAYSSSQR VSSYRRTFGG APSFPLGSPL SSPVFPRAGF GTKGSSSSVT SRVYQVSRTS
GGAGGLGALR ASRLGSTRVP SSYGAGELLD FSLADAVNQE FLTTRTNEKV ELQELNDRFA
NYIEKVRFLE QQNAALAAEV NRLKGREPTR VAEIYEEELR ELRRQVEVLT NQRARVDVER
DNLLDDLQRL KAKLQEEIQL KEEAENNLAA FRADVDAATL ARIDLERRIE SLNEEIAFLK
KVHEEEIREL QAQLQEQQVQ VEMDMSKPDL TAALRDIRAQ YETIAAKNIS EAEEWYKSKV
SDLTQAANKN NDALRQAKQE MMEYRHQIQS YTCEIDALKG TNDSLMRQMR ELEDRFASEA
SGYQDNIARL EEEIRHLKDE MARHLREYQD LLNVKMALDV EIATYRKLLE GEESRINLPI
QTFSALNFRE TSPEQRGSEV HTKKTVMIKT IETRDGEVVS EATQQQHEVL
