SYNCI_MOUSE
ID SYNCI_MOUSE Reviewed; 470 AA.
AC Q9EPM5; Q3KP79; Q3TKN1; Q3TUH9; Q8C4J4; Q9CT88;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Syncoilin;
DE AltName: Full=Syncoilin intermediate filament 1;
DE AltName: Full=Syncoilin-1;
GN Name=Sync; Synonyms=Sync1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC17787.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DTNA, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11053421; DOI=10.1074/jbc.m008305200;
RA Newey S.E., Howman E.V., Ponting C.P., Benson M.A., Nawrotzki R., Loh N.Y.,
RA Davies K.E., Blake D.J.;
RT "Syncoilin, a novel member of the intermediate filament superfamily that
RT interacts with alpha-dystrobrevin in skeletal muscle.";
RL J. Biol. Chem. 276:6645-6655(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC38387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38387.1};
RC TISSUE=Blastocyst {ECO:0000312|EMBL:BAE39114.1},
RC Embryo {ECO:0000312|EMBL:BAB23246.1}, and
RC Embryonic head {ECO:0000312|EMBL:BAC38387.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI06856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DTNA, AND SUBCELLULAR LOCATION.
RX PubMed=11694502; DOI=10.1074/jbc.m105273200;
RA Poon E., Howman E.V., Newey S.E., Davies K.E.;
RT "Association of syncoilin and desmin: linking intermediate filament
RT proteins to the dystrophin-associated protein complex.";
RL J. Biol. Chem. 277:3433-3439(2002).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17629480; DOI=10.1016/j.nmd.2007.06.004;
RA McCullagh K.J.A., Edwards B., Poon E., Lovering R.M., Paulin D.,
RA Davies K.E.;
RT "Intermediate filament-like protein syncoilin in normal and myopathic
RT striated muscle.";
RL Neuromuscul. Disord. 17:970-979(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18367591; DOI=10.1152/ajpcell.00049.2008;
RA Zhang J., Bang M.L., Gokhin D.S., Lu Y., Cui L., Li X., Gu Y., Dalton N.D.,
RA Scimia M.C., Peterson K.L., Lieber R.L., Chen J.;
RT "Syncoilin is required for generating maximum isometric stress in skeletal
RT muscle but dispensable for muscle cytoarchitecture.";
RL Am. J. Physiol. 294:C1175-C1182(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Atypical type III intermediate filament (IF) protein that may
CC play a supportive role in the efficient coupling of mechanical stress
CC between the myofibril and fiber exterior. May facilitate lateral force
CC transmission during skeletal muscle contraction. Does not form
CC homofilaments nor heterofilaments with other IF proteins.
CC {ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:18367591}.
CC -!- SUBUNIT: May link the dystrophin-associated glycoprotein complex (DAPC)
CC to intracellular desmin (DES) filaments. Interacts with DES and DTNA.
CC {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502}.
CC -!- INTERACTION:
CC Q9EPM5; P15331: Prph; NbExp=3; IntAct=EBI-7424051, EBI-1634736;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:11694502,
CC ECO:0000269|PubMed:17629480}. Note=In skeletal muscle, colocalizes with
CC DES and DTNA, and is localized at the myotendinous and neuromuscular
CC junctions, sarcolemma and Z-lines. In myotubes, detected in a punctate
CC cytoplasmic pattern. {ECO:0000269|PubMed:11053421,
CC ECO:0000269|PubMed:11694502, ECO:0000269|PubMed:17629480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11053421};
CC IsoId=Q9EPM5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9EPM5-2; Sequence=VSP_052551, VSP_052552;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9EPM5-3; Sequence=VSP_052550;
CC -!- TISSUE SPECIFICITY: Detected strongly in skeletal muscle and heart and
CC weakly in lung (at protein level). Highly expressed in skeletal muscle
CC and lung and weakly in lung and testis. {ECO:0000269|PubMed:11053421}.
CC -!- INDUCTION: Up-regulated in dystrophic muscle (at protein level).
CC {ECO:0000269|PubMed:11053421, ECO:0000269|PubMed:17629480}.
CC -!- DISRUPTION PHENOTYPE: Displays no obvious abnormalities, have a reduced
CC capacity to generate force during isometric contractions in skeletal
CC muscle. {ECO:0000269|PubMed:18367591}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AJ251641; CAC17787.1; -; mRNA.
DR EMBL; AK004279; BAB23246.1; -; mRNA.
DR EMBL; AK081983; BAC38387.1; -; mRNA.
DR EMBL; AK160756; BAE35992.1; -; mRNA.
DR EMBL; AK166916; BAE39114.1; -; mRNA.
DR EMBL; AL607123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106855; AAI06856.1; -; mRNA.
DR CCDS; CCDS18687.1; -. [Q9EPM5-1]
DR RefSeq; NP_075974.3; NM_023485.3. [Q9EPM5-1]
DR AlphaFoldDB; Q9EPM5; -.
DR SMR; Q9EPM5; -.
DR BioGRID; 213071; 4.
DR IntAct; Q9EPM5; 1.
DR MINT; Q9EPM5; -.
DR STRING; 10090.ENSMUSP00000099659; -.
DR iPTMnet; Q9EPM5; -.
DR PhosphoSitePlus; Q9EPM5; -.
DR MaxQB; Q9EPM5; -.
DR PaxDb; Q9EPM5; -.
DR PRIDE; Q9EPM5; -.
DR ProteomicsDB; 263179; -. [Q9EPM5-1]
DR ProteomicsDB; 263180; -. [Q9EPM5-2]
DR ProteomicsDB; 263181; -. [Q9EPM5-3]
DR Antibodypedia; 54803; 169 antibodies from 20 providers.
DR DNASU; 68828; -.
DR Ensembl; ENSMUST00000102599; ENSMUSP00000099659; ENSMUSG00000001333. [Q9EPM5-1]
DR GeneID; 68828; -.
DR KEGG; mmu:68828; -.
DR UCSC; uc008uwq.1; mouse. [Q9EPM5-2]
DR UCSC; uc008uwr.1; mouse. [Q9EPM5-1]
DR CTD; 81493; -.
DR MGI; MGI:1916078; Sync.
DR VEuPathDB; HostDB:ENSMUSG00000001333; -.
DR eggNOG; ENOG502RKZJ; Eukaryota.
DR GeneTree; ENSGT00390000018108; -.
DR HOGENOM; CLU_562526_0_0_1; -.
DR InParanoid; Q9EPM5; -.
DR OMA; FKVTREC; -.
DR OrthoDB; 906986at2759; -.
DR PhylomeDB; Q9EPM5; -.
DR BioGRID-ORCS; 68828; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9EPM5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9EPM5; protein.
DR Bgee; ENSMUSG00000001333; Expressed in lumbar dorsal root ganglion and 114 other tissues.
DR ExpressionAtlas; Q9EPM5; baseline and differential.
DR Genevisible; Q9EPM5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005882; C:intermediate filament; ISS:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0045103; P:intermediate filament-based process; IDA:MGI.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR027702; Syncoilin.
DR PANTHER; PTHR47147; PTHR47147; 1.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Intermediate filament;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..470
FT /note="Syncoilin"
FT /id="PRO_0000306181"
FT DOMAIN 157..452
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..148
FT /note="Head"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..192
FT /note="Coil 1A"
FT REGION 193..219
FT /note="Linker 1"
FT REGION 220..297
FT /note="Coil 1b"
FT REGION 298..337
FT /note="Linker 2"
FT REGION 338..445
FT /note="Coil 2"
FT REGION 446..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..470
FT /note="Tail"
FT COMPBIAS 23..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7C4"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052550"
FT VAR_SEQ 443..453
FT /note="AMLPKSLEQAD -> SVFSASQVSQI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052551"
FT VAR_SEQ 454..470
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052552"
FT CONFLICT 23
FT /note="A -> E (in Ref. 4; AAI06856)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="L -> Q (in Ref. 4; AAI06856)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="Q -> K (in Ref. 2; BAC38387)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="M -> T (in Ref. 4; AAI06856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53630 MW; 3D3B6026B099B229 CRC64;
MASPEPLRGG DGARASREPH TEASFPLQES ESPKEAKTFN PEATLSLEGT VNLEDILYLG
ASGDFEESFY EEEYEKPALT LFIDESRQPD EALGLEEPVR PEEMLSVEES VTPDEVQISE
QPVEPAKSPT ACEGEMVATE GSLPAQPIPN TEEDPLSVED LERLEARFQQ CVQAVSQLEE
ERDQLIHELV LLREPALQEV QQVHQDILAA YKLHAQAELE RDGLREEIRT VKQKLFKVTK
ECVAYQYQLE CRQQDVAQFA DCREALTTRA AQLSEELTQL RDACQKQKEQ LQQQLEAPPT
QSDGHFLQES RRLSTQFENL MAESRQGLEE EYEPQLLRLL ERKEAGTKAL QDTQAEIQEM
REALRPLEAE ARQLQLQNRN LEDQITLVRQ KRDEEVQQYR EQLEEMEERQ RQLRSGVQVQ
QQKNKEMERL RMSLAEELST YKAMLPKSLE QADAPTSQAG GVEAQSPGTV
