SMU1_HUMAN
ID SMU1_HUMAN Reviewed; 513 AA.
AC Q2TAY7; B4E3L0; Q9BU59; Q9HA96; Q9NVD1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=WD40 repeat-containing protein SMU1;
DE AltName: Full=Smu-1 suppressor of mec-8 and unc-52 protein homolog;
DE Contains:
DE RecName: Full=WD40 repeat-containing protein SMU1, N-terminally processed;
GN Name=SMU1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Skin;
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 [4]
RP PROTEIN SEQUENCE OF 2-12; 114-123; 275-287 AND 318-332, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP IDENTIFICATION.
RX PubMed=15878348; DOI=10.1016/j.yexcr.2005.02.017;
RA Sugaya K., Hongo E., Tsuji H.;
RT "A temperature-sensitive mutation in the WD repeat-containing protein Smu1
RT is related to maintenance of chromosome integrity.";
RL Exp. Cell Res. 306:242-251(2005).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP SUBUNIT, AND INTERACTION WITH IK.
RX PubMed=22365833; DOI=10.1016/j.molcel.2011.12.034;
RA Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S., Weimann M.,
RA Will C.L., Pena V., Luehrmann R., Stelzl U.;
RT "Dynamic protein-protein interaction wiring of the human spliceosome.";
RL Mol. Cell 45:567-580(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH IK,
RP IDENTIFICATION IN A COMPLEX WITH INFLUENZA A VIRUS RNA POLYMERASE SUBUNITS
RP PB1 AND PB2 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=24945353; DOI=10.1371/journal.ppat.1004164;
RA Fournier G., Chiang C., Munier S., Tomoiu A., Demeret C., Vidalain P.O.,
RA Jacob Y., Naffakh N.;
RT "Recruitment of RED-SMU1 complex by Influenza A Virus RNA polymerase to
RT control Viral mRNA splicing.";
RL PLoS Pathog. 10:E1004164-E1004164(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-379, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
RP INTERACTION WITH IK, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome (PubMed:28781166). Regulates alternative splicing of the
CC HSPG2 pre-mRNA (By similarity). Required for normal accumulation of IK
CC (PubMed:24945353). Required for normal mitotic spindle assembly and
CC normal progress through mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q76B40, ECO:0000269|PubMed:24945353,
CC ECO:0000269|PubMed:28781166, ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Required, together with IK, for normal
CC splicing of influenza A virus NS1 pre-mRNA, which is required for the
CC production of the exportin NS2 and for the production of influenza A
CC virus particles. Not required for the production of VSV virus
CC particles. {ECO:0000269|PubMed:24945353}.
CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:22365833,
CC PubMed:28781166). Interacts with IK (PubMed:28781166, PubMed:24945353,
CC PubMed:22365833). {ECO:0000269|PubMed:22365833,
CC ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: (Microbial infection) Identified in a complex with IK and
CC influenza A virus RNA polymerase subunits PB1 and PB2; does not
CC directly interact with the viral proteins by itself.
CC {ECO:0000269|PubMed:22365833}.
CC -!- INTERACTION:
CC Q2TAY7; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-298027, EBI-11156432;
CC Q2TAY7; Q13123: IK; NbExp=6; IntAct=EBI-298027, EBI-713456;
CC Q2TAY7; Q9Y605: MRFAP1; NbExp=5; IntAct=EBI-298027, EBI-995714;
CC Q2TAY7; Q96HT8: MRFAP1L1; NbExp=7; IntAct=EBI-298027, EBI-748896;
CC Q2TAY7; Q4VC12: MSS51; NbExp=3; IntAct=EBI-298027, EBI-11599933;
CC Q2TAY7; P49821: NDUFV1; NbExp=3; IntAct=EBI-298027, EBI-748312;
CC Q2TAY7; A6NK89: RASSF10; NbExp=3; IntAct=EBI-298027, EBI-6912267;
CC Q2TAY7; O43711: TLX3; NbExp=3; IntAct=EBI-298027, EBI-3939165;
CC Q2TAY7; O76024: WFS1; NbExp=3; IntAct=EBI-298027, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99M63}. Nucleus
CC {ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q76B40}. Note=Colocalizes with SRSF1 in
CC nuclear speckles. {ECO:0000250|UniProtKB:Q76B40}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2TAY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TAY7-2; Sequence=VSP_056394;
CC -!- DOMAIN: The WD repeats assemble into a seven-bladed WD propeller.
CC {ECO:0000250|UniProtKB:G5EEG7}.
CC -!- SIMILARITY: Belongs to the WD repeat SMU1 family. {ECO:0000305}.
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DR EMBL; AK001667; BAA91822.1; -; mRNA.
DR EMBL; AK022032; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK304767; BAG65522.1; -; mRNA.
DR EMBL; AL162590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002876; AAH02876.1; -; mRNA.
DR EMBL; BC110654; AAI10655.1; -; mRNA.
DR CCDS; CCDS6534.1; -. [Q2TAY7-1]
DR RefSeq; NP_060695.2; NM_018225.2. [Q2TAY7-1]
DR PDB; 5O9Z; EM; 4.50 A; L=1-513.
DR PDB; 6AHD; EM; 3.80 A; Y=1-513.
DR PDB; 6Q8F; X-ray; 1.90 A; A/B=2-513.
DR PDB; 6Q8I; X-ray; 3.17 A; A/B/E/F/I/J/M/N=2-513.
DR PDB; 6Q8J; X-ray; 1.80 A; A=2-196.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6Q8F; -.
DR PDBsum; 6Q8I; -.
DR PDBsum; 6Q8J; -.
DR AlphaFoldDB; Q2TAY7; -.
DR SMR; Q2TAY7; -.
DR BioGRID; 120528; 124.
DR CORUM; Q2TAY7; -.
DR IntAct; Q2TAY7; 37.
DR MINT; Q2TAY7; -.
DR STRING; 9606.ENSP00000380336; -.
DR GlyGen; Q2TAY7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2TAY7; -.
DR MetOSite; Q2TAY7; -.
DR PhosphoSitePlus; Q2TAY7; -.
DR SwissPalm; Q2TAY7; -.
DR BioMuta; SMU1; -.
DR DMDM; 109939732; -.
DR EPD; Q2TAY7; -.
DR jPOST; Q2TAY7; -.
DR MassIVE; Q2TAY7; -.
DR MaxQB; Q2TAY7; -.
DR PaxDb; Q2TAY7; -.
DR PeptideAtlas; Q2TAY7; -.
DR PRIDE; Q2TAY7; -.
DR ProteomicsDB; 5908; -.
DR ProteomicsDB; 61473; -. [Q2TAY7-1]
DR Antibodypedia; 10816; 110 antibodies from 24 providers.
DR DNASU; 55234; -.
DR Ensembl; ENST00000397149.4; ENSP00000380336.3; ENSG00000122692.9. [Q2TAY7-1]
DR GeneID; 55234; -.
DR KEGG; hsa:55234; -.
DR MANE-Select; ENST00000397149.4; ENSP00000380336.3; NM_018225.3; NP_060695.2.
DR UCSC; uc003zsf.2; human. [Q2TAY7-1]
DR CTD; 55234; -.
DR DisGeNET; 55234; -.
DR GeneCards; SMU1; -.
DR HGNC; HGNC:18247; SMU1.
DR HPA; ENSG00000122692; Low tissue specificity.
DR MIM; 617811; gene.
DR neXtProt; NX_Q2TAY7; -.
DR OpenTargets; ENSG00000122692; -.
DR PharmGKB; PA134903890; -.
DR VEuPathDB; HostDB:ENSG00000122692; -.
DR eggNOG; KOG0275; Eukaryota.
DR GeneTree; ENSGT00940000155007; -.
DR HOGENOM; CLU_000288_57_38_1; -.
DR InParanoid; Q2TAY7; -.
DR OMA; FIEVWNY; -.
DR PhylomeDB; Q2TAY7; -.
DR TreeFam; TF313969; -.
DR PathwayCommons; Q2TAY7; -.
DR SignaLink; Q2TAY7; -.
DR BioGRID-ORCS; 55234; 809 hits in 1047 CRISPR screens.
DR ChiTaRS; SMU1; human.
DR GeneWiki; SMU1; -.
DR GenomeRNAi; 55234; -.
DR Pharos; Q2TAY7; Tbio.
DR PRO; PR:Q2TAY7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q2TAY7; protein.
DR Bgee; ENSG00000122692; Expressed in medial globus pallidus and 199 other tissues.
DR ExpressionAtlas; Q2TAY7; baseline and differential.
DR Genevisible; Q2TAY7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR045184; SMU1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22848; PTHR22848; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..513
FT /note="WD40 repeat-containing protein SMU1"
FT /id="PRO_0000424520"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..513
FT /note="WD40 repeat-containing protein SMU1, N-terminally
FT processed"
FT /id="PRO_0000237590"
FT DOMAIN 6..38
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 40..92
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 212..253
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 262..303
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 305..346
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 347..386
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 395..436
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 440..479
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 482..513
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..315
FT /note="Required for interaction with IK and with influenza
FT A virus RNA polymerase"
FT /evidence="ECO:0000269|PubMed:24945353"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylserine; in WD40 repeat-containing protein
FT SMU1, N-terminally processed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056394"
FT CONFLICT 62
FT /note="A -> V (in Ref. 3; AAI10655)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="I -> V (in Ref. 1; AK022032)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="G -> R (in Ref. 1; AK022032)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="L -> P (in Ref. 1; BAA91822)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="G -> A (in Ref. 3; AAI10655)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6Q8I"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:6Q8J"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6Q8I"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:6Q8J"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:6Q8J"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6Q8I"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6Q8J"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6Q8F"
SQ SEQUENCE 513 AA; 57544 MW; CB201E939DCCA188 CRC64;
MSIEIESSDV IRLIMQYLKE NSLHRALATL QEETTVSLNT VDSIESFVAD INSGHWDTVL
QAIQSLKLPD KTLIDLYEQV VLELIELREL GAARSLLRQT DPMIMLKQTQ PERYIHLENL
LARSYFDPRE AYPDGSSKEK RRAAIAQALA GEVSVVPPSR LMALLGQALK WQQHQGLLPP
GMTIDLFRGK AAVKDVEEEK FPTQLSRHIK FGQKSHVECA RFSPDGQYLV TGSVDGFIEV
WNFTTGKIRK DLKYQAQDNF MMMDDAVLCM CFSRDTEMLA TGAQDGKIKV WKIQSGQCLR
RFERAHSKGV TCLSFSKDSS QILSASFDQT IRIHGLKSGK TLKEFRGHSS FVNEATFTQD
GHYIISASSD GTVKIWNMKT TECSNTFKSL GSTAGTDITV NSVILLPKNP EHFVVCNRSN
TVVIMNMQGQ IVRSFSSGKR EGGDFVCCAL SPRGEWIYCV GEDFVLYCFS TVTGKLERTL
TVHEKDVIGI AHHPHQNLIA TYSEDGLLKL WKP
