RMI2_HUMAN
ID RMI2_HUMAN Reviewed; 147 AA.
AC Q96E14; B3KVZ6; Q49AE2; Q8TBL0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=RecQ-mediated genome instability protein 2;
DE Short=hRMI2;
DE AltName: Full=BLM-associated protein of 18 kDa;
DE Short=BLAP18;
GN Name=RMI2; Synonyms=C16orf75;
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] (ISOFORM 1).
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Lymph, Skin, and Testis;
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 FUNCTION, IDENTIFICATION IN THE RMI COMPLEX, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-121.
RX PubMed=18923082; DOI=10.1101/gad.1708608;
RA Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W.,
RA Hoatlin M.E., Hickson I.D., Wang W.;
RT "RMI, a new OB-fold complex essential for Bloom syndrome protein to
RT maintain genome stability.";
RL Genes Dev. 22:2843-2855(2008).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE RMI COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-24; TRP-59; LYS-100;
RP LYS-121 AND TRP-135.
RX PubMed=18923083; DOI=10.1101/gad.1725108;
RA Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H.,
RA Andreassen P.R., Sung P., Meetei A.R.;
RT "BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component
RT of the Bloom helicase-double Holliday junction dissolvasome.";
RL Genes Dev. 22:2856-2868(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP 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 [10]
RP FUNCTION, AND PROBABLE INVOLVEMENT IN BLOOM-LIKE SYNDROME.
RX PubMed=27977684; DOI=10.1371/journal.pgen.1006483;
RA Hudson D.F., Amor D.J., Boys A., Butler K., Williams L., Zhang T.,
RA Kalitsis P.;
RT "Loss of RMI2 increases genome instability and causes a Bloom-like
RT syndrome.";
RL PLoS Genet. 12:E1006483-E1006483(2016).
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates. It is required to regulate sister chromatid segregation
CC and to limit DNA crossover. Essential for the stability, localization,
CC and function of BLM, TOP3A, and complexes containing BLM. In the RMI
CC complex, it is required to target BLM to chromatin and stress-induced
CC nuclear foci and mitotic phosphorylation of BLM.
CC {ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083,
CC ECO:0000269|PubMed:27977684}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC and RMI2. The RMI complex interacts with BLM.
CC {ECO:0000269|PubMed:18923082, ECO:0000269|PubMed:18923083}.
CC -!- INTERACTION:
CC Q96E14; Q9H9A7: RMI1; NbExp=4; IntAct=EBI-2555534, EBI-621339;
CC Q96E14-1; Q9H9A7: RMI1; NbExp=13; IntAct=EBI-15876491, EBI-621339;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18923082}.
CC Note=Colocalizes with BLM at nuclear DNA repair foci.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96E14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96E14-2; Sequence=VSP_027287;
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:18923083}.
CC -!- DISEASE: Note=A homozygous deletion of RMI2 has been found in a family
CC with a Bloom-like syndrome and is probable responsible for the
CC phenotype. Patients manifest depigmented skin lesions, multiple cafe-
CC au-lait macules, and growth deficiency. Cells from affected individuals
CC show a high rate of sister chromatid exchange and increased chromosomal
CC breaks. {ECO:0000269|PubMed:27977684}.
CC -!- SIMILARITY: Belongs to the RMI2 family. {ECO:0000305}.
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DR EMBL; AK123764; BAG53958.1; -; mRNA.
DR EMBL; AC009121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85155.1; -; Genomic_DNA.
DR EMBL; BC013040; AAH13040.2; -; mRNA.
DR EMBL; BC022427; AAH22427.1; -; mRNA.
DR EMBL; BC031016; AAH31016.1; -; mRNA.
DR EMBL; BC039361; AAH39361.1; -; mRNA.
DR CCDS; CCDS10548.1; -. [Q96E14-1]
DR RefSeq; NP_689521.1; NM_152308.2. [Q96E14-1]
DR PDB; 3MXN; X-ray; 1.55 A; B=1-147.
DR PDB; 3NBH; X-ray; 2.00 A; B=6-147.
DR PDB; 4DAY; X-ray; 3.30 A; B=1-147.
DR PDBsum; 3MXN; -.
DR PDBsum; 3NBH; -.
DR PDBsum; 4DAY; -.
DR AlphaFoldDB; Q96E14; -.
DR SMR; Q96E14; -.
DR BioGRID; 125466; 28.
DR ComplexPortal; CPX-3301; BTR double Holliday Junction dissolution complex.
DR DIP; DIP-56480N; -.
DR IntAct; Q96E14; 12.
DR MINT; Q96E14; -.
DR STRING; 9606.ENSP00000310356; -.
DR iPTMnet; Q96E14; -.
DR PhosphoSitePlus; Q96E14; -.
DR BioMuta; RMI2; -.
DR DMDM; 74731517; -.
DR EPD; Q96E14; -.
DR jPOST; Q96E14; -.
DR MassIVE; Q96E14; -.
DR MaxQB; Q96E14; -.
DR PaxDb; Q96E14; -.
DR PeptideAtlas; Q96E14; -.
DR PRIDE; Q96E14; -.
DR ProteomicsDB; 76362; -. [Q96E14-1]
DR ProteomicsDB; 76363; -. [Q96E14-2]
DR Antibodypedia; 52376; 40 antibodies from 15 providers.
DR DNASU; 116028; -.
DR Ensembl; ENST00000312499.6; ENSP00000310356.5; ENSG00000175643.10. [Q96E14-1]
DR Ensembl; ENST00000572173.1; ENSP00000461206.1; ENSG00000175643.10. [Q96E14-2]
DR GeneID; 116028; -.
DR KEGG; hsa:116028; -.
DR MANE-Select; ENST00000312499.6; ENSP00000310356.5; NM_152308.3; NP_689521.1.
DR UCSC; uc002daw.2; human. [Q96E14-1]
DR CTD; 116028; -.
DR DisGeNET; 116028; -.
DR GeneCards; RMI2; -.
DR HGNC; HGNC:28349; RMI2.
DR HPA; ENSG00000175643; Tissue enhanced (lymphoid).
DR MalaCards; RMI2; -.
DR MIM; 612426; gene.
DR neXtProt; NX_Q96E14; -.
DR OpenTargets; ENSG00000175643; -.
DR Orphanet; 508512; Intrauterine growth restriction-congenital multiple cafe-au-lait macules-increased sister chromatid exchange syndrome.
DR PharmGKB; PA145149635; -.
DR VEuPathDB; HostDB:ENSG00000175643; -.
DR eggNOG; ENOG502S4AN; Eukaryota.
DR GeneTree; ENSGT00390000001653; -.
DR HOGENOM; CLU_2526905_0_0_1; -.
DR InParanoid; Q96E14; -.
DR OMA; RVSLVWM; -.
DR OrthoDB; 1604165at2759; -.
DR PhylomeDB; Q96E14; -.
DR TreeFam; TF332971; -.
DR PathwayCommons; Q96E14; -.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function.
DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function.
DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2.
DR SignaLink; Q96E14; -.
DR BioGRID-ORCS; 116028; 70 hits in 1086 CRISPR screens.
DR GenomeRNAi; 116028; -.
DR Pharos; Q96E14; Tbio.
DR PRO; PR:Q96E14; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96E14; protein.
DR Bgee; ENSG00000175643; Expressed in ventricular zone and 127 other tissues.
DR ExpressionAtlas; Q96E14; baseline and differential.
DR Genevisible; Q96E14; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0043007; P:maintenance of rDNA; IBA:GO_Central.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0033045; P:regulation of sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0071139; P:resolution of recombination intermediates; IDA:ComplexPortal.
DR DisProt; DP02895; -.
DR Gene3D; 2.40.50.140; -; 1.
DR IDEAL; IID00419; -.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR032245; RMI2.
DR PANTHER; PTHR33962; PTHR33962; 1.
DR Pfam; PF16100; RMI2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA replication;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..147
FT /note="RecQ-mediated genome instability protein 2"
FT /id="PRO_0000297577"
FT DNA_BIND 44..114
FT /note="OB"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..98
FT /note="MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGP
FT LDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVP -> MKQTQVGSL
FT FSLGIRNPEPGPVSGTAVPRQLAWKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027287"
FT MUTAGEN 24
FT /note="K->A: Abolishes interaction with RMI1, TOP3A and
FT BLM."
FT /evidence="ECO:0000269|PubMed:18923083"
FT MUTAGEN 59
FT /note="W->A: According to PubMed:18923083, abolishes
FT interaction with RMI1, TOP3A and BLM. According to
FT PubMed:18923082, does not affects interaction with RMI1 and
FT TOP3A."
FT /evidence="ECO:0000269|PubMed:18923083"
FT MUTAGEN 100
FT /note="K->A: Does not affect interaction with RMI1, TOP3A
FT and BLM."
FT /evidence="ECO:0000269|PubMed:18923083"
FT MUTAGEN 121
FT /note="K->A: According to PubMed:18923083, does not affect
FT interaction with RMI1, TOP3A and BLM. According to
FT PubMed:18923082, affects interaction with BLM and the BMI
FT complex."
FT /evidence="ECO:0000269|PubMed:18923082,
FT ECO:0000269|PubMed:18923083"
FT MUTAGEN 135
FT /note="W->A: Abolishes interaction with RMI1, TOP3A and
FT BLM."
FT /evidence="ECO:0000269|PubMed:18923083"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3NBH"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 56..68
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4DAY"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3MXN"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:3MXN"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3MXN"
SQ SEQUENCE 147 AA; 15865 MW; C385825F9AB4439E CRC64;
MAAAADSFSG GPAGVRLPRS PPLKVLAEQL RRDAEGGPGA WRLSRAAAGR GPLDLAAVWM
QGRVVMADRG EARLRDPSGD FSVRGLERVP RGRPCLVPGK YVMVMGVVQA CSPEPCLQAV
KMTDLSDNPI HESMWELEVE DLHRNIP
