SYNEM_MOUSE
ID SYNEM_MOUSE Reviewed; 1561 AA.
AC Q70IV5; Q3UPZ4; Q6A081; Q70IV3; Q70IV4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Synemin {ECO:0000303|PubMed:15265691};
DE AltName: Full=Desmuslin {ECO:0000250|UniProtKB:O15061};
GN Name=Synm {ECO:0000312|MGI:MGI:2661187};
GN Synonyms=Dmn {ECO:0000312|MGI:MGI:2661187},
GN Kiaa0353 {ECO:0000312|EMBL:BAD32215.1};
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:CAE30277.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAE30277.1};
RC TISSUE=Skeletal muscle {ECO:0000269|PubMed:15265691};
RX PubMed=15265691; DOI=10.1016/j.yexcr.2004.04.023;
RA Xue Z., Cheraud Y., Brocheriou V., Izmiryan A., Titeux M., Paulin D.,
RA Li Z.;
RT "The mouse synemin gene encodes three intermediate filament proteins
RT generated by alternative exon usage and different open reading frames.";
RL Exp. Cell Res. 298:431-444(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE25250.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25250.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAE25250.1};
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:BAD32215.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1560 (ISOFORM 1).
RC TISSUE=Embryonic intestine {ECO:0000312|EMBL:BAD32215.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5] {ECO:0000305}
RP INTERACTION WITH GFAP AND VIM, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17356066; DOI=10.1242/jcs.03423;
RA Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M., Skalli O.;
RT "Synemin is expressed in reactive astrocytes in neurotrauma and interacts
RT differentially with vimentin and GFAP intermediate filament networks.";
RL J. Cell Sci. 120:1267-1277(2007).
RN [6] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=19124017; DOI=10.1016/j.yexcr.2008.12.009;
RA Izmiryan A., Franco C.A., Paulin D., Li Z., Xue Z.;
RT "Synemin isoforms during mouse development: multiplicity of partners in
RT vascular and neuronal systems.";
RL Exp. Cell Res. 315:769-783(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778; SER-780; SER-1049;
RP SER-1077 AND SER-1087, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, 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).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1481, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Type-VI intermediate filament (IF) which plays an important
CC cytoskeletal role within the muscle cell cytoskeleton. It forms
CC heteromeric IFs with desmin and/or vimentin, and via its interaction
CC with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1,
CC utrophin and vinculin, is able to link these heteromeric IFs to
CC adherens-type junctions, such as to the costameres, neuromuscular
CC junctions, and myotendinous junctions within striated muscle cells (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15265691}.
CC -!- SUBUNIT: Interacts with DES, DMD, DTNA, TLN1, UTRN and VCL (By
CC similarity). Isoform 1 and isoform 2 interact with GFAP and VIM.
CC {ECO:0000250|UniProtKB:O15061, ECO:0000269|PubMed:17356066}.
CC -!- INTERACTION:
CC Q70IV5; A2ASS6: Ttn; NbExp=3; IntAct=EBI-9989763, EBI-9672947;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17356066}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O15061}. Note=There are at least two distinct
CC SYNM subpopulations, one in which SYMN interacts with DES within the Z-
CC lines, and another in which it interacts with both DTNA and DES at the
CC costamere. {ECO:0000250|UniProtKB:O15061, ECO:0000269|PubMed:17356066}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15265691}; Synonyms=H
CC {ECO:0000269|PubMed:15265691};
CC IsoId=Q70IV5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15265691}; Synonyms=M
CC {ECO:0000269|PubMed:15265691};
CC IsoId=Q70IV5-2; Sequence=VSP_053035;
CC Name=3 {ECO:0000269|PubMed:15265691}; Synonyms=L
CC {ECO:0000269|PubMed:15265691};
CC IsoId=Q70IV5-3; Sequence=VSP_053033, VSP_053034;
CC -!- TISSUE SPECIFICITY: Isoform 2 and isoform 3 are detected in adult
CC skeletal muscle, heart and bladder, whereas isoform 1 is only detected
CC in adult bladder (at protein level). {ECO:0000269|PubMed:15265691}.
CC -!- DEVELOPMENTAL STAGE: At 11.5 dpc, isoform 1 and isoform 2 are widely
CC expressed in the developing nervous and vascular systems and are also
CC found specifically associated with vimentin in endothelial cells. By 15
CC dpc, isoform 1, isoform 2 and isoform 3, are found coexpressed with
CC neurofilament, peripherin and internexin in the peripheral nervous
CC system (at protein level). In the developing embryo, isoform 2 is
CC detected as early as 5 dpc, whereas isoform 1 is first observed at 9
CC dpc in the nervous system and mesodermic derivatives. Isoform 3 is
CC observed later in neurons at 15 dpc. {ECO:0000269|PubMed:19124017}.
CC -!- INDUCTION: Up-regulated in reactive astrocytes following neurotrauma
CC (at protein level). {ECO:0000269|PubMed:17356066}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AJ579700; CAE30277.1; -; mRNA.
DR EMBL; AJ579701; CAE30278.1; -; mRNA.
DR EMBL; AJ579702; CAE30279.1; -; mRNA.
DR EMBL; AK143019; BAE25250.1; -; mRNA.
DR EMBL; AC158296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK172937; BAD32215.1; -; mRNA.
DR CCDS; CCDS39982.1; -. [Q70IV5-1]
DR CCDS; CCDS39983.1; -. [Q70IV5-2]
DR CCDS; CCDS85316.1; -. [Q70IV5-3]
DR RefSeq; NP_899135.3; NM_183312.3.
DR RefSeq; NP_964001.2; NM_201639.2. [Q70IV5-1]
DR RefSeq; NP_997546.2; NM_207663.3. [Q70IV5-2]
DR AlphaFoldDB; Q70IV5; -.
DR SMR; Q70IV5; -.
DR BioGRID; 231405; 9.
DR IntAct; Q70IV5; 3.
DR MINT; Q70IV5; -.
DR STRING; 10090.ENSMUSP00000073855; -.
DR iPTMnet; Q70IV5; -.
DR PhosphoSitePlus; Q70IV5; -.
DR MaxQB; Q70IV5; -.
DR PaxDb; Q70IV5; -.
DR PeptideAtlas; Q70IV5; -.
DR PRIDE; Q70IV5; -.
DR ProteomicsDB; 263185; -. [Q70IV5-1]
DR ProteomicsDB; 263186; -. [Q70IV5-2]
DR ProteomicsDB; 263187; -. [Q70IV5-3]
DR Antibodypedia; 29140; 175 antibodies from 20 providers.
DR DNASU; 233335; -.
DR Ensembl; ENSMUST00000051389; ENSMUSP00000050987; ENSMUSG00000030554. [Q70IV5-2]
DR Ensembl; ENSMUST00000074233; ENSMUSP00000073855; ENSMUSG00000030554. [Q70IV5-1]
DR GeneID; 233335; -.
DR KEGG; mmu:233335; -.
DR UCSC; uc009hiv.1; mouse. [Q70IV5-2]
DR UCSC; uc009hiw.1; mouse. [Q70IV5-1]
DR UCSC; uc009hix.1; mouse. [Q70IV5-3]
DR CTD; 23336; -.
DR MGI; MGI:2661187; Synm.
DR VEuPathDB; HostDB:ENSMUSG00000030554; -.
DR eggNOG; ENOG502QTUH; Eukaryota.
DR GeneTree; ENSGT00940000159268; -.
DR HOGENOM; CLU_002793_0_1_1; -.
DR InParanoid; Q70IV5; -.
DR OrthoDB; 104920at2759; -.
DR PhylomeDB; Q70IV5; -.
DR BioGRID-ORCS; 233335; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Synm; mouse.
DR PRO; PR:Q70IV5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q70IV5; protein.
DR Bgee; ENSMUSG00000030554; Expressed in triceps brachii and 197 other tissues.
DR ExpressionAtlas; Q70IV5; baseline and differential.
DR Genevisible; Q70IV5; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043034; C:costamere; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0019215; F:intermediate filament binding; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0017166; F:vinculin binding; ISS:UniProtKB.
DR GO; GO:0031443; P:fast-twitch skeletal muscle fiber contraction; IMP:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR030634; SYNM.
DR PANTHER; PTHR47136; PTHR47136; 1.
DR Pfam; PF00038; Filament; 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 Alternative splicing; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Intermediate filament; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1561
FT /note="Synemin"
FT /id="PRO_0000364438"
FT DOMAIN 11..322
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..10
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 11..320
FT /note="Interaction with DMD and UTRN"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT REGION 11..49
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 50..58
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 59..163
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 164..186
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 187..300
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 301..1561
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 371..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1453
FT /note="Interaction with TLN1 and VCL"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT REGION 1212..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1557
FT /note="Interaction with DMD and UTRN"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT REGION 1491..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 1425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15061"
FT MOD_RES 1481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 336..371
FT /note="EPRNTSYRYTNSVLQRKNEKNLFPRRKTPWAAVNHS -> DGFERHESDPQL
FT DPRHRVGSGSSRRVSPWWLENCTQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15265691"
FT /id="VSP_053033"
FT VAR_SEQ 372..1561
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15265691"
FT /id="VSP_053034"
FT VAR_SEQ 1152..1453
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15265691,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_053035"
FT CONFLICT 122
FT /note="E -> K (in Ref. 1; CAE30277/CAE30278/CAE30279)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="A -> S (in Ref. 1; CAE30277/CAE30278/CAE30279)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="E -> G (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="Y -> C (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="P -> S (in Ref. 1; CAE30277 and 4; BAD32215)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="A -> T (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="A -> V (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="L -> F (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="E -> D (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="S -> F (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1114
FT /note="S -> F (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="S -> F (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="L -> I (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="R -> P (in Ref. 1; CAE30277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="V -> A (in Ref. 1; CAE30277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="T -> A (in Ref. 1; CAE30277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1348
FT /note="H -> Q (in Ref. 1; CAE30277)"
FT /evidence="ECO:0000305"
FT CONFLICT 1499
FT /note="S -> F (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1556
FT /note="Missing (in Ref. 1; CAE30277/CAE30278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1561 AA; 173209 MW; 1DFC4DA574CC6A43 CRC64;
MLSWRLQTGS EKAELQELNA RLYDYVCRVR ELERENLLLE EELRSRLSRE DRWAEDQALY
AEEARSLRQQ LDELNWSTAL AEGERDALRR ELLELQREGV EAGTARSRLD AELGAQRREL
EEALGARAAL EALLGRLETE RRDLDAAHER QVRDLRARAA SLTMHFRARA TSPAAPPPRL
RDVHDSYALL VAESWRESVQ LYEDEVRELE QALRRGQESR LQAEDEARLC AQEADALRNQ
ALELEQLRAR LEDELLRMRE EYGMQAEERQ RVIDSLEDEK EALTLAMADR LRDYQELLQV
KTGLSLEVAT YRALLEGESN PEILIWTENI ENVPQEPRNT SYRYTNSVLQ RKNEKNLFPR
RKTPWAAVNH SSASYSNWPG HLDSQTTTAV GSAARRGLLT SRHSSSATTS GQQKPLEKTI
SSRANLRPVT PTHGFLRNTD AQMKTLPHRS KVEGTGDTHA RRATESVITR ESYRGHQGHV
AAGAVSSTPS NERTVILGKK LEAQATKEQE RDRSGVIRIK PEEKMFDSKE KASEERNLRW
EELTKLDRDA RKRESRHLRD EAREKEALKE RSVKEREVPI SLEVSRGSRA EVSTIHLQSP
GRKDVSHSGG REAETKETRF RLDTQDTASS LQSDSTTETI AESIVTTILK QFTQSPGAEE
EATSFPDTKV TYVDRKEFPG DGKTKTEIVV ESKLTDVVDV SDEAGLDYLL SKDVKEVGLK
GKSTETMIGE MINLGLKGRE GRAKVVNVEI VEEPMSYIGG GKIDFSTPFQ VEEVDDVSPS
PKGFVEEEDG EGETHMAFSM RPHQTKQPQG TIPHVEEVTE AGDSEGEQSY FVSTPDEYPG
GHDREDDGSV YGQIHIEEES TIRYSWQDEI AQGTWRRKMR GDVGGEKPVK VLEVPALSLG
GAIGSAHLKE EASGELRAEP TVIEKEIKIP HEFHTSIKGV FSSEPRHQLV EVIGQLEETL
PERMKEELSA LTRQSQGESG SVSVDVKKVQ SAAGGSVTLM AEVNLSQTVD ADQLDLEQLS
RDEAGEIERA VESVVRESLA KRSSPVPRSP DREDGEEVPA GGILFKRWAT RELYSPSGER
DDAGQVSPSS DQRVTQGPVS ATVEVTSPTG FVQSHVLEDV SQSVRHVKLG PTEMWRTEQV
TFGGPTAQVV EVSGDFSEAV SSEGASRSVR HITLGPHQSQ VSTEVIFRGS VPTWQETGDT
EKPGPVVLSV GADISGSGRM PGSERSHTEK EIRFQGPVSG TAQVGGNFAT EESVGSQTFV
RSLQLGPKEG FREEIQFIAP IPDKVGWGEE DSEHTKVSLE RATSIQRIDI VPQRYLASKQ
MAPQTLEFRD SEDMVMVEGS AGTIQATHNF TSDREILQNK ENTFQRVISG SPPDSVGDTG
AEVTANVSRS FRHIQIGPTE EEPSEYFVTG RPVSKTFVLD GSVASPGLVG GADGGSTPCR
IALGPKETSF TFQMDLSDTR AIRSWTRDTG SEVEAHGVSH RGGWRIAHSR DERVASTGSG
ASPGDAHQAP GEKGTEQAGF DKTVQLQRMV DQRSVASDEK KVALLYLDNE EEEEEEGEGW
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