ID SMBP2_HUMAN Reviewed; 993 AA. AC P38935; A0PJD2; Q00443; Q14177; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 227. DE RecName: Full=DNA-binding protein SMUBP-2; DE EC=3.6.4.12 {ECO:0000269|PubMed:30218034}; DE EC=3.6.4.13 {ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:22965130}; DE AltName: Full=ATP-dependent helicase IGHMBP2; DE AltName: Full=Glial factor 1; DE Short=GF-1; DE AltName: Full=Immunoglobulin mu-binding protein 2; GN Name=IGHMBP2; Synonyms=SMBP2, SMUBP2; 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], FUNCTION, AND VARIANTS SER-201 AND VAL-275. RX PubMed=8349627; DOI=10.1016/s0021-9258(19)85357-7; RA Fukita Y., Mizuta T.-R., Shirozu M., Ozawa K., Shimizu A., Honjo T.; RT "The human S mu bp-2, a DNA-binding protein specific to the single-stranded RT guanine-rich sequence related to the immunoglobulin mu chain switch RT region."; RL J. Biol. Chem. 268:17463-17470(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10049831; DOI=10.1006/viro.1998.9588; RA Zhang Q., Wang Y.C., Montalvo E.A.; RT "Smubp-2 represses the Epstein-Barr virus lytic switch promoter."; RL Virology 255:160-170(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-868. RC TISSUE=Brain; 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] RP PROTEIN SEQUENCE OF 2-12; 221-233 AND 824-831, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 491-866. RC TISSUE=Brain; RX PubMed=1714899; DOI=10.1016/s0021-9258(18)98490-5; RA Kerr D., Khalili K.; RT "A recombinant cDNA derived from human brain encodes a DNA binding protein RT that stimulates transcription of the human neurotropic virus JCV."; RL J. Biol. Chem. 266:15876-15881(1991). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] RP FUNCTION AS AN ATP-DEPENDENT HELICASE, CATALYTIC ACTIVITY, INTERACTION WITH RP RIBOSOMES, AND CHARACTERIZATION OF VARIANTS HMNR1 ARG-196; ALA-221; RP ARG-241; LYS-382; PRO-445; ILE-493; ASN-565; ILE-583 AND HIS-603. RX PubMed=19158098; DOI=10.1093/hmg/ddp028; RA Guenther U.P., Handoko L., Laggerbauer B., Jablonka S., Chari A., RA Alzheimer M., Ohmer J., Ploettner O., Gehring N., Sickmann A., von Au K., RA Schuelke M., Fischer U.; RT "IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular RT disorder distal SMA type 1 (DSMA1)."; RL Hum. Mol. Genet. 18:1288-1300(2009). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RUVBL1; RUVBL2; RP GTF3C1 AND ABT1, AND TRNA-BINDING. RX PubMed=19299493; DOI=10.1093/hmg/ddp134; RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., RA Mourelatos Z.; RT "Biochemical and genetic evidence for a role of IGHMBP2 in the RT translational machinery."; RL Hum. Mol. Genet. 18:2115-2126(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30218034; DOI=10.1038/s41467-018-06313-y; RA Kanaan J., Raj S., Decourty L., Saveanu C., Croquette V., Le Hir H.; RT "UPF1-like helicase grip on nucleic acids dictates processivity."; RL Nat. Commun. 9:3752-3752(2018). RN [15] RP STRUCTURE BY NMR OF 709-794. RX PubMed=12547203; DOI=10.1016/s0022-2836(02)01381-5; RA Liepinsh E., Leonchiks A., Sharipo A., Guignard L., Otting G.; RT "Solution structure of the R3H domain from human Smubp-2."; RL J. Mol. Biol. 326:217-223(2003). RN [16] {ECO:0007744|PDB:2LRR} RP STRUCTURE BY NMR OF 711-786 IN COMPLEX WITH THE 5'-END OF SINGLE-STRANDED RP DNA, FUNCTION, AND DOMAIN. RX PubMed=22999958; DOI=10.1016/j.jmb.2012.09.010; RA Jaudzems K., Jia X., Yagi H., Zhulenkovs D., Graham B., Otting G., RA Liepinsh E.; RT "Structural basis for 5'-end-specific recognition of single-stranded DNA by RT the R3H domain from human Smubp-2."; RL J. Mol. Biol. 424:42-53(2012). RN [17] {ECO:0007744|PDB:4B3F, ECO:0007744|PDB:4B3G} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-648 IN COMPLEX WITH RNA, RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN. RX PubMed=22965130; DOI=10.1093/nar/gks792; RA Lim S.C., Bowler M.W., Lai T.F., Song H.; RT "The Ighmbp2 helicase structure reveals the molecular basis for disease- RT causing mutations in DMSA1."; RL Nucleic Acids Res. 40:11009-11022(2012). RN [18] RP VARIANTS HMNR1 ARG-213; LYS-514 AND ILE-580. RX PubMed=11528396; DOI=10.1038/ng703; RA Grohmann K., Schuelke M., Diers A., Hoffmann K., Lucke B., Adams C., RA Bertini E., Leonhardt-Horti H., Muntoni F., Ouvrier R., Pfeufer A., RA Rossi R., Van Maldergem L., Wilmshurst J.M., Wienker T.F., Sendtner M., RA Rudnik-Schoeneborn S., Zerres K., Huebner C.; RT "Mutations in the gene encoding immunoglobulin mu-binding protein 2 cause RT spinal muscular atrophy with respiratory distress type 1."; RL Nat. Genet. 29:75-77(2001). RN [19] RP VARIANTS HMNR1 PRO-192; ALA-221; ARG-241; LYS-334; PRO-361; PRO-364; RP LYS-382; PRO-426; ASN-565; LYS-572 DEL; PRO-577; ILE-583; CYS-586; HIS-603; RP CYS-637 AND GLU-974. RX PubMed=14681881; DOI=10.1002/ana.10755; RA Grohmann K., Varon R., Stolz P., Schuelke M., Janetzki C., Bertini E., RA Bushby K., Muntoni F., Ouvrier R., Van Maldergem L., Goemans N.M.L.A., RA Lochmueller H., Eichholz S., Adams C., Bosch F., Grattan-Smith P., RA Navarro C., Neitzel H., Polster T., Topaloglu H., Steglich C., RA Guenther U.P., Zerres K., Rudnik-Schoeneborn S., Huebner C.; RT "Infantile spinal muscular atrophy with respiratory distress type 1 RT (SMARD1)."; RL Ann. Neurol. 54:719-724(2003). RN [20] RP VARIANT HMNR1 LEU-369. RX PubMed=15290238; DOI=10.1007/s00439-004-1156-0; RA Guenther U.P., Schuelke M., Bertini E., D'Amico A., Goemans N., RA Grohmann K., Huebner C., Varon R.; RT "Genomic rearrangements at the IGHMBP2 gene locus in two patients with RT SMARD1."; RL Hum. Genet. 115:319-326(2004). RN [21] RP VARIANTS HMNR1 ARG-196; LEU-216; PRO-251; ASN-565; PRO-577; CYS-603 AND RP CYS-637. RX PubMed=15108294; DOI=10.1002/humu.9241; RA Maystadt I., Zarhrate M., Landrieu P., Boespflug-Tanguy O., Sukno S., RA Collignon P., Melki J., Verellen-Dumoulin C., Munnich A., Viollet L.; RT "Allelic heterogeneity of SMARD1 at the IGHMBP2 locus."; RL Hum. Mutat. 23:525-526(2004). RN [22] RP VARIANT LYS-879. RX PubMed=15797190; DOI=10.1016/j.pediatrneurol.2004.11.003; RA Tachi N., Kikuchi S., Kozuka N., Nogami A.; RT "A new mutation of IGHMBP2 gene in spinal muscular atrophy with respiratory RT distress type 1."; RL Pediatr. Neurol. 32:288-290(2005). RN [23] RP VARIANTS HMNR1 PRO-17; PRO-361; ARG-386; PRO-445; PRO-472 AND SER-581. RX PubMed=17431882; DOI=10.1002/humu.20525; RA Guenther U.P., Varon R., Schlicke M., Dutrannoy V., Volk A., Huebner C., RA von Au K., Schuelke M.; RT "Clinical and mutational profile in spinal muscular atrophy with RT respiratory distress (SMARD): defining novel phenotypes through RT hierarchical cluster analysis."; RL Hum. Mutat. 28:808-815(2007). RN [24] RP VARIANT HMNR1 ILE-493, AND CHARACTERIZATION OF VARIANT HMNR1 ILE-493. RX PubMed=18802676; DOI=10.1007/s00109-008-0402-7; RA Guenther U.P., Handoko L., Varon R., Stephani U., Tsao C.Y., Mendell J.R., RA Luetzkendorf S., Huebner C., von Au K., Jablonka S., Dittmar G., RA Heinemann U., Schuetz A., Schuelke M.; RT "Clinical variability in distal spinal muscular atrophy type 1 (DSMA1): RT determination of steady-state IGHMBP2 protein levels in five patients with RT infantile and juvenile disease."; RL J. Mol. Med. 87:31-41(2009). RN [25] RP INVOLVEMENT IN CMT2S, TISSUE SPECIFICITY, AND VARIANTS CMT2S VAL-202; RP GLY-373 AND THR-528. RX PubMed=25439726; DOI=10.1016/j.ajhg.2014.10.002; RA Cottenie E., Kochanski A., Jordanova A., Bansagi B., Zimon M., Horga A., RA Jaunmuktane Z., Saveri P., Rasic V.M., Baets J., Bartsakoulia M., RA Ploski R., Teterycz P., Nikolic M., Quinlivan R., Laura M., Sweeney M.G., RA Taroni F., Lunn M.P., Moroni I., Gonzalez M., Hanna M.G., Bettencourt C., RA Chabrol E., Franke A., von Au K., Schilhabel M., Kabzinska D., RA Hausmanowa-Petrusewicz I., Brandner S., Lim S.C., Song H., Choi B.O., RA Horvath R., Chung K.W., Zuchner S., Pareyson D., Harms M., Reilly M.M., RA Houlden H.; RT "Truncating and missense mutations in IGHMBP2 cause Charcot-Marie Tooth RT disease type 2."; RL Am. J. Hum. Genet. 95:590-601(2014). CC -!- FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplexes in an CC ATP-dependent reaction (PubMed:19158098, PubMed:30218034, CC PubMed:22999958). Specific to 5'-phosphorylated single-stranded CC guanine-rich sequences (PubMed:8349627, PubMed:22999958). May play a CC role in RNA metabolism, ribosome biogenesis or initiation of CC translation (PubMed:19299493, PubMed:19158098). May play a role in CC regulation of transcription (By similarity). Interacts with tRNA-Tyr CC (PubMed:19299493). {ECO:0000250|UniProtKB:Q9EQN5, CC ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:19299493, CC ECO:0000269|PubMed:22999958, ECO:0000269|PubMed:30218034, CC ECO:0000269|PubMed:8349627}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC Evidence={ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:30218034}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:30218034}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:22965130}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:22965130}; CC -!- SUBUNIT: Homooligomer (PubMed:19299493). Interacts with RUVBL1 CC (PubMed:19299493). Interacts with RUVBL2 (PubMed:19299493). Interacts CC with GTF3C1 (PubMed:19299493). Interacts with ABT1 (PubMed:19299493). CC Interacts with ribosomes (PubMed:19158098). CC {ECO:0000269|PubMed:19158098, ECO:0000269|PubMed:19299493}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19299493}. Cytoplasm CC {ECO:0000269|PubMed:19299493}. Cell projection, axon CC {ECO:0000250|UniProtKB:P40694}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Expressed in the CC developing and adult human brain, with highest expression in the CC cerebellum. Moderately expressed in fibroblasts. CC {ECO:0000269|PubMed:25439726}. CC -!- DOMAIN: The R3H domain recognizes phosphorylated 5'-ends of single- CC stranded nucleic acids which promotes binding of nucleic acids and CC stimulates ATPase activity. {ECO:0000269|PubMed:22965130, CC ECO:0000269|PubMed:22999958}. CC -!- DISEASE: Neuronopathy, distal hereditary motor, autosomal recessive 1 CC (HMNR1) [MIM:604320]: A form of distal hereditary motor neuronopathy, a CC heterogeneous group of neuromuscular disorders caused by selective CC degeneration of motor neurons in the anterior horn of the spinal cord, CC without sensory deficit in the posterior horn. The overall clinical CC picture consists of a classical distal muscular atrophy syndrome in the CC legs without clinical sensory loss. The disease starts with weakness CC and wasting of distal muscles of the anterior tibial and peroneal CC compartments of the legs. Later on, weakness and atrophy may expand to CC the proximal muscles of the lower limbs and/or to the distal upper CC limbs. {ECO:0000269|PubMed:11528396, ECO:0000269|PubMed:14681881, CC ECO:0000269|PubMed:15108294, ECO:0000269|PubMed:15290238, CC ECO:0000269|PubMed:17431882, ECO:0000269|PubMed:18802676, CC ECO:0000269|PubMed:19158098}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Charcot-Marie-Tooth disease, axonal, 2S (CMT2S) [MIM:616155]: CC An axonal form of Charcot-Marie-Tooth disease, a disorder of the CC peripheral nervous system, characterized by progressive weakness and CC atrophy, initially of the peroneal muscles and later of the distal CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two CC main groups on the basis of electrophysiologic properties and CC histopathology: primary peripheral demyelinating neuropathies CC (designated CMT1 when they are dominantly inherited) and primary CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group CC are characterized by signs of axonal degeneration in the absence of CC obvious myelin alterations, normal or slightly reduced nerve conduction CC velocities, and progressive distal muscle weakness and atrophy. CC {ECO:0000269|PubMed:25439726}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {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; L14754; AAA53082.1; -; mRNA. DR EMBL; L24544; AAA70430.1; -; Genomic_DNA. DR EMBL; AP000808; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC025299; AAH25299.1; -; mRNA. DR EMBL; M64979; AAA58611.1; -; mRNA. DR CCDS; CCDS8187.1; -. DR PIR; A47500; A47500. DR RefSeq; NP_002171.2; NM_002180.2. DR PDB; 1MSZ; NMR; -; A=711-786. DR PDB; 2LRR; NMR; -; A=711-786. DR PDB; 4B3F; X-ray; 2.50 A; X=3-648. DR PDB; 4B3G; X-ray; 2.85 A; A/B=3-648. DR PDBsum; 1MSZ; -. DR PDBsum; 2LRR; -. DR PDBsum; 4B3F; -. DR PDBsum; 4B3G; -. DR AlphaFoldDB; P38935; -. DR BMRB; P38935; -. DR SMR; P38935; -. DR BioGRID; 109728; 32. DR IntAct; P38935; 27. DR MINT; P38935; -. DR STRING; 9606.ENSP00000255078; -. DR GlyGen; P38935; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P38935; -. DR PhosphoSitePlus; P38935; -. DR SwissPalm; P38935; -. DR BioMuta; IGHMBP2; -. DR DMDM; 317373494; -. DR EPD; P38935; -. DR jPOST; P38935; -. DR MassIVE; P38935; -. DR MaxQB; P38935; -. DR PaxDb; 9606-ENSP00000255078; -. DR PeptideAtlas; P38935; -. DR ProteomicsDB; 55306; -. DR Pumba; P38935; -. DR Antibodypedia; 54271; 109 antibodies from 22 providers. DR DNASU; 3508; -. DR Ensembl; ENST00000255078.8; ENSP00000255078.4; ENSG00000132740.10. DR GeneID; 3508; -. DR KEGG; hsa:3508; -. DR MANE-Select; ENST00000255078.8; ENSP00000255078.4; NM_002180.3; NP_002171.2. DR UCSC; uc001ook.2; human. DR AGR; HGNC:5542; -. DR CTD; 3508; -. DR DisGeNET; 3508; -. DR GeneCards; IGHMBP2; -. DR GeneReviews; IGHMBP2; -. DR HGNC; HGNC:5542; IGHMBP2. DR HPA; ENSG00000132740; Low tissue specificity. DR MalaCards; IGHMBP2; -. DR MIM; 600502; gene. DR MIM; 604320; phenotype. DR MIM; 616155; phenotype. DR neXtProt; NX_P38935; -. DR OpenTargets; ENSG00000132740; -. DR Orphanet; 443073; Charcot-Marie-Tooth disease type 2S. DR Orphanet; 98920; Spinal muscular atrophy with respiratory distress type 1. DR PharmGKB; PA29731; -. DR VEuPathDB; HostDB:ENSG00000132740; -. DR eggNOG; KOG1803; Eukaryota. DR GeneTree; ENSGT00930000151035; -. DR HOGENOM; CLU_001666_5_0_1; -. DR InParanoid; P38935; -. DR OMA; TIIHGPP; -. DR OrthoDB; 170190at2759; -. DR PhylomeDB; P38935; -. DR TreeFam; TF105388; -. DR BRENDA; 3.6.4.12; 2681. DR PathwayCommons; P38935; -. DR SignaLink; P38935; -. DR BioGRID-ORCS; 3508; 22 hits in 1161 CRISPR screens. DR ChiTaRS; IGHMBP2; human. DR EvolutionaryTrace; P38935; -. DR GeneWiki; IGHMBP2; -. DR GenomeRNAi; 3508; -. DR Pharos; P38935; Tbio. DR PRO; PR:P38935; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P38935; Protein. DR Bgee; ENSG00000132740; Expressed in mucosa of stomach and 119 other cell types or tissues. DR ExpressionAtlas; P38935; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0032574; F:5'-3' RNA helicase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB. DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0003678; F:DNA helicase activity; TAS:ProtInc. DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB. DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:UniProtKB. DR CDD; cd18044; DEXXQc_SMUBP2; 1. DR CDD; cd02641; R3H_Smubp-2_like; 1. DR CDD; cd18808; SF1_C_Upf1; 1. DR Gene3D; 2.40.30.270; -; 1. DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 3.30.1370.50; R3H-like domain; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR035896; AN1-like_Znf. DR InterPro; IPR041679; DNA2/NAM7-like_C. DR InterPro; IPR041677; DNA2/NAM7_AAA_11. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001374; R3H_dom. DR InterPro; IPR036867; R3H_dom_sf. DR InterPro; IPR034072; R3H_Smubp-2. DR InterPro; IPR047187; SF1_C_Upf1. DR InterPro; IPR004483; SMUBP-2/Hcs1-like. DR InterPro; IPR048761; SMUBP-2_HCS1_1B. DR InterPro; IPR000058; Znf_AN1. DR NCBIfam; TIGR00376; IGHMBP2 family helicase; 1. DR PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1. DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1. DR Pfam; PF13086; AAA_11; 1. DR Pfam; PF13087; AAA_12; 1. DR Pfam; PF01424; R3H; 1. DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1. DR Pfam; PF01428; zf-AN1; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00393; R3H; 1. DR SMART; SM00154; ZnF_AN1; 1. DR SUPFAM; SSF118310; AN1-like Zinc finger; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF82708; R3H domain; 1. DR PROSITE; PS51061; R3H; 1. DR PROSITE; PS51039; ZF_AN1; 1. DR Genevisible; P38935; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; ATP-binding; Cell projection; KW Charcot-Marie-Tooth disease; Cytoplasm; Direct protein sequencing; KW Disease variant; DNA-binding; Helicase; Hydrolase; Metal-binding; KW Neurodegeneration; Neuropathy; Nucleotide-binding; Nucleus; KW Reference proteome; Ribonucleoprotein; RNA-binding; Transcription; KW Transcription regulation; tRNA-binding; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..993 FT /note="DNA-binding protein SMUBP-2" FT /id="PRO_0000080701" FT DOMAIN 723..786 FT /note="R3H" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382" FT ZN_FING 891..940 FT /note="AN1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT REGION 638..785 FT /note="SS DNA-binding" FT /evidence="ECO:0000269|PubMed:8349627, FT ECO:0000305|PubMed:22999958" FT REGION 651..723 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 782..828 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 841..879 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 971..993 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 864..868 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 651..682 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 704..718 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..816 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 843..857 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 214..221 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499" FT BINDING 403 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q92900" FT BINDING 442 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q92900" FT BINDING 571 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q92900" FT BINDING 897 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 902 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 913 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 916 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 921 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 924 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 930 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT BINDING 932 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT VARIANT 17 FT /note="L -> P (in HMNR1; dbSNP:rs1594412120)" FT /evidence="ECO:0000269|PubMed:17431882" FT /id="VAR_058497" FT VARIANT 75 FT /note="A -> T (in dbSNP:rs2228206)" FT /id="VAR_055225" FT VARIANT 192 FT /note="L -> P (in HMNR1; dbSNP:rs879253996)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022321" FT VARIANT 196 FT /note="Q -> R (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs1594422506)" FT /evidence="ECO:0000269|PubMed:15108294, FT ECO:0000269|PubMed:19158098" FT /id="VAR_058498" FT VARIANT 201 FT /note="L -> S (in dbSNP:rs560096)" FT /evidence="ECO:0000269|PubMed:8349627" FT /id="VAR_024242" FT VARIANT 202 FT /note="F -> V (in CMT2S; dbSNP:rs724159958)" FT /evidence="ECO:0000269|PubMed:25439726" FT /id="VAR_072694" FT VARIANT 213 FT /note="H -> R (in HMNR1; dbSNP:rs137852666)" FT /evidence="ECO:0000269|PubMed:11528396" FT /id="VAR_022322" FT VARIANT 216 FT /note="P -> L (in HMNR1; dbSNP:rs1594422676)" FT /evidence="ECO:0000269|PubMed:15108294" FT /id="VAR_058499" FT VARIANT 221 FT /note="T -> A (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs1594422709)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:19158098" FT /id="VAR_022323" FT VARIANT 241 FT /note="C -> R (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs1594427373)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:19158098" FT /id="VAR_022324" FT VARIANT 251 FT /note="L -> P (in HMNR1; dbSNP:rs1594427489)" FT /evidence="ECO:0000269|PubMed:15108294" FT /id="VAR_058500" FT VARIANT 275 FT /note="I -> V (in dbSNP:rs10896380)" FT /evidence="ECO:0000269|PubMed:8349627" FT /id="VAR_024243" FT VARIANT 334 FT /note="E -> K (in HMNR1; dbSNP:rs1594431740)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022325" FT VARIANT 361 FT /note="L -> P (in HMNR1; dbSNP:rs201060167)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:17431882" FT /id="VAR_022326" FT VARIANT 364 FT /note="L -> P (in HMNR1; dbSNP:rs1594445394)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022327" FT VARIANT 369 FT /note="F -> L (in HMNR1; dbSNP:rs137852670)" FT /evidence="ECO:0000269|PubMed:15290238" FT /id="VAR_072695" FT VARIANT 373 FT /note="V -> G (in CMT2S; dbSNP:rs724159959)" FT /evidence="ECO:0000269|PubMed:25439726" FT /id="VAR_072696" FT VARIANT 382 FT /note="E -> K (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs776730737)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:19158098" FT /id="VAR_022328" FT VARIANT 386 FT /note="W -> R (in HMNR1; dbSNP:rs759641927)" FT /evidence="ECO:0000269|PubMed:17431882" FT /id="VAR_058501" FT VARIANT 426 FT /note="L -> P (in HMNR1; dbSNP:rs1555247218)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022329" FT VARIANT 445 FT /note="H -> P (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs571142182)" FT /evidence="ECO:0000269|PubMed:17431882, FT ECO:0000269|PubMed:19158098" FT /id="VAR_058502" FT VARIANT 472 FT /note="L -> P (in HMNR1; dbSNP:rs1594451536)" FT /evidence="ECO:0000269|PubMed:17431882" FT /id="VAR_058503" FT VARIANT 493 FT /note="T -> I (in HMNR1; does not affect activity; reduces FT protein steady-state levels; dbSNP:rs780594709)" FT /evidence="ECO:0000269|PubMed:18802676, FT ECO:0000269|PubMed:19158098" FT /id="VAR_058504" FT VARIANT 514 FT /note="E -> K (in HMNR1; dbSNP:rs137852665)" FT /evidence="ECO:0000269|PubMed:11528396" FT /id="VAR_022330" FT VARIANT 528 FT /note="A -> T (in CMT2S; dbSNP:rs724159960)" FT /evidence="ECO:0000269|PubMed:25439726" FT /id="VAR_072697" FT VARIANT 557 FT /note="P -> A (in dbSNP:rs7122089)" FT /id="VAR_055226" FT VARIANT 565 FT /note="D -> N (in HMNR1; does not affect ATPase activity; FT loss of helicase activity on RNA duplices; FT dbSNP:rs770111639)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:15108294, ECO:0000269|PubMed:19158098" FT /id="VAR_022331" FT VARIANT 572 FT /note="Missing (in HMNR1; dbSNP:rs775542203)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022332" FT VARIANT 577 FT /note="L -> P (in HMNR1; dbSNP:rs1483165002)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:15108294" FT /id="VAR_022333" FT VARIANT 580 FT /note="V -> I (in HMNR1; dbSNP:rs137852667)" FT /evidence="ECO:0000269|PubMed:11528396" FT /id="VAR_022334" FT VARIANT 581 FT /note="R -> S (in HMNR1; dbSNP:rs1594454382)" FT /evidence="ECO:0000269|PubMed:17431882" FT /id="VAR_058505" FT VARIANT 583 FT /note="N -> I (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs1594454388)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:19158098" FT /id="VAR_022335" FT VARIANT 586 FT /note="G -> C (in HMNR1)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022336" FT VARIANT 603 FT /note="R -> C (in HMNR1; dbSNP:rs1465803265)" FT /evidence="ECO:0000269|PubMed:15108294" FT /id="VAR_058506" FT VARIANT 603 FT /note="R -> H (in HMNR1; severe reduction of ATPase FT activity and loss of helicase activity on RNA duplices; FT dbSNP:rs151079750)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:19158098" FT /id="VAR_022337" FT VARIANT 637 FT /note="R -> C (in HMNR1; dbSNP:rs201563456)" FT /evidence="ECO:0000269|PubMed:14681881, FT ECO:0000269|PubMed:15108294" FT /id="VAR_022338" FT VARIANT 671 FT /note="T -> A (in dbSNP:rs622082)" FT /id="VAR_020147" FT VARIANT 694 FT /note="R -> W (in dbSNP:rs2236654)" FT /id="VAR_021899" FT VARIANT 879 FT /note="T -> K (in dbSNP:rs17612126)" FT /evidence="ECO:0000269|PubMed:15797190" FT /id="VAR_022339" FT VARIANT 928 FT /note="E -> K (in dbSNP:rs2275996)" FT /id="VAR_021900" FT VARIANT 974 FT /note="D -> E (in HMNR1; uncertain significance; FT dbSNP:rs147674615)" FT /evidence="ECO:0000269|PubMed:14681881" FT /id="VAR_022340" FT CONFLICT 292 FT /note="I -> N (in Ref. 1; AAA53082)" FT /evidence="ECO:0000305" FT CONFLICT 461 FT /note="L -> V (in Ref. 1; AAA53082)" FT /evidence="ECO:0000305" FT CONFLICT 491..494 FT /note="VDTA -> GGRV (in Ref. 6; AAA58611)" FT /evidence="ECO:0000305" FT CONFLICT 863 FT /note="E -> K (in Ref. 6; AAA58611)" FT /evidence="ECO:0000305" FT CONFLICT 866 FT /note="K -> T (in Ref. 6; AAA58611)" FT /evidence="ECO:0000305" FT HELIX 4..33 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 45..57 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 63..70 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:4B3G" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 102..110 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 142..156 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:4B3G" FT HELIX 164..170 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:4B3G" FT HELIX 194..205 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 207..213 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 220..233 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 238..244 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 245..257 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 285..288 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 293..300 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:4B3G" FT TURN 305..308 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 320..344 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 346..351 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 352..355 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 360..363 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 370..374 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 382..385 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 392..399 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 411..415 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 416..419 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 422..430 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 440..444 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 446..456 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 465..469 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 482..485 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 487..492 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 512..527 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 535..540 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 542..552 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 560..563 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 572..578 FT /evidence="ECO:0007829|PDB:4B3F" FT TURN 589..592 FT /evidence="ECO:0007829|PDB:4B3G" FT HELIX 594..602 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 604..612 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 621..632 FT /evidence="ECO:0007829|PDB:4B3F" FT STRAND 633..638 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 639..641 FT /evidence="ECO:0007829|PDB:4B3F" FT HELIX 727..739 FT /evidence="ECO:0007829|PDB:1MSZ" FT STRAND 742..746 FT /evidence="ECO:0007829|PDB:1MSZ" FT HELIX 753..764 FT /evidence="ECO:0007829|PDB:1MSZ" FT STRAND 767..772 FT /evidence="ECO:0007829|PDB:1MSZ" FT STRAND 774..776 FT /evidence="ECO:0007829|PDB:1MSZ" FT STRAND 779..784 FT /evidence="ECO:0007829|PDB:1MSZ" SQ SEQUENCE 993 AA; 109149 MW; DE785579EE60E26F CRC64; MASAAVESFV TKQLDLLELE RDAEVEERRS WQENISLKEL QSRGVCLLKL QVSSQRTGLY GRLLVTFEPR RYGSAAALPS NSFTSGDIVG LYDAANEGSQ LATGILTRVT QKSVTVAFDE SHDFQLSLDR ENSYRLLKLA NDVTYRRLKK ALIALKKYHS GPASSLIEVL FGRSAPSPAS EIHPLTFFNT CLDTSQKEAV LFALSQKELA IIHGPPGTGK TTTVVEIILQ AVKQGLKVLC CAPSNIAVDN LVERLALCKQ RILRLGHPAR LLESIQQHSL DAVLARSDSA QIVADIRKDI DQVFVKNKKT QDKREKSNFR NEIKLLRKEL KEREEAAMLE SLTSANVVLA TNTGASADGP LKLLPESYFD VVVIDECAQA LEASCWIPLL KARKCILAGD HKQLPPTTVS HKAALAGLSL SLMERLAEEY GARVVRTLTV QYRMHQAIMR WASDTMYLGQ LTAHSSVARH LLRDLPGVAA TEETGVPLLL VDTAGCGLFE LEEEDEQSKG NPGEVRLVSL HIQALVDAGV PARDIAVVSP YNLQVDLLRQ SLVHRHPELE IKSVDGFQGR EKEAVILSFV RSNRKGEVGF LAEDRRINVA VTRARRHVAV ICDSRTVNNH AFLKTLVEYF TQHGEVRTAF EYLDDIVPEN YSHENSQGSS HAATKPQGPA TSTRTGSQRQ EGGQEAAAPA RQGRKKPAGK SLASEAPSQP SLNGGSPEGV ESQDGVDHFR AMIVEFMASK KMQLEFPPSL NSHDRLRVHQ IAEEHGLRHD SSGEGKRRFI TVSKRAPRPR AALGPPAGTG GPAPLQPVPP TPAQTEQPPR EQRGPDQPDL RTLHLERLQR VRSAQGQPAS KEQQASGQQK LPEKKKKKAK GHPATDLPTE EDFEALVSAA VKADNTCGFA KCTAGVTTLG QFCQLCSRRY CLSHHLPEIH GCGERARAHA RQRISREGVL YAGSGTKNGS LDPAKRAQLQ RRLDKKLSEL SNQRTSRRKE RGT //