DESM_CANLF
ID DESM_CANLF Reviewed; 469 AA.
AC Q5XFN2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Desmin;
GN Name=DES;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15475165; DOI=10.1016/j.gene.2004.06.050;
RA Stabej P., Imholz S., Versteeg S.A., Zijlstra C., Stokhof A.A.,
RA Domanjko-Petric A., Leegwater P.A.J., van Oost B.A.;
RT "Characterization of the canine desmin (DES) gene and evaluation as a
RT candidate gene for dilated cardiomyopathy in the Dobermann.";
RL Gene 340:241-249(2004).
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-28 AND SER-32.
RX PubMed=24413773; DOI=10.1093/cvr/cvu003;
RA Agnetti G., Halperin V.L., Kirk J.A., Chakir K., Guo Y., Lund L.,
RA Nicolini F., Gherli T., Guarnieri C., Caldarera C.M., Tomaselli G.F.,
RA Kass D.A., Van Eyk J.E.;
RT "Desmin modifications associate with amyloid-like oligomers deposition in
RT heart failure.";
RL Cardiovasc. Res. 102:24-34(2014).
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 (PubMed:24413773). 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). Interacts
CC with ASB2; the interaction targets DES for proteasomal degradation (By
CC similarity). {ECO:0000250|UniProtKB:P17661,
CC ECO:0000250|UniProtKB:P31001, ECO:0000269|PubMed:24413773}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:24413773}. 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,
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; BK005142; DAA05325.1; -; Genomic_DNA.
DR RefSeq; NP_001012394.1; NM_001012394.1.
DR AlphaFoldDB; Q5XFN2; -.
DR SMR; Q5XFN2; -.
DR STRING; 9615.ENSCAFP00000052382; -.
DR iPTMnet; Q5XFN2; -.
DR PaxDb; Q5XFN2; -.
DR PRIDE; Q5XFN2; -.
DR Ensembl; ENSCAFT00030019567; ENSCAFP00030017065; ENSCAFG00030010141.
DR Ensembl; ENSCAFT00040046751; ENSCAFP00040040807; ENSCAFG00040025051.
DR GeneID; 497091; -.
DR KEGG; cfa:497091; -.
DR CTD; 1674; -.
DR eggNOG; KOG0977; Eukaryota.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; Q5XFN2; -.
DR OMA; TMSQSYS; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Reactome; R-CFA-390522; Striated Muscle Contraction.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
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_0000063770"
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 28
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:24413773"
FT MOD_RES 32
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:24413773"
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 76
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; 53321 MW; 55A18E42D6D6C31B CRC64;
MSQAYSSSQR VSSYRRTFGG AGGFPLGSPL GSPVFPRAGF GTKGSSSSVT SRVYQVSRTS
GGAGGLGALR AGRLGTGRAP SYSAGELLDF SLADAVNQEF LTTRTNEKVE LQELNDRFAN
YIEKVRFLEQ QNAALAAEVN RLKGREPTRV AEIYEEELRE LRRQVEVLTN QRARVDVERD
NLLDDLQRLK AKLQEEIQLK EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK
VHEEEIRELQ AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE MEDRFASEAS
GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE IATYRKLLEG EESRINLPIQ
TYSALNFRET SPEQRGSEVH TKKTVMIKTI ETRDGEVVSE ATQQQHEVL
