SMBP2_HUMAN
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 03-AUG-2022, entry version 218.
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 HMN6 ARG-196; ALA-221; ARG-241;
RP 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 HMN6 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 HMN6 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 HMN6 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 HMN6 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 HMN6 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 HMN6 ILE-493, AND CHARACTERIZATION OF VARIANT HMN6 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, 6 (HMN6) [MIM:604320]:
CC A neuromuscular disorder. Distal hereditary motor neuronopathies
CC constitute a heterogeneous group of neuromuscular disorders caused by
CC selective degeneration of motor neurons in the anterior horn of the
CC spinal cord, without sensory deficit in the posterior horn. The overall
CC clinical picture consists of a classical distal muscular atrophy
CC syndrome in the legs without clinical sensory loss. The disease starts
CC with weakness and wasting of distal muscles of the anterior tibial and
CC peroneal compartments of the legs. Later on, weakness and atrophy may
CC expand to the proximal muscles of the lower limbs and/or to the distal
CC upper 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 2S (CMT2S) [MIM:616155]: An axonal
CC form of Charcot-Marie-Tooth disease, a disorder of the peripheral
CC nervous system, characterized by progressive weakness and atrophy,
CC initially of the peroneal muscles and later of the distal muscles of
CC the arms. Charcot-Marie-Tooth disease is classified in two main groups
CC on the basis of electrophysiologic properties and histopathology:
CC primary peripheral demyelinating neuropathies (designated CMT1 when
CC they are dominantly inherited) and primary peripheral axonal
CC neuropathies (CMT2). Neuropathies of the CMT2 group are characterized
CC by signs of axonal degeneration in the absence of obvious myelin
CC alterations, normal or slightly reduced nerve conduction velocities,
CC 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}.
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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; 29.
DR IntAct; P38935; 25.
DR STRING; 9606.ENSP00000255078; -.
DR iPTMnet; P38935; -.
DR PhosphoSitePlus; P38935; -.
DR BioMuta; IGHMBP2; -.
DR DMDM; 317373494; -.
DR EPD; P38935; -.
DR jPOST; P38935; -.
DR MassIVE; P38935; -.
DR MaxQB; P38935; -.
DR PaxDb; P38935; -.
DR PeptideAtlas; P38935; -.
DR PRIDE; P38935; -.
DR ProteomicsDB; 55306; -.
DR Antibodypedia; 54271; 97 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 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; YKRMEST; -.
DR OrthoDB; 633768at2759; -.
DR PhylomeDB; P38935; -.
DR TreeFam; TF105388; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; P38935; -.
DR SignaLink; P38935; -.
DR BioGRID-ORCS; 3508; 21 hits in 1083 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 117 other tissues.
DR ExpressionAtlas; P38935; baseline and differential.
DR Genevisible; P38935; HS.
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; cd02641; R3H_Smubp-2_like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 4.10.1110.10; -; 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; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01424; R3H; 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; SSF118310; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR TIGRFAMs; TIGR00376; TIGR00376; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
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 HMN6; 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 HMN6; dbSNP:rs879253996)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022321"
FT VARIANT 196
FT /note="Q -> R (in HMN6; severe reduction of ATPase activity
FT 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 HMN6; dbSNP:rs137852666)"
FT /evidence="ECO:0000269|PubMed:11528396"
FT /id="VAR_022322"
FT VARIANT 216
FT /note="P -> L (in HMN6; dbSNP:rs1594422676)"
FT /evidence="ECO:0000269|PubMed:15108294"
FT /id="VAR_058499"
FT VARIANT 221
FT /note="T -> A (in HMN6; severe reduction of ATPase activity
FT 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 HMN6; severe reduction of ATPase activity
FT 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 HMN6; 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 HMN6; dbSNP:rs1594431740)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022325"
FT VARIANT 361
FT /note="L -> P (in HMN6; 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 HMN6; dbSNP:rs1594445394)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022327"
FT VARIANT 369
FT /note="F -> L (in HMN6; 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 HMN6; severe reduction of ATPase activity
FT 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 HMN6; dbSNP:rs759641927)"
FT /evidence="ECO:0000269|PubMed:17431882"
FT /id="VAR_058501"
FT VARIANT 426
FT /note="L -> P (in HMN6; dbSNP:rs1555247218)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022329"
FT VARIANT 445
FT /note="H -> P (in HMN6; severe reduction of ATPase activity
FT 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 HMN6; dbSNP:rs1594451536)"
FT /evidence="ECO:0000269|PubMed:17431882"
FT /id="VAR_058503"
FT VARIANT 493
FT /note="T -> I (in HMN6; 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 HMN6; 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 HMN6; 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 HMN6; dbSNP:rs775542203)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022332"
FT VARIANT 577
FT /note="L -> P (in HMN6; 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 HMN6; dbSNP:rs137852667)"
FT /evidence="ECO:0000269|PubMed:11528396"
FT /id="VAR_022334"
FT VARIANT 581
FT /note="R -> S (in HMN6; dbSNP:rs1594454382)"
FT /evidence="ECO:0000269|PubMed:17431882"
FT /id="VAR_058505"
FT VARIANT 583
FT /note="N -> I (in HMN6; severe reduction of ATPase activity
FT 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 HMN6)"
FT /evidence="ECO:0000269|PubMed:14681881"
FT /id="VAR_022336"
FT VARIANT 603
FT /note="R -> C (in HMN6; dbSNP:rs1465803265)"
FT /evidence="ECO:0000269|PubMed:15108294"
FT /id="VAR_058506"
FT VARIANT 603
FT /note="R -> H (in HMN6; severe reduction of ATPase activity
FT 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 HMN6; 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 HMN6; unknown pathological 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
