DESM_RAT
ID DESM_RAT Reviewed; 469 AA.
AC P48675;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Desmin;
GN Name=Des;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Aorta;
RX PubMed=8286410;
RA van Groningen J.J.M., Bloemers H.P.J., Swart G.W.M.;
RT "Rat desmin gene structure and expression.";
RL Biochim. Biophys. Acta 1217:107-109(1994).
RN [2]
RP ADP-RIBOSYLATION AT ARG-58.
RX PubMed=8900395; DOI=10.1006/abbi.1996.0449;
RA Zhou H., Huiatt T.W., Robson R.M., Sernett S.W., Graves D.J.;
RT "Characterization of ADP-ribosylation sites on desmin and restoration of
RT desmin intermediate filament assembly by de-ADP-ribosylation.";
RL Arch. Biochem. Biophys. 334:214-222(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-28; SER-32; SER-45;
RP SER-68; SER-81; SER-289; SER-357; SER-360 AND SER-423, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23615443; DOI=10.1091/mbc.e12-11-0840;
RA Baker L.K., Gillis D.C., Sharma S., Ambrus A., Herrmann H., Conover G.M.;
RT "Nebulin binding impedes mutant desmin filament assembly.";
RL Mol. Biol. Cell 24:1918-1932(2013).
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 (By similarity). Interacts with DST (By similarity).
CC Interacts with MTM1 (By similarity). Interacts with EPPK1; interaction
CC is dependent of higher-order structure of intermediate filament (By
CC similarity). Interacts with CRYAB (By similarity). Interacts with NEB
CC (via nebulin repeats 160-164) (By similarity). Interacts (via rod
CC region) with NEBL (via nebulin repeats 1-5) (By similarity).
CC {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:23615443}. 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. Interacts with
CC ASB2; the interaction targets DES for proteasomal degradation (By
CC similarity). {ECO:0000250|UniProtKB:P17661,
CC ECO:0000250|UniProtKB:P31001}.
CC -!- PTM: ADP-ribosylation prevents ability to form intermediate filaments.
CC {ECO:0000269|PubMed:8900395}.
CC -!- PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1,
CC phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by
CC ROCK1 contribute to efficient separation of desmin intermediate
CC filaments during mitosis. {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; X73524; CAA51920.1; -; Genomic_DNA.
DR PIR; I52469; I52469.
DR RefSeq; NP_071976.1; NM_022531.1.
DR AlphaFoldDB; P48675; -.
DR SMR; P48675; -.
DR IntAct; P48675; 6.
DR STRING; 10116.ENSRNOP00000026860; -.
DR iPTMnet; P48675; -.
DR PhosphoSitePlus; P48675; -.
DR jPOST; P48675; -.
DR PaxDb; P48675; -.
DR PRIDE; P48675; -.
DR GeneID; 64362; -.
DR KEGG; rno:64362; -.
DR UCSC; RGD:620686; rat.
DR CTD; 1674; -.
DR RGD; 620686; Des.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P48675; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P48675; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P48675; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097512; C:cardiac myofibril; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005916; C:fascia adherens; ISO:RGD.
DR GO; GO:0005921; C:gap junction; IDA:BHF-UCL.
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; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0045098; C:type III intermediate filament; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 1: Evidence at protein 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_0000063775"
FT DOMAIN 107..415
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..108
FT /note="Head"
FT REGION 109..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 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:0007744|PubMed:22673903"
FT MOD_RES 28
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000305|PubMed:8900395"
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:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
FT MOD_RES 76
FT /note="Phosphothreonine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
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:0007744|PubMed:22673903"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 469 AA; 53457 MW; 4E53A71FC1C55BDF CRC64;
MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSVT SRVYQVSRTS
GGAGGLGSLR ASRLGTTRAP SYGAGELLDF SLADAVNQEF LATRTNEKVE LQELNDRFAN
YFEKVRFLEQ 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
