DESM_MESAU
ID DESM_MESAU Reviewed; 469 AA.
AC P02541;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Desmin;
GN Name=DES;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3855248; DOI=10.1016/0092-8674(85)90038-8;
RA Quax W.J., van den Broek L., Egberts W.V., Ramaekers F., Bloemendal H.;
RT "Characterization of the hamster desmin gene: expression and formation of
RT desmin filaments in nonmuscle cells after gene transfer.";
RL Cell 43:327-338(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-469.
RX PubMed=6091127; DOI=10.1073/pnas.81.19.5970;
RA Quax W.J., van den Heuvel R., Egberts W.V., Quax-Jeuken Y.E.F.M.,
RA Bloemendal H.;
RT "Intermediate filament cDNAs from BHK-21 cells: demonstration of distinct
RT genes for desmin and vimentin in all vertebrate classes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5970-5974(1984).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K02407; AAA37071.1; -; mRNA.
DR EMBL; M12104; AAA37072.1; -; Genomic_DNA.
DR EMBL; M12102; AAA37072.1; JOINED; Genomic_DNA.
DR EMBL; M12103; AAA37072.1; JOINED; Genomic_DNA.
DR PIR; A02956; DMHY.
DR PIR; A24783; A24783.
DR RefSeq; NP_001268541.1; NM_001281612.1.
DR AlphaFoldDB; P02541; -.
DR SMR; P02541; -.
DR STRING; 10036.XP_005070527.1; -.
DR GeneID; 101837949; -.
DR CTD; 1674; -.
DR eggNOG; KOG0977; Eukaryota.
DR OrthoDB; 655109at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0097512; C:cardiac myofibril; IEA:Ensembl.
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; IEA:UniProtKB-KW.
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:0045109; P:intermediate filament organization; ISS:UniProtKB.
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..469
FT /note="Desmin"
FT /id="PRO_0000063772"
FT DOMAIN 107..415
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..107
FT /note="Head"
FT REGION 108..140
FT /note="Coil 1A"
FT REGION 141..150
FT /note="Linker 1"
FT REGION 151..251
FT /note="Coil 1B"
FT REGION 252..267
FT /note="Linker 12"
FT REGION 267..414
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT REGION 268..286
FT /note="Coil 2A"
FT REGION 287..294
FT /note="Linker 2"
FT REGION 295..411
FT /note="Coil 2B"
FT REGION 412..469
FT /note="Tail"
FT REGION 437..452
FT /note="Interaction with CRYAB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT SITE 353
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 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
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 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
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 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
SQ SEQUENCE 469 AA; 53439 MW; 9C9A55545EB22EED CRC64;
MSQAYSSSQR VSSYRRTFGG APSFSLGSPL SSPVFPRAGF GTKGSSSSVT SRVYQVSRTS
GGAGGLGSLR ASRLGSTRAP SYGAGELLDF SLADAVNQEF LATRTNEKVE LQELNDRFAN
YIEKVRFLEQ QNAALAAEVN RLKGREPTRV AELYEEEMRE LRRQVEVLTN QRARVDVERD
NLIDDLQRLK AKLQEEIQLR EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK
VHEEEIRELQ AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE LEDRFASEAS
GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE IATYRKLLEG EESRINLPIQ
TFSALNFRET SPEQRGSEVH TKKTVMIKTI ETRDGEVVSE ATQQQHEVL
