DESM_CHICK
ID DESM_CHICK Reviewed; 464 AA.
AC P02542; E1BZ05;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Desmin;
GN Name=DES;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-464.
RC TISSUE=Gizzard;
RX PubMed=6202512; DOI=10.1002/j.1460-2075.1982.tb01368.x;
RA Geisler N., Weber K.;
RT "The amino acid sequence of chicken muscle desmin provides a common
RT structural model for intermediate filament proteins.";
RL EMBO J. 1:1649-1656(1982).
RN [3]
RP ERRATUM OF PUBMED:6202512.
RX PubMed=16453447;
RA Geisler N., Weber K.;
RL EMBO J. 2:625-625(1983).
RN [4]
RP PROTEIN SEQUENCE OF 2-89 AND 255-416.
RX PubMed=6889923; DOI=10.1016/0092-8674(82)90033-2;
RA Geisler N., Kaufmann E., Weber K.;
RT "Proteinchemical characterization of three structurally distinct domains
RT along the protofilament unit of desmin 10 nm filaments.";
RL Cell 30:277-286(1982).
RN [5]
RP PROTEIN SEQUENCE OF 325-464.
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 367-464.
RX PubMed=6594672; DOI=10.1073/pnas.81.22.6909;
RA Capetanaki Y.G., Ngai J., Lazarides E.;
RT "Characterization and regulation in the expression of a gene coding for the
RT intermediate filament protein desmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6909-6913(1984).
RN [7]
RP PHOSPHORYLATION AT SER-7; SER-23 AND THR-65.
RX PubMed=8439342; DOI=10.1006/bbrc.1993.1138;
RA Kusubata M., Matsuoka Y., Tsujimura K., Ito H., Ando S., Kamijo M.,
RA Yasuda H., Ohba Y., Okumura E., Kishimoto T.;
RT "cdc2 kinase phosphorylation of desmin at three serine/threonine residues
RT in the amino-terminal head domain.";
RL Biochem. Biophys. Res. Commun. 190:927-934(1993).
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.
CC {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
CC -!- SUBUNIT: Homomer. {ECO:0000250|UniProtKB:P17661}.
CC -!- INTERACTION:
CC P02542; Q96RG2: PASK; Xeno; NbExp=2; IntAct=EBI-8614455, EBI-1042651;
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}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AADN05000350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K02445; AAA48751.1; -; mRNA.
DR PIR; A90969; DMCH.
DR AlphaFoldDB; P02542; -.
DR SMR; P02542; -.
DR IntAct; P02542; 1.
DR MINT; P02542; -.
DR STRING; 9031.ENSGALP00000018424; -.
DR iPTMnet; P02542; -.
DR PaxDb; P02542; -.
DR Ensembl; ENSGALT00000018446; ENSGALP00000018424; ENSGALG00000011306.
DR VEuPathDB; HostDB:geneid_395906; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000155522; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P02542; -.
DR OMA; TMSQSYS; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P02542; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000011306; Expressed in muscle tissue and 13 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097433; C:dense body; IDA:AgBase.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:AgBase.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0045098; C:type III intermediate filament; IDA:CAFA.
DR GO; GO:0030018; C:Z disc; ISS: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:0045107; P:intermediate filament polymerization; IDA:CAFA.
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 Cell membrane; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Intermediate filament; Membrane; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15592404"
FT CHAIN 2..464
FT /note="Desmin"
FT /id="PRO_0000063776"
FT DOMAIN 100..408
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..100
FT /note="Head"
FT REGION 101..133
FT /note="Coil 1A"
FT REGION 134..143
FT /note="Linker 1"
FT REGION 144..244
FT /note="Coil 1B"
FT REGION 245..260
FT /note="Linker 12"
FT REGION 261..279
FT /note="Coil 2A"
FT REGION 280..287
FT /note="Linker 2"
FT REGION 288..404
FT /note="Coil 2B"
FT REGION 405..464
FT /note="Tail"
FT SITE 346
FT /note="Stutter"
FT MOD_RES 2
FT /note="Blocked amino end (Ser)"
FT /evidence="ECO:0000269|PubMed:6202512"
FT MOD_RES 7
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:8439342"
FT MOD_RES 23
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:8439342"
FT MOD_RES 65
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:8439342"
FT CONFLICT 71
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 53513 MW; 63AAFE036B5FE94D CRC64;
MSQSYSSSQR VSSYRRTFGG GTSPVFPRAS FGSRGSGSSV TSRVYQVSRT SAVPTLSTFR
TTRVTPLRTY QSAYQGAGEL LDFSLADAMN QEFLQTRTNE KVELQELNDR FANYIEKVRF
LEQQNALMVA EVNRLRGKEP TRVAEMYEEE LRELRRQVDA LTGQRARVEV ERDNLLDDLQ
KLKQRLQEEI QLKEEAENNL AAFRADVDAA TLARIDLERR IESLQEEIAF LKKVHEEEIR
ELQAQLQEQH IQVEMDISKP DLTAALRDIR AQYESIAAKN IAEAEEWYKS KVSDLTQAAN
KNNDALRQAK QEMLEYRHQI QSYTCEIDAL KGTNDSLMRQ MREMEERFAG EAGGYQDTIA
RLEEEIRHLK DEMARHLREY QDLLNVKMAL DVEIATYRKL LEGEENRISI PMHQTFASAL
NFRETSPDQR GSEVHTKKTV MIKTIETRDG EVVSEATQQQ HEVL
