MTMRD_HUMAN
ID MTMRD_HUMAN Reviewed; 1849 AA.
AC Q86WG5; Q3MJF0; Q68DQ3; Q6P459; Q6PJD1; Q7Z325; Q7Z621; Q86VE2; Q96FE2;
AC Q9C097;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myotubularin-related protein 13 {ECO:0000305};
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 13 {ECO:0000305};
DE AltName: Full=SET-binding factor 2 {ECO:0000303|PubMed:12554688};
GN Name=SBF2; Synonyms=CMT4B2, KIAA1766, MTMR13;
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] (ISOFORM 1), INVOLVEMENT IN CMT4B2, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Sciatic nerve;
RX PubMed=12554688; DOI=10.1093/hmg/ddg030;
RA Senderek J., Bergmann C., Weber S., Ketelsen U.-P., Schorle H.,
RA Rudnik-Schoeneborn S., Buettner R., Buchheim E., Zerres K.;
RT "Mutation of the SBF2 gene, encoding a novel member of the myotubularin
RT family, in Charcot-Marie-Tooth neuropathy type 4B2/11p15.";
RL Hum. Mol. Genet. 12:349-356(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-1216.
RC TISSUE=Brain, Cervix, Duodenum, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-1152 (ISOFORM 3).
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1849 (ISOFORM 1).
RC TISSUE=Fetal brain, and Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP INVOLVEMENT IN CMT4B2.
RX PubMed=12687498; DOI=10.1086/375034;
RA Azzedine H., Bolino A., Taieb T., Birouk N., Di Duca M., Bouhouche A.,
RA Benamou S., Mrabet A., Hammadouche T., Chkili T., Gouider R., Ravazzolo R.,
RA Brice A., Laporte J., LeGuern E.;
RT "Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and Sbf1,
RT in two families with an autosomal recessive demyelinating form of Charcot-
RT Marie-Tooth disease associated with early-onset glaucoma.";
RL Am. J. Hum. Genet. 72:1141-1153(2003).
RN [6]
RP INVOLVEMENT IN CMT4B2.
RX PubMed=15304601; DOI=10.1212/01.wnl.0000133211.40288.9a;
RA Hirano R., Takashima H., Umehara F., Arimura H., Michizono K., Okamoto Y.,
RA Nakagawa M., Boerkoel C.F., Lupski J.R., Osame M., Arimura K.;
RT "SET binding factor 2 (SBF2) mutation causes CMT4B with juvenile onset
RT glaucoma.";
RL Neurology 63:577-580(2004).
RN [7]
RP INVOLVEMENT IN CMT4B2.
RX PubMed=15477569; DOI=10.1212/01.wnl.0000140617.02312.80;
RA Conforti F.L., Muglia M., Mazzei R., Patitucci A., Valentino P.,
RA Magariello A., Sprovieri T., Bono F., Bergmann C., Gabriele A.L.,
RA Peluso G., Nistico R., Senderek J., Quattrone A.;
RT "A new SBF2 mutation in a family with recessive demyelinating Charcot-
RT Marie-Tooth (CMT4B2).";
RL Neurology 63:1327-1328(2004).
RN [8]
RP INTERACTION WITH MTMR2, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15998640; DOI=10.1074/jbc.m505159200;
RA Robinson F.L., Dixon J.E.;
RT "The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a
RT membrane-associated pseudophosphatase also mutated in type 4B Charcot-
RT Marie-Tooth disease.";
RL J. Biol. Chem. 280:31699-31707(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
RX PubMed=20937701; DOI=10.1083/jcb.201008051;
RA Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.;
RT "Family-wide characterization of the DENN domain Rab GDP-GTP exchange
RT factors.";
RL J. Cell Biol. 191:367-381(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1127, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [13]
RP FUNCTION, AND INTERACTION WITH RAB21 AND VAMP8.
RX PubMed=25648148; DOI=10.15252/embr.201439464;
RA Jean S., Cox S., Nassari S., Kiger A.A.;
RT "Starvation-induced MTMR13 and RAB21 activity regulates VAMP8 to promote
RT autophagosome-lysosome fusion.";
RL EMBO Rep. 16:297-311(2015).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which activates
CC RAB21 and possibly RAB28 (PubMed:20937701, PubMed:25648148). Promotes
CC the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins
CC into their active GTP-bound form (PubMed:20937701, PubMed:25648148). In
CC response to starvation-induced autophagy, activates RAB21 which in turn
CC binds to and regulates SNARE protein VAMP8 endolysosomal transport
CC required for SNARE-mediated autophagosome-lysosome fusion
CC (PubMed:25648148). Acts as an adapter for the phosphatase MTMR2 (By
CC similarity). Increases MTMR2 catalytic activity towards
CC phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards
CC phosphatidylinositol 3-phosphate (By similarity).
CC {ECO:0000250|UniProtKB:E9PXF8, ECO:0000269|PubMed:20937701,
CC ECO:0000269|PubMed:25648148}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterotetramer consisting of one
CC MTMR2 dimer and one SBF2/MTMR13 dimer (PubMed:15998640). Interacts with
CC class II PI3-kinase PIK3C2A (By similarity). Interacts (via DENN
CC domain) with RAB21 (in GDP-bound form) in response to starvation; the
CC interaction activates RAB21 (PubMed:25648148). Interacts with VAMP8 in
CC response to starvation (PubMed:25648148).
CC {ECO:0000250|UniProtKB:E9PXF8, ECO:0000269|PubMed:15998640,
CC ECO:0000269|PubMed:25648148}.
CC -!- INTERACTION:
CC Q86WG5; Q13643: FHL3; NbExp=3; IntAct=EBI-2683289, EBI-741101;
CC Q86WG5; Q93062: RBPMS; NbExp=3; IntAct=EBI-2683289, EBI-740322;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15998640}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9PXF8}. Membrane
CC {ECO:0000269|PubMed:15998640}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15998640}. Endosome membrane
CC {ECO:0000250|UniProtKB:E9PXF8}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:E9PXF8}.
CC Note=Associated with membranes (PubMed:15998640). Localizes to vacuoles
CC in hypo-osmotic conditions (By similarity). Membrane localization is
CC likely to be mediated via its interaction with MTMR2 (By similarity).
CC {ECO:0000250|UniProtKB:E9PXF8, ECO:0000269|PubMed:15998640}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86WG5-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q86WG5-3; Sequence=VSP_017157, VSP_017158;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in spinal cord.
CC {ECO:0000269|PubMed:12554688}.
CC -!- DOMAIN: The C-terminal domain mediates homodimerization (By
CC similarity). By mediating SBF2/MTMR13 homodimerization, indirectly
CC involved in SBF2/MTMR13 and MTMR2 heterotetramerization (By
CC similarity). {ECO:0000250|UniProtKB:E9PXF8}.
CC -!- DOMAIN: The GRAM domain mediates binding to phosphatidylinositol 4-
CC phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-
CC biphosphate and phosphatidylinositol 3,4,5-trisphosphate.
CC {ECO:0000250|UniProtKB:E9PXF8}.
CC -!- DOMAIN: The PH domain binds preferentially phosphatidylinositol 3,4,5-
CC trisphosphate (By similarity). Appears to be dispensable for
CC localization to membranes (By similarity).
CC {ECO:0000250|UniProtKB:E9PXF8}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 4B2 (CMT4B2) [MIM:604563]: A
CC recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and 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). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet. By
CC convention autosomal recessive forms of demyelinating Charcot-Marie-
CC Tooth disease are designated CMT4. {ECO:0000269|PubMed:12554688,
CC ECO:0000269|PubMed:12687498, ECO:0000269|PubMed:15304601,
CC ECO:0000269|PubMed:15477569}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 1410 in the dsPTPase catalytic loop, suggesting that it has no
CC phosphatase activity. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
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DR EMBL; AY234241; AAO62733.1; -; mRNA.
DR EMBL; BC011143; AAH11143.1; -; mRNA.
DR EMBL; BC043389; AAH43389.1; -; mRNA.
DR EMBL; BC053867; AAH53867.1; -; mRNA.
DR EMBL; BC063656; AAH63656.1; -; mRNA.
DR EMBL; BC101466; AAI01467.1; -; mRNA.
DR EMBL; AB051553; BAB21857.1; -; mRNA.
DR EMBL; BX538184; CAD98056.1; -; mRNA.
DR EMBL; CR749312; CAH18167.1; -; mRNA.
DR CCDS; CCDS31427.1; -. [Q86WG5-1]
DR RefSeq; NP_112224.1; NM_030962.3. [Q86WG5-1]
DR AlphaFoldDB; Q86WG5; -.
DR SMR; Q86WG5; -.
DR BioGRID; 123597; 49.
DR IntAct; Q86WG5; 23.
DR MINT; Q86WG5; -.
DR STRING; 9606.ENSP00000256190; -.
DR DEPOD; SBF2; -.
DR iPTMnet; Q86WG5; -.
DR PhosphoSitePlus; Q86WG5; -.
DR BioMuta; SBF2; -.
DR DMDM; 74750502; -.
DR EPD; Q86WG5; -.
DR jPOST; Q86WG5; -.
DR MassIVE; Q86WG5; -.
DR MaxQB; Q86WG5; -.
DR PaxDb; Q86WG5; -.
DR PeptideAtlas; Q86WG5; -.
DR PRIDE; Q86WG5; -.
DR ProteomicsDB; 70158; -. [Q86WG5-1]
DR ProteomicsDB; 70159; -. [Q86WG5-3]
DR Antibodypedia; 24321; 42 antibodies from 11 providers.
DR DNASU; 81846; -.
DR Ensembl; ENST00000256190.13; ENSP00000256190.8; ENSG00000133812.18. [Q86WG5-1]
DR Ensembl; ENST00000533770.6; ENSP00000509247.1; ENSG00000133812.18. [Q86WG5-3]
DR GeneID; 81846; -.
DR KEGG; hsa:81846; -.
DR MANE-Select; ENST00000256190.13; ENSP00000256190.8; NM_030962.4; NP_112224.1.
DR UCSC; uc001mib.2; human. [Q86WG5-1]
DR CTD; 81846; -.
DR DisGeNET; 81846; -.
DR GeneCards; SBF2; -.
DR GeneReviews; SBF2; -.
DR HGNC; HGNC:2135; SBF2.
DR HPA; ENSG00000133812; Low tissue specificity.
DR MalaCards; SBF2; -.
DR MIM; 604563; phenotype.
DR MIM; 607697; gene.
DR neXtProt; NX_Q86WG5; -.
DR OpenTargets; ENSG00000133812; -.
DR Orphanet; 99956; Charcot-Marie-Tooth disease type 4B2.
DR PharmGKB; PA26649; -.
DR VEuPathDB; HostDB:ENSG00000133812; -.
DR eggNOG; KOG1090; Eukaryota.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000155385; -.
DR HOGENOM; CLU_002298_1_1_1; -.
DR InParanoid; Q86WG5; -.
DR PhylomeDB; Q86WG5; -.
DR TreeFam; TF318583; -.
DR PathwayCommons; Q86WG5; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q86WG5; -.
DR BioGRID-ORCS; 81846; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; SBF2; human.
DR GeneWiki; SBF2; -.
DR GenomeRNAi; 81846; -.
DR Pharos; Q86WG5; Tbio.
DR PRO; PR:Q86WG5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86WG5; protein.
DR Bgee; ENSG00000133812; Expressed in epithelial cell of pancreas and 186 other tissues.
DR ExpressionAtlas; Q86WG5; baseline and differential.
DR Genevisible; Q86WG5; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042552; P:myelination; NAS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13339; PH-GRAM_MTMR13; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR030567; MTMR13.
DR InterPro; IPR037823; MTMR13_PH-GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF4; PTHR10807:SF4; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF12335; SBF2; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell projection;
KW Charcot-Marie-Tooth disease; Cytoplasm; Endosome;
KW Guanine-nucleotide releasing factor; Membrane; Neurodegeneration;
KW Neuropathy; Phosphoprotein; Reference proteome.
FT CHAIN 1..1849
FT /note="Myotubularin-related protein 13"
FT /id="PRO_0000094945"
FT DOMAIN 7..172
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 191..324
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 326..427
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 871..957
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 1108..1584
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT DOMAIN 1743..1847
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1629..1682
FT /note="Required for homodimerization and interaction with
FT MTMR2"
FT /evidence="ECO:0000250|UniProtKB:E9PXF8,
FT ECO:0000269|PubMed:15998640"
FT REGION 1674..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1152
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11214970"
FT /id="VSP_017157"
FT VAR_SEQ 1153..1849
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11214970"
FT /id="VSP_017158"
FT VARIANT 303
FT /note="P -> L (in dbSNP:rs16907355)"
FT /id="VAR_051766"
FT VARIANT 679
FT /note="E -> K (in dbSNP:rs7102464)"
FT /id="VAR_051767"
FT VARIANT 1216
FT /note="Q -> E (in dbSNP:rs12574508)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051768"
FT CONFLICT 1586
FT /note="E -> G (in Ref. 4; CAH18167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1665
FT /note="E -> V (in Ref. 4; CAH18167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1849 AA; 208464 MW; 9EDBA3E3AC05DD3E CRC64;
MARLADYFIV VGYDHEKPGS GEGLGKIIQR FPQKDWDDTP FPQGIELFCQ PGGWQLSRER
KQPTFFVVVL TDIDSDRHYC SCLTFYEAEI NLQGTKKEEI EGEAKVSGLI QPAEVFAPKS
LVLVSRLYYP EIFRACLGLI YTVYVDSLNV SLESLIANLC ACLVPAAGGS QKLFSLGAGD
RQLIQTPLHD SLPITGTSVA LLFQQLGIQN VLSLFCAVLT ENKVLFHSAS FQRLSDACRA
LESLMFPLKY SYPYIPILPA QLLEVLSSPT PFIIGVHSVF KTDVHELLDV IIADLDGGTI
KIPECIHLSS LPEPLLHQTQ SALSLILHPD LEVADHAFPP PRTALSHSKM LDKEVRAVFL
RLFAQLFQGY RSCLQLIRIH AEPVIHFHKT AFLGQRGLVE NDFLTKVLSG MAFAGFVSER
GPPYRSCDLF DELVAFEVER IKVEENNPVK MIKHVRELAE QLFKNENPNP HMAFQKVPRP
TEGSHLRVHI LPFPEINEAR VQELIQENVA KNQNAPPATR IEKKCVVPAG PPVVSIMDKV
TTVFNSAQRL EVVRNCISFI FENKILETEK TLPAALRALK GKAARQCLTD ELGLHVQQNR
AILDHQQFDY IIRMMNCTLQ DCSSLEEYNI AAALLPLTSA FYRKLAPGVS QFAYTCVQDH
PIWTNQQFWE TTFYNAVQEQ VRSLYLSAKE DNHAPHLKQK DKLPDDHYQE KTAMDLAAEQ
LRLWPTLSKS TQQELVQHEE STVFSQAIHF ANLMVNLLVP LDTSKNKLLR TSAPGDWESG
SNSIVTNSIA GSVAESYDTE SGFEDSENTD IANSVVRFIT RFIDKVCTES GVTQDHIKSL
HCMIPGIVAM HIETLEAVHR ESRRLPPIQK PKILRPALLP GEEIVCEGLR VLLDPDGREE
ATGGLLGGPQ LLPAEGALFL TTYRILFRGT PHDQLVGEQT VVRSFPIASI TKEKKITMQN
QLQQNMQEGL QITSASFQLI KVAFDEEVSP EVVEIFKKQL MKFRYPQSIF STFAFAAGQT
TPQIILPKQK EKNTSFRTFS KTIVKGAKRA GKMTIGRQYL LKKKTGTIVE ERVNRPGWNE
DDDVSVSDES ELPTSTTLKA SEKSTMEQLV EKACFRDYQR LGLGTISGSS SRSRPEYFRI
TASNRMYSLC RSYPGLLVVP QAVQDSSLPR VARCYRHNRL PVVCWKNSRS GTLLLRSGGF
HGKGVVGLFK SQNSPQAAPT SSLESSSSIE QEKYLQALLN AVSVHQKLRG NSTLTVRPAF
ALSPGVWASL RSSTRLISSP TSFIDVGARL AGKDHSASFS NSSYLQNQLL KRQAALYIFG
EKSQLRNFKV EFALNCEFVP VEFHEIRQVK ASFKKLMRAC IPSTIPTDSE VTFLKALGDS
EWFPQLHRIM QLAVVVSEVL ENGSSVLVCL EEGWDITAQV TSLVQLLSDP FYRTLEGFQM
LVEKEWLSFG HKFSQRSSLT LNCQGSGFAP VFLQFLDCVH QVHNQYPTEF EFNLYYLKFL
AFHYVSNRFK TFLLDSDYER LEHGTLFDDK GEKHAKKGVC IWECIDRMHK RSPIFFNYLY
SPLEIEALKP NVNVSSLKKW DYYIEETLST GPSYDWMMLT PKHFPSEDSD LAGEAGPRSQ
RRTVWPCYDD VSCTQPDALT SLFSEIEKLE HKLNQAPEKW QQLWERVTVD LKEEPRTDRS
QRHLSRSPGI VSTNLPSYQK RSLLHLPDSS MGEEQNSSIS PSNGVERRAA TLYSQYTSKN
DENRSFEGTL YKRGALLKGW KPRWFVLDVT KHQLRYYDSG EDTSCKGHID LAEVEMVIPA
GPSMGAPKHT SDKAFFDLKT SKRVYNFCAQ DGQSAQQWMD KIQSCISDA
