SMG1_MOUSE
ID SMG1_MOUSE Reviewed; 3658 AA.
AC Q8BKX6; E9QLR6; Q5DU42; Q6ZQC0; Q8BLU4; Q8BWJ5; Q8BXD3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein kinase SMG1;
DE Short=SMG-1;
DE EC=2.7.11.1;
DE AltName: Full=Lambda/iota protein kinase C-interacting protein {ECO:0000250|UniProtKB:Q96Q15};
DE Short=Lambda-interacting protein {ECO:0000250|UniProtKB:Q96Q15};
DE AltName: Full=Nonsense mediated mRNA decay-associated PI3K-related kinase SMG1 {ECO:0000312|MGI:MGI:1919742};
GN Name=Smg1 {ECO:0000312|MGI:MGI:1919742};
GN Synonyms=Atx {ECO:0000250|UniProtKB:Q96Q15},
GN Kiaa0421 {ECO:0000250|UniProtKB:Q96Q15},
GN Lip {ECO:0000250|UniProtKB:Q96Q15};
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]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2976-3658.
RC TISSUE=Fetal brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1996 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Head, Heart, and Vein;
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 [4]
RP PROTEIN SEQUENCE OF 67-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3567; THR-3570 AND THR-3574,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=32665638; DOI=10.1038/s41598-020-67834-5;
RA Snyder E., Chukrallah L., Seltzer K., Goodwin L., Braun R.E.;
RT "ADAD1 and ADAD2, testis-specific adenosine deaminase domain-containing
RT proteins, are required for male fertility.";
RL Sci. Rep. 10:11536-11536(2020).
CC -!- FUNCTION: Serine/threonine protein kinase involved in both mRNA
CC surveillance and genotoxic stress response pathways. Recognizes the
CC substrate consensus sequence [ST]-Q. Plays a central role in nonsense-
CC mediated decay (NMD) of mRNAs containing premature stop codons by
CC phosphorylating UPF1/RENT1. Recruited by release factors to stalled
CC ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase
CC complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3)
CC complex. In EJC-dependent NMD, the SURF complex associates with the
CC exon junction complex (EJC) through UPF2 and allows the formation of an
CC UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD.
CC Also acts as a genotoxic stress-activated protein kinase that displays
CC some functional overlap with ATM. Can phosphorylate p53/TP53 and is
CC required for optimal p53/TP53 activation after cellular exposure to
CC genotoxic stress. Its depletion leads to spontaneous DNA damage and
CC increased sensitivity to ionizing radiation (IR). May activate PRKCI
CC but not PRKCZ (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by caffeine, LY294002 and wortmannin.
CC -!- SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and
CC SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large
CC conformational change in the SMG1 C-terminal head domain containing the
CC catalytic domain. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3)
CC complex. Part of a complex composed of SMG1, DHX34 and UPF1; within the
CC complex DHX34 acts as a scaffolding protein to facilitate SMG1
CC phosphorylation of UPF1 (By similarity). Interacts with PRKCI.
CC Interacts with TELO2 and TTI1. Interacts with RUVBL1 and RUVBL2.
CC Interacts with DHX34 (via C-terminus); the interaction is RNA-
CC independent (By similarity). {ECO:0000250|UniProtKB:Q96Q15}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96Q15}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96Q15}. Note=Present in the chromatoid body.
CC {ECO:0000269|PubMed:32665638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BKX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKX6-2; Sequence=VSP_017749, VSP_017750;
CC Name=3;
CC IsoId=Q8BKX6-3; Sequence=VSP_017751, VSP_017752;
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q96Q15}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90238.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC131788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129136; BAC97946.1; -; mRNA.
DR EMBL; AK220328; BAD90238.1; ALT_INIT; mRNA.
DR EMBL; AK041264; BAC30884.2; -; mRNA.
DR EMBL; AK047829; BAC33168.2; -; mRNA.
DR EMBL; AK049391; BAC33729.1; -; mRNA.
DR EMBL; AK052331; BAC34941.1; -; mRNA.
DR CCDS; CCDS40102.1; -. [Q8BKX6-1]
DR RefSeq; NP_001026984.1; NM_001031814.1. [Q8BKX6-1]
DR SMR; Q8BKX6; -.
DR BioGRID; 231444; 6.
DR STRING; 10090.ENSMUSP00000032891; -.
DR iPTMnet; Q8BKX6; -.
DR PhosphoSitePlus; Q8BKX6; -.
DR EPD; Q8BKX6; -.
DR MaxQB; Q8BKX6; -.
DR PaxDb; Q8BKX6; -.
DR PeptideAtlas; Q8BKX6; -.
DR PRIDE; Q8BKX6; -.
DR ProteomicsDB; 257270; -. [Q8BKX6-1]
DR ProteomicsDB; 257271; -. [Q8BKX6-2]
DR ProteomicsDB; 257272; -. [Q8BKX6-3]
DR Antibodypedia; 6280; 215 antibodies from 16 providers.
DR DNASU; 233789; -.
DR Ensembl; ENSMUST00000032891; ENSMUSP00000032891; ENSMUSG00000030655. [Q8BKX6-1]
DR GeneID; 233789; -.
DR KEGG; mmu:233789; -.
DR UCSC; uc009jjp.1; mouse. [Q8BKX6-1]
DR UCSC; uc009jjq.1; mouse. [Q8BKX6-3]
DR UCSC; uc009jjr.1; mouse. [Q8BKX6-2]
DR CTD; 23049; -.
DR MGI; MGI:1919742; Smg1.
DR VEuPathDB; HostDB:ENSMUSG00000030655; -.
DR eggNOG; KOG0891; Eukaryota.
DR GeneTree; ENSGT00940000154776; -.
DR InParanoid; Q8BKX6; -.
DR OMA; EAIIMRH; -.
DR OrthoDB; 26975at2759; -.
DR PhylomeDB; Q8BKX6; -.
DR TreeFam; TF352560; -.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 233789; 15 hits in 113 CRISPR screens.
DR ChiTaRS; Smg1; mouse.
DR PRO; PR:Q8BKX6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BKX6; protein.
DR Bgee; ENSMUSG00000030655; Expressed in embryonic post-anal tail and 221 other tissues.
DR ExpressionAtlas; Q8BKX6; baseline and differential.
DR Genevisible; Q8BKX6; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR031559; SMG1.
DR InterPro; IPR035175; SMG1_N.
DR InterPro; IPR039414; SMG1_PIKKc.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR Pfam; PF17229; SMG1_N; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Kinase; Manganese;
KW Metal-binding; Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..3658
FT /note="Serine/threonine-protein kinase SMG1"
FT /id="PRO_0000229792"
FT DOMAIN 1281..1864
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1815..1850
FT /note="HEAT"
FT DOMAIN 2122..2461
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3626..3658
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2134
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2330..2338
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2350..2374
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3565..3588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3565..3580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 3547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q15"
FT MOD_RES 3553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q15"
FT MOD_RES 3567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3570
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3574
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 273..284
FT /note="LVMTSLQSILEN -> VRARDPQCSAVR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017749"
FT VAR_SEQ 285..3658
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017750"
FT VAR_SEQ 431..433
FT /note="LYR -> SVF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017751"
FT VAR_SEQ 434..3658
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017752"
FT CONFLICT 566
FT /note="I -> V (in Ref. 3; BAC33168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3658 AA; 409769 MW; 8C13F45BE0D35042 CRC64;
MSRRAPGSRL SSGGGGTKYP RSWNDWQPRT DSASADPDTL KYSSSRDRGV SSSYGLQPSN
SAVVSRQRHD DTRGHADIQN DEKGGYSVNG GSGENTYGRK SLGQELRINN VTSPEFTSVQ
HGSRALATKD MRKSQERSMS YSDESRLSNL LRRITREDDR DRRLATVKQL KEFIQQPENK
LVLVKQLDNI LAAVHDVLNE SSKLLQELRQ EGACCLGLLC ASLSYEAEKI FKWIFSKFSS
SAKDEVKLLY LCATYRALET VGEKKAFSSV MQLVMTSLQS ILENVDTPEL LCKCVKCILL
VARCYPHIFS TNFRDTVDIL VGWHIDHTQK PSLTQQVSGW LQSLEPFWVA DLAFSTTLLG
QFLEDMEAYA EDLSHVASGE SVDEDVPPPS VSLPKLAALL RVFSTVVRSI GERFSPIRGP
PITEAYVTDV LYRVMRCVTA ANQVFFSEAV LTAANECVGV LLGSLDPSMT IHCDMVITYG
LDQLENCQTC GTDYIISVLN LLTLIVEQIN TKLPSSFVEK LFIPSSKLLF LRYHKEKEVV
AVAHAVYQAV LSLKNIPVLE TAYKLILGEM TCALNNLLHS LQLPDACSEI KHEAFQNHVF
NIDNANFVVI FDLSALTTIG NAKNSLIGMW ALSPTVFALL SKNLMIVHSD LAVHFPAIQY
AVLYTLYSHC TRHDHFISSS LSSSSPSLFD GAVISTVTTA TKKHFSIILN LLGILLKKDN
LNQDTRKLLM TWALEVAVLM KKSETYAPLF SLPSFHKFSK GLLANTLVED VNICLQACSS
LHALSSSLPD DLLQRCVDVC RVQLVHSGTR IRQAFGKLLK SIPLDVVLSN NNHTEIQEIS
LALRSHMSKA PSNTFHPQDF SDVISFILYG NSHRTGKDNW LERLFYSCQR LDKRDQSTIP
RNLLKTDAVL WQWAIWEAAQ FTVLSKLRTP LGRAQDTFQT IEGIIRSLAA HTLNPDQDVS
QWTTADNDEG HGSNQLRLVL LLQYLENLEK LMYNAYEGCA NALTSPPKVI RTFFYTNRQT
CQDWLTRIRL SIMRVGLLAG QPAVTVRHGF DLLTEMKTNS LTQGSELEVT IMMVVEALCE
LHCPEAIQGI AVWSSSAVGK NLLWINSVAQ QAEGRFEKAS VEYQEHLCAM TGVDCCISSF
DKSVLTLANA GRNSASPKHS LNGESRKTVL SKSIDSSPEV ISYLGNKACE CYISIADWAA
VQEWQNAVHD LKKNSSSTSL NLKADFNYIK SLSSFESGEF VECTEQLELL PGENINLLAG
GSKEKIDMKK LLPNMLSPDP RELQKSIEVQ LLRSSVFLAT ALNHMEQDQK WQSLTENVVK
YLKQTSRIAI GPLRLSTLTV SQSLPVLSTL QLYCSSALEN TVSNRLSTED CLIPLFSDAL
RSCKQHDVRP WMQALRYTMY QNQLLEKIKE QTVPIRSHLM ELGLTAAKFA RKRGNVSLAT
RLLAQCSEVQ LGKTTTAQDL VQHFKKLSTQ GQVDEKWGPE LDIEKTKLLY TAGQSTHAME
MLSSCAISFC KSAKAEYAVA KSILTLAKWV QAEWKEISGQ LRQVYRAQQQ QNLSGLSTLS
RNILALIELP SANTVGEEHP RIESESTVHI GVGEPDFILG QLYHLSSVQA PEVAKSWAAL
ASWAYRWGRK VVDNASQGEG VRLLPREKSE VQNLLPDTIT EEEKERIYGI LGQAVCRPAG
IQDEDITLQI TESEDNEDDD MVDVIWRQLI SSCPWLSELD ENATEGVIKV WRKVVDRIFS
LYKLSCSAYF TFLKLNAGQV LLDEDDPRLH LSHRAEQSTD DVIVMATLRL LRLLVKHAGE
LRQYLEHGLE TTPTAPWRGI IPQLFSRLNH PEVYVRQSIC NLLCRVAQDS PHLILYPAIV
GTISLSSESQ ASGNKYSSAI PTLLGNIQGE ELLVSECEGG SPPASQDSNK DEPKSGLNED
QAMMQDCYSK IVDKLSSANP TMVLQVQMLV AELRRVTVLW DELWLGVLLQ QHMYVLRRIQ
QLEDEVKRVQ NNNTLRKEEK IAIMREKHTA LMKPIVFALE HVRSITAAPA ETPHEKWFQD
NYGDAIDNAL EKLKTPSNPA KPGSSWIPFK EIMLSLQQRA QKRASYILRL DEISPWLAAM
TNTEIALPGE VSARDTVTIH SVGGTITILP TKTKPKKLLF LGSDGKSYPY LFKGLEDLHL
DERIMQFLSI VNTMFATINR QETPRFHARH YSVTPLGTRS GLIQWVDGAT PLFGLYKRWQ
QREAALQAQK AQDSYQTPQN PSIVPRPSEL YYSKIGPALK TVGLSLDVSR RDWPLHVMKA
VLEELMEATP PNLLAKELWS SCTTPDEWWR VTQSYARSTA VMSMVGYIIG LGDRHLDNVL
IDMTTGEVVH IDYNVCFEKG KSLRVPEKVP FRMTQNIETA LGVTGVEGVF RLSCEQVLHI
MRRGRETLLT LLEAFVYDPL VDWTAGGEAG FAGAVYGGGG QQAESKQSKR EMEREITRSL
FSSRVAEIKV NWFKNRDEML VVLPKLDSSL DEYLSLQEQL TDVEKLQGKL LEEIEFLEGA
EGVDHPSHTL QHRYSEHTQL QTQQRAVQEA IQVKLNEFEQ WITHYQAAFN NLEATQLASL
LQEISTQMDL GPPSYVPATA FLQNAGQAHL ISQCEQLEGE VGALLQQRRS VLRGCLEQLH
HYATVALQYP KAIFQKHRIE QWKAWMEELI CNTTVERCQE LYRKYEMQYA PQPPPTVCQF
ITATEMTLQR YAADINSRLI RQVERLKQEA VTVPVCEDQL KEIERCIKVF LHENGEEGSL
SLASVIISAL CTLTRRNLMM EGAASSAGEQ LVDLTSRDGA WFLEELCSMS GNVTCLVQLL
KQCHLVPQDL DIPNPVEASE AVHLANGVYT SLQELNSNFR QIIFPEALRC LMKGECTLES
MLHELDSLIE QTTDGVPLQT LVESLQAYLR NTAMGLEEET HAHYIDVARM LHAQYGELIQ
PRNGSVDETP KMSAGQMLLV AFDGMFAQVE TAFGLLVEKL NKMEIPVAWR KIDIIREARS
TQVNFFDDDN HRQVLEEIFF LKRLQTIKEF FRLCGTFSKT LSGSSSLEDQ NTVNGPVQIV
NVKTLFRNSC FSEDQMAKPI KAFTADFVRQ LLIGLPNQAL GLTLCSFISA LGVDIIAQVE
AKDFGAESKV SVDDLCKKAV EHNIQVGKFS QLVMNRATVL ASSYDTAWKK HDLVRRLETS
ISSCKTSLQR VQLHIAMFQW QHEDLLISRP QAMSVTPPRS AILTSMKKKL HALSQIETSI
GTVQEKLAAL EASIEQRLKW AGGANPALAP VLQDFEATIA ERRNLVLKES QRANQVTFLC
SNIIHFESLR TRTAEALSLD AALFELIKRC QQMCSFASQF NSSVSELELR LLQRVDTTLE
HPIGSSEWLL SAHKQLTQDM STQRAVQTEK EQQIETVCET IQSLVDSVKT VLTGHNRQLG
DVKHLLKAMA KDEEAALADA EDIPYESSVR QFLAEYKSWQ DNIQTVLFTL VQAMGQVRSQ
EHVEMLQEIT PTLKELKTQS QSIYNNLVSF ASPLVTDAAN ECSSPTSSAT YQPSFAAAVR
SNTGQKTQPD VMSQNAKKLI QKNLATSADT PPSTIPGTGK SIACSPKKAV RDPKTGKAVQ
ERNSYAVSVW KRVKAKLEGR DVDPNRRMSV AEQVDYVIKE ATNLDNLAQL YEGWTAWV
