DESM_PIG
ID DESM_PIG Reviewed; 471 AA.
AC P02540; O62656;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Desmin;
GN Name=DES;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC 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 [MRNA].
RA Tuggle C.K., Sanchez-Serrano I., Smith B., Marklund L., Ernst C.;
RT "Muscle ESTs II: cloning, sequencing and mapping the pig gene for the
RT intermediate filament protein desmin (DES).";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Longissimus muscle;
RA Beuzen N.D., Hall A.D., Gallagher A., Chang K.-C.;
RT "A polymorphic CT-repeat at the porcine desmin locus with an effect on meat
RT quality.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 334-471.
RX PubMed=6945574; DOI=10.1073/pnas.78.7.4120;
RA Geisler N., Weber K.;
RT "Comparison of the proteins of two immunologically distinct intermediate-
RT sized filaments by amino acid sequence analysis: desmin and vimentin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4120-4123(1981).
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; AB011676; BAA25136.1; -; Genomic_DNA.
DR EMBL; AB011674; BAA25134.1; -; mRNA.
DR EMBL; AF136188; AAD46492.1; -; mRNA.
DR EMBL; AF363284; AAK51087.1; -; mRNA.
DR PIR; A02955; DMPG.
DR RefSeq; NP_001001535.1; NM_001001535.1.
DR AlphaFoldDB; P02540; -.
DR SMR; P02540; -.
DR STRING; 9823.ENSSSCP00000021504; -.
DR PaxDb; P02540; -.
DR PeptideAtlas; P02540; -.
DR PRIDE; P02540; -.
DR Ensembl; ENSSSCT00000030104; ENSSSCP00000021504; ENSSSCG00000020785.
DR Ensembl; ENSSSCT00015045488; ENSSSCP00015018025; ENSSSCG00015032038.
DR Ensembl; ENSSSCT00025019257; ENSSSCP00025007801; ENSSSCG00025014279.
DR Ensembl; ENSSSCT00030014460; ENSSSCP00030006492; ENSSSCG00030010480.
DR Ensembl; ENSSSCT00035020132; ENSSSCP00035007213; ENSSSCG00035015748.
DR Ensembl; ENSSSCT00040026345; ENSSSCP00040011142; ENSSSCG00040019479.
DR Ensembl; ENSSSCT00045066391; ENSSSCP00045047089; ENSSSCG00045038283.
DR Ensembl; ENSSSCT00050055578; ENSSSCP00050023578; ENSSSCG00050040989.
DR Ensembl; ENSSSCT00055005105; ENSSSCP00055003947; ENSSSCG00055002623.
DR Ensembl; ENSSSCT00060064376; ENSSSCP00060027594; ENSSSCG00060047403.
DR Ensembl; ENSSSCT00065046861; ENSSSCP00065020150; ENSSSCG00065034406.
DR Ensembl; ENSSSCT00070031867; ENSSSCP00070026567; ENSSSCG00070016194.
DR GeneID; 396725; -.
DR KEGG; ssc:396725; -.
DR CTD; 1674; -.
DR VGNC; VGNC:96159; DES.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000155522; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P02540; -.
DR OMA; TMSQSYS; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Reactome; R-SSC-390522; Striated Muscle Contraction.
DR Proteomes; UP000008227; Chromosome 15.
DR Proteomes; UP000314985; Chromosome 15.
DR Bgee; ENSSSCG00000020785; Expressed in psoas major muscle and 36 other tissues.
DR ExpressionAtlas; P02540; baseline and differential.
DR Genevisible; P02540; SS.
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 1: Evidence at protein level;
KW ADP-ribosylation; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Intermediate filament; Membrane; Methylation;
KW Muscle protein; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02542"
FT CHAIN 2..471
FT /note="Desmin"
FT /id="PRO_0000063774"
FT DOMAIN 109..417
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..109
FT /note="Head"
FT REGION 110..142
FT /note="Coil 1A"
FT REGION 143..152
FT /note="Linker 1"
FT REGION 153..253
FT /note="Coil 1B"
FT REGION 254..269
FT /note="Linker 12"
FT REGION 269..416
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT REGION 270..288
FT /note="Coil 2A"
FT REGION 289..296
FT /note="Linker 2"
FT REGION 297..413
FT /note="Coil 2B"
FT REGION 414..471
FT /note="Tail"
FT REGION 439..454
FT /note="Interaction with CRYAB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT SITE 355
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 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31001"
SQ SEQUENCE 471 AA; 53629 MW; 4D6992271A004630 CRC64;
MSQAYSSSQR VSSYRRTFGG APSFPLGSPL SSPVFPRAGF GTKGSSSSVT SRVYQVSRTS
GGAGGLGPLR ASRLGATRVP SSSYGAGELL DFSLADAVNQ EFLTTRTNEK VELQELNDRF
ANYIEKVRFL EQQNAALAAE VNRLKGREPT RVAEIYEEEL RELRRQVEVL TNQRARVDVE
RDNLLDDLQR LKAKLQEEIQ LKEEAENNLA AFRADVDAAT LARIDLERRI ESLNEEIAFL
KKVHEEEIRE LQAQLQEQQV QVEMDMSKPD LTAALRDIRA QYETIAAKNI SEAEEWYKSK
VSDLTQAANK NNDALRQAKQ EMMEYRHQIQ SYTCEIDALK GTNDSLMRQM RELEDRFASE
ASGYQDNIAR LEEEIRHLKD EMARHLREYQ DLLNVKMALD VEIATYRKLL EGEESRINLP
IQTFSALNFR ETSPEQRGSE VHTKKTVMIK TIETRDGEVV SEATQQQHEV L
