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MYOTI_HUMAN
ID   MYOTI_HUMAN             Reviewed;         498 AA.
AC   Q9UBF9; A0A4R6; B4DT79;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Myotilin;
DE   AltName: Full=57 kDa cytoskeletal protein;
DE   AltName: Full=Myofibrillar titin-like Ig domains protein;
DE   AltName: Full=Titin immunoglobulin domain protein;
GN   Name=MYOT; Synonyms=TTID;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP   GLN-74.
RC   TISSUE=Bone marrow;
RX   PubMed=10486214; DOI=10.1006/geno.1999.5912;
RA   Godley L.A., Lai F., Liu J., Zhao N., Le Beau M.M.;
RT   "TTID: a novel gene at 5q31 encoding a protein with titin-like features.";
RL   Genomics 60:226-233(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, INTERACTION WITH ACTN1,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT GLN-74.
RC   TISSUE=Skeletal muscle;
RX   PubMed=10369880; DOI=10.1093/hmg/8.7.1329;
RA   Salmikangas P., Mykkaenen O.M., Groenholm M., Heiska L., Kere J.,
RA   Carpen O.;
RT   "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded
RT   by a candidate gene for limb-girdle muscular dystrophy.";
RL   Hum. Mol. Genet. 8:1329-1336(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pericardium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-74.
RC   TISSUE=Liver;
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   [6]
RP   INTERACTION WITH FLNC.
RX   PubMed=11038172; DOI=10.1083/jcb.151.2.235;
RA   van der Ven P.F.M., Wiesner S., Salmikangas P., Auerbach D., Himmel M.,
RA   Kempa S., Hayess K., Pacholsky D., Taivainen A., Schroeder R., Carpen O.,
RA   Fuerst D.O.;
RT   "Indications for a novel muscular dystrophy pathway: gamma-filamin, the
RT   muscle-specific filamin isoform, interacts with myotilin.";
RL   J. Cell Biol. 151:235-248(2000).
RN   [7]
RP   FUNCTION IN MYOFIBRIL ASSEMBLY AND STABILITY, SUBUNIT, AND INTERACTION WITH
RP   ACTA1.
RX   PubMed=12499399; DOI=10.1093/hmg/ddg020;
RA   Salmikangas P., van der Ven P.F.M., Lalowski M., Taivainen A., Zhao F.,
RA   Suila H., Schroeder R., Lappalainen P., Fuerst D.O., Carpen O.;
RT   "Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-
RT   links actin filaments and controls sarcomere assembly.";
RL   Hum. Mol. Genet. 12:189-203(2003).
RN   [8]
RP   INTERACTION WITH FLNA; FLNB; FLNC; MYOZ1 AND MYOZ2, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16076904; DOI=10.1242/jcs.02484;
RA   Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA   Carpen O., Faulkner G., Borradori L.;
RT   "The Z-disc proteins myotilin and FATZ-1 interact with each other and are
RT   connected to the sarcolemma via muscle-specific filamins.";
RL   J. Cell Sci. 118:3739-3749(2005).
RN   [9]
RP   STRUCTURE BY NMR OF 249-344.
RX   PubMed=19418025; DOI=10.1007/s10858-009-9320-4;
RA   Heikkinen O., Permi P., Koskela H., Carpen O., Ylaenne J., Kilpelaeinen I.;
RT   "Solution structure of the first immunoglobulin domain of human myotilin.";
RL   J. Biomol. NMR 44:107-112(2009).
RN   [10]
RP   STRUCTURE BY NMR OF 344-449.
RG   Northeast structural genomics consortium (NESG);
RT   "Solution NMR structure of the Ig-like C2-type 2 domain of human myotilin.
RT   Northeast structural genomics target HR3158.";
RL   Submitted (JUL-2009) to the PDB data bank.
RN   [11]
RP   VARIANT MFM3 ILE-57, AND INTERACTION WITH ACTN1.
RX   PubMed=10958653; DOI=10.1093/hmg/9.14.2141;
RA   Hauser M.A., Horrigan S.K., Salmikangas P., Torian U.M., Viles K.D.,
RA   Dancel R., Tim R.W., Taivainen A., Bartoloni L., Gilchrist J.M.,
RA   Stajich J.M., Gaskell P.C., Gilbert J.R., Vance J.M., Pericak-Vance M.A.,
RA   Carpen O., Westbrook C.A., Speer M.C.;
RT   "Myotilin is mutated in limb girdle muscular dystrophy 1A.";
RL   Hum. Mol. Genet. 9:2141-2147(2000).
RN   [12]
RP   VARIANT MFM3 PHE-55.
RX   PubMed=12428213; DOI=10.1086/344532;
RA   Hauser M.A., Conde C.B., Kowaljow V., Zeppa G., Taratuto A.L., Torian U.M.,
RA   Vance J.M., Pericak-Vance M.A., Speer M.C., Rosa A.L.;
RT   "Myotilin mutation found in second pedigree with LGMD1A.";
RL   Am. J. Hum. Genet. 71:1428-1432(2002).
RN   [13]
RP   VARIANTS MFM3 PHE-55; CYS-60; PHE-60 AND ILE-95.
RX   PubMed=15111675; DOI=10.1212/01.wnl.0000123576.74801.75;
RA   Selcen D., Engel A.G.;
RT   "Mutations in myotilin cause myofibrillar myopathy.";
RL   Neurology 62:1363-1371(2004).
RN   [14]
RP   ERRATUM OF PUBMED:15111675.
RA   Selcen D., Engel A.G.;
RL   Neurology 63:405-405(2004).
RN   [15]
RP   VARIANT SBM PHE-39.
RX   PubMed=16380616; DOI=10.1212/01.wnl.0000188872.28149.9a;
RA   Foroud T., Pankratz N., Batchman A.P., Pauciulo M.W., Vidal R.,
RA   Miravalle L., Goebel H.H., Cushman L.J., Azzarelli B., Horak H., Farlow M.,
RA   Nichols W.C.;
RT   "A mutation in myotilin causes spheroid body myopathy.";
RL   Neurology 65:1936-1940(2005).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] ILE-33.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Component of a complex of multiple actin cross-linking
CC       proteins. Involved in the control of myofibril assembly and stability
CC       at the Z lines in muscle cells. {ECO:0000269|PubMed:12499399}.
CC   -!- SUBUNIT: Homodimer. Interacts with ACTA1, ACTN1, FLNA, FLNB, FLNC and
CC       MYOZ2. Interacts with the C-terminal region of MYOZ1.
CC       {ECO:0000269|PubMed:10369880, ECO:0000269|PubMed:10958653,
CC       ECO:0000269|PubMed:11038172, ECO:0000269|PubMed:12499399,
CC       ECO:0000269|PubMed:16076904}.
CC   -!- INTERACTION:
CC       Q9UBF9; P35609: ACTN2; NbExp=3; IntAct=EBI-296701, EBI-77797;
CC       Q9UBF9; Q08043: ACTN3; NbExp=3; IntAct=EBI-296701, EBI-2880652;
CC       Q9UBF9; Q14315: FLNC; NbExp=6; IntAct=EBI-296701, EBI-489954;
CC       Q9UBF9; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-296701, EBI-744782;
CC       Q9UBF9; Q99471: PFDN5; NbExp=3; IntAct=EBI-296701, EBI-357275;
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000269|PubMed:10369880}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10369880}. Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000269|PubMed:16076904}. Note=Sarcomeric, also localized to the
CC       sarcolemma (PubMed:10369880). Colocalizes with MYOZ1 at the Z-lines in
CC       skeletal muscle (PubMed:16076904). {ECO:0000269|PubMed:10369880,
CC       ECO:0000269|PubMed:16076904}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UBF9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UBF9-2; Sequence=VSP_041450;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC       Expressed in skeletal muscle, heart, bone marrow and thyroid gland.
CC       {ECO:0000269|PubMed:10369880, ECO:0000269|PubMed:10486214}.
CC   -!- DISEASE: Myopathy, myofibrillar, 3 (MFM3) [MIM:609200]: A form of
CC       myofibrillar myopathy, a group of chronic neuromuscular disorders
CC       characterized at ultrastructural level by disintegration of the
CC       sarcomeric Z disk and myofibrils, and replacement of the normal
CC       myofibrillar markings by small dense granules, or larger hyaline
CC       masses, or amorphous material. MFM3 is characterized by progressive
CC       skeletal muscle weakness greater distally than proximally, tight heel
CC       cords, hyporeflexia, cardiomyopathy and peripheral neuropathy in some
CC       patients. Affected muscle exhibits disorganization and streaming of the
CC       Z-line, presence of large hyaline structures, excessive accumulation of
CC       myotilin and other ectopically expressed proteins and prominent
CC       congophilic deposits. {ECO:0000269|PubMed:10958653,
CC       ECO:0000269|PubMed:12428213, ECO:0000269|PubMed:15111675}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Spheroid body myopathy (SBM) [MIM:182920]: Autosomal dominant
CC       form of myofibrillar myopathy (MFM), characterized by slowly
CC       progressing proximal muscle weakness and dysarthric nasal speech. There
CC       is no evidence of cardiomyopathy. Muscle biopsy shows spheroid bodies
CC       within the type I muscle fibers. {ECO:0000269|PubMed:16380616}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}.
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DR   EMBL; AF133820; AAD29051.2; -; mRNA.
DR   EMBL; AF144477; AAD44754.1; -; mRNA.
DR   EMBL; AK300088; BAG61891.1; -; mRNA.
DR   EMBL; AC106791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005376; AAH05376.1; -; mRNA.
DR   CCDS; CCDS4194.1; -. [Q9UBF9-1]
DR   CCDS; CCDS47268.1; -. [Q9UBF9-2]
DR   RefSeq; NP_001129412.1; NM_001135940.1. [Q9UBF9-2]
DR   RefSeq; NP_001287840.1; NM_001300911.1.
DR   RefSeq; NP_006781.1; NM_006790.2.
DR   PDB; 2KDG; NMR; -; A=249-344.
DR   PDB; 2KKQ; NMR; -; A=344-449.
DR   PDBsum; 2KDG; -.
DR   PDBsum; 2KKQ; -.
DR   AlphaFoldDB; Q9UBF9; -.
DR   SASBDB; Q9UBF9; -.
DR   SMR; Q9UBF9; -.
DR   BioGRID; 114878; 19.
DR   IntAct; Q9UBF9; 11.
DR   STRING; 9606.ENSP00000239926; -.
DR   iPTMnet; Q9UBF9; -.
DR   PhosphoSitePlus; Q9UBF9; -.
DR   BioMuta; MYOT; -.
DR   DMDM; 311033402; -.
DR   EPD; Q9UBF9; -.
DR   MassIVE; Q9UBF9; -.
DR   PaxDb; Q9UBF9; -.
DR   PeptideAtlas; Q9UBF9; -.
DR   PRIDE; Q9UBF9; -.
DR   ProteomicsDB; 83962; -. [Q9UBF9-1]
DR   ProteomicsDB; 83963; -. [Q9UBF9-2]
DR   Antibodypedia; 26530; 270 antibodies from 31 providers.
DR   DNASU; 9499; -.
DR   Ensembl; ENST00000421631.6; ENSP00000391185.2; ENSG00000120729.10. [Q9UBF9-2]
DR   GeneID; 9499; -.
DR   KEGG; hsa:9499; -.
DR   UCSC; uc003lbv.4; human. [Q9UBF9-1]
DR   CTD; 9499; -.
DR   DisGeNET; 9499; -.
DR   GeneCards; MYOT; -.
DR   HGNC; HGNC:12399; MYOT.
DR   HPA; ENSG00000120729; Group enriched (skeletal muscle, tongue).
DR   MalaCards; MYOT; -.
DR   MIM; 182920; phenotype.
DR   MIM; 604103; gene.
DR   MIM; 609200; phenotype.
DR   neXtProt; NX_Q9UBF9; -.
DR   OpenTargets; ENSG00000120729; -.
DR   Orphanet; 266; Autosomal dominant limb-girdle muscular dystrophy type 1A.
DR   Orphanet; 98911; Distal myotilinopathy.
DR   Orphanet; 268129; Spheroid body myopathy.
DR   PharmGKB; PA37064; -.
DR   VEuPathDB; HostDB:ENSG00000120729; -.
DR   eggNOG; ENOG502QTWI; Eukaryota.
DR   GeneTree; ENSGT00940000159795; -.
DR   HOGENOM; CLU_006487_0_0_1; -.
DR   InParanoid; Q9UBF9; -.
DR   OrthoDB; 496055at2759; -.
DR   PhylomeDB; Q9UBF9; -.
DR   PathwayCommons; Q9UBF9; -.
DR   SignaLink; Q9UBF9; -.
DR   BioGRID-ORCS; 9499; 12 hits in 1069 CRISPR screens.
DR   ChiTaRS; MYOT; human.
DR   EvolutionaryTrace; Q9UBF9; -.
DR   GeneWiki; Myotilin; -.
DR   GenomeRNAi; 9499; -.
DR   Pharos; Q9UBF9; Tbio.
DR   PRO; PR:Q9UBF9; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UBF9; protein.
DR   Bgee; ENSG00000120729; Expressed in hindlimb stylopod muscle and 107 other tissues.
DR   ExpressionAtlas; Q9UBF9; baseline and differential.
DR   Genevisible; Q9UBF9; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051393; F:alpha-actinin binding; IDA:MGI.
DR   GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central.
DR   GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR   GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW   Cytoplasm; Cytoskeleton; Disease variant; Immunoglobulin domain;
KW   Limb-girdle muscular dystrophy; Membrane; Methylation; Muscle protein;
KW   Myofibrillar myopathy; Reference proteome; Repeat.
FT   CHAIN           1..498
FT                   /note="Myotilin"
FT                   /id="PRO_0000072687"
FT   DOMAIN          250..335
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          349..441
FT                   /note="Ig-like C2-type 2"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..150
FT                   /note="Necessary for interaction with ACTN1"
FT   REGION          202..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..498
FT                   /note="Necessary for interaction with ACTA1"
FT                   /evidence="ECO:0000269|PubMed:12499399"
FT   REGION          215..493
FT                   /note="Necessary for interaction with FLNC"
FT   COMPBIAS        8..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIF9"
FT   VAR_SEQ         1..184
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041450"
FT   VARIANT         33
FT                   /note="S -> I (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035520"
FT   VARIANT         39
FT                   /note="S -> F (in SBM)"
FT                   /evidence="ECO:0000269|PubMed:16380616"
FT                   /id="VAR_029532"
FT   VARIANT         50
FT                   /note="Q -> R (in dbSNP:rs34717730)"
FT                   /id="VAR_049914"
FT   VARIANT         55
FT                   /note="S -> F (in MFM3 and MFM3)"
FT                   /evidence="ECO:0000269|PubMed:12428213,
FT                   ECO:0000269|PubMed:15111675"
FT                   /id="VAR_021569"
FT   VARIANT         57
FT                   /note="T -> I (in MFM3; does not abolish interaction with
FT                   ACTN1; dbSNP:rs28937597)"
FT                   /evidence="ECO:0000269|PubMed:10958653"
FT                   /id="VAR_021570"
FT   VARIANT         60
FT                   /note="S -> C (in MFM3)"
FT                   /evidence="ECO:0000269|PubMed:15111675"
FT                   /id="VAR_021571"
FT   VARIANT         60
FT                   /note="S -> F (in MFM3)"
FT                   /evidence="ECO:0000269|PubMed:15111675"
FT                   /id="VAR_021572"
FT   VARIANT         74
FT                   /note="K -> Q (in dbSNP:rs6890689)"
FT                   /evidence="ECO:0000269|PubMed:10369880,
FT                   ECO:0000269|PubMed:10486214, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_029533"
FT   VARIANT         95
FT                   /note="S -> I (in MFM3)"
FT                   /evidence="ECO:0000269|PubMed:15111675"
FT                   /id="VAR_021573"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          280..285
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          305..312
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          319..327
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          330..341
FT                   /evidence="ECO:0007829|PDB:2KDG"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          358..361
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          364..372
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          379..384
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          396..400
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          405..413
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   HELIX           415..417
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          419..427
FT                   /evidence="ECO:0007829|PDB:2KKQ"
FT   STRAND          430..441
FT                   /evidence="ECO:0007829|PDB:2KKQ"
SQ   SEQUENCE   498 AA;  55395 MW;  7F226DD43A0C611B CRC64;
     MFNYERPKHF IQSQNPCGSR LQPPGPETSS FSSQTKQSSI IIQPRQCTEQ RFSASSTLSS
     HITMSSSAFP ASPKQHAGSN PGQRVTTTYN QSPASFLSSI LPSQPDYNSS KIPSAMDSNY
     QQSSAGQPIN AKPSQTANAK PIPRTPDHEI QGSKEALIQD LERKLKCKDT LLHNGNQRLT
     YEEKMARRLL GPQNAAAVFQ AQDDSGAQDS QQHNSEHARL QVPTSQVRSR STSRGDVNDQ
     DAIQEKFYPP RFIQVPENMS IDEGRFCRMD FKVSGLPAPD VSWYLNGRTV QSDDLHKMIV
     SEKGLHSLIF EVVRASDAGA YACVAKNRAG EATFTVQLDV LAKEHKRAPM FIYKPQSKKV
     LEGDSVKLEC QISAIPPPKL FWKRNNEMVQ FNTDRISLYQ DNTGRVTLLI KDVNKKDAGW
     YTVSAVNEAG VTTCNTRLDV TARPNQTLPA PKQLRVRPTF SKYLALNGKG LNVKQAFNPE
     GEFQRLAAQS GLYESEEL
 
 
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