ID MTMR5_MOUSE Reviewed; 1867 AA.
AC Q6ZPE2; B2RXQ1; B2RXX4; B7ZWK2; Q4QQM2; Q8BK68; Q8K2Z0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Myotubularin-related protein 5;
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 5 {ECO:0000305};
DE AltName: Full=SET-binding factor 1;
DE Short=Sbf1;
GN Name=Sbf1; Synonyms=Kiaa3020, Mtmr5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1521-1867.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP STRUCTURE BY NMR OF 1762-1865.
RG RIKEN structural genomics initiative (RSGI);
RT "solution structure of the C-terminal pleckstrin homology domain of Sbf1
RT from mouse.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Acts as an adapter for the phosphatase MTMR2 to regulate
CC MTMR2 catalytic activity and subcellular location. May function as a
CC guanine nucleotide exchange factor (GEF) activating RAB28. Promotes the
CC exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into
CC their active GTP-bound form. Inhibits myoblast differentiation in vitro
CC and induces oncogenic transformation in fibroblasts.
CC {ECO:0000250|UniProtKB:O95248}.
CC -!- SUBUNIT: Heterodimer with lipid phosphatase MTMR2. Interacts with
CC KMT2A/MLL1 (via SET domain). Interacts with SUV39H1.
CC {ECO:0000250|UniProtKB:O95248}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95248}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O95248}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPE2-2; Sequence=VSP_047523;
CC -!- DOMAIN: The C-terminal domain mediates interaction with MTMR2.
CC {ECO:0000250|UniProtKB:O95248}.
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 1422 in the dsPTPase catalytic loop and does not have phosphatase
CC activity (By similarity). The pocket is however sufficiently preserved
CC to bind phosphorylated substrates, and maybe protect them from
CC phosphatases. {ECO:0000250|UniProtKB:O95248, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29156.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98295.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AK129485; BAC98295.1; ALT_INIT; mRNA.
DR EMBL; AC160538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029156; AAH29156.1; ALT_INIT; mRNA.
DR EMBL; BC098209; AAH98209.1; -; mRNA.
DR EMBL; BC157935; AAI57936.1; -; mRNA.
DR EMBL; BC158013; AAI58014.1; -; mRNA.
DR EMBL; BC172094; AAI72094.1; -; mRNA.
DR EMBL; AK076039; BAC36139.1; -; mRNA.
DR CCDS; CCDS37175.2; -. [Q6ZPE2-1]
DR CCDS; CCDS49699.1; -. [Q6ZPE2-2]
DR RefSeq; NP_001074499.2; NM_001081030.2. [Q6ZPE2-1]
DR RefSeq; NP_001164032.1; NM_001170561.1. [Q6ZPE2-2]
DR PDB; 1V5U; NMR; -; A=1762-1865.
DR PDBsum; 1V5U; -.
DR AlphaFoldDB; Q6ZPE2; -.
DR SMR; Q6ZPE2; -.
DR BioGRID; 219065; 13.
DR IntAct; Q6ZPE2; 5.
DR MINT; Q6ZPE2; -.
DR STRING; 10090.ENSMUSP00000118107; -.
DR GlyGen; Q6ZPE2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZPE2; -.
DR PhosphoSitePlus; Q6ZPE2; -.
DR SwissPalm; Q6ZPE2; -.
DR EPD; Q6ZPE2; -.
DR jPOST; Q6ZPE2; -.
DR MaxQB; Q6ZPE2; -.
DR PaxDb; 10090-ENSMUSP00000118107; -.
DR PeptideAtlas; Q6ZPE2; -.
DR ProteomicsDB; 287636; -. [Q6ZPE2-1]
DR ProteomicsDB; 287637; -. [Q6ZPE2-2]
DR Pumba; Q6ZPE2; -.
DR Antibodypedia; 28572; 102 antibodies from 15 providers.
DR DNASU; 77980; -.
DR Ensembl; ENSMUST00000123791.8; ENSMUSP00000120725.2; ENSMUSG00000036529.18. [Q6ZPE2-1]
DR Ensembl; ENSMUST00000144585.9; ENSMUSP00000118107.3; ENSMUSG00000036529.18. [Q6ZPE2-2]
DR GeneID; 77980; -.
DR KEGG; mmu:77980; -.
DR UCSC; uc007xfz.1; mouse. [Q6ZPE2-1]
DR UCSC; uc011zxu.1; mouse. [Q6ZPE2-2]
DR AGR; MGI:1925230; -.
DR CTD; 6305; -.
DR MGI; MGI:1925230; Sbf1.
DR VEuPathDB; HostDB:ENSMUSG00000036529; -.
DR eggNOG; KOG1090; Eukaryota.
DR eggNOG; KOG2080; Eukaryota.
DR GeneTree; ENSGT00940000155263; -.
DR HOGENOM; CLU_002298_1_1_1; -.
DR InParanoid; Q6ZPE2; -.
DR OMA; NCINCIF; -.
DR OrthoDB; 3195274at2759; -.
DR TreeFam; TF318583; -.
DR Reactome; R-MMU-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 77980; 12 hits in 79 CRISPR screens.
DR ChiTaRS; Sbf1; mouse.
DR EvolutionaryTrace; Q6ZPE2; -.
DR PRO; PR:Q6ZPE2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6ZPE2; Protein.
DR Bgee; ENSMUSG00000036529; Expressed in dentate gyrus of hippocampal formation granule cell and 232 other cell types or tissues.
DR ExpressionAtlas; Q6ZPE2; baseline and differential.
DR Genevisible; Q6ZPE2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0001691; F:pseudophosphatase activity; TAS:MGI.
DR GO; GO:0001558; P:regulation of cell growth; TAS:MGI.
DR GO; GO:0007286; P:spermatid development; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd01235; PH_Sbf1_hMTMR5; 1.
DR Gene3D; 3.30.450.200; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; 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; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF43; MYOTUBULARIN-RELATED PROTEIN 5; 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; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm;
KW Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1867
FT /note="Myotubularin-related protein 5"
FT /id="PRO_0000293476"
FT DOMAIN 7..184
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 203..336
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 338..439
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 880..968
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 1120..1596
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT DOMAIN 1761..1865
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 102..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95248"
FT MOD_RES 1137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95248"
FT MOD_RES 1222
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95248"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95248"
FT VAR_SEQ 1275
FT /note="H -> HVPSPRARVTTLSNPLAASASRWTASR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047523"
FT CONFLICT 317
FT /note="C -> R (in Ref. 3; AAI72094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1347
FT /note="E -> D (in Ref. 3; AAI57936)"
FT /evidence="ECO:0000305"
FT CONFLICT 1521
FT /note="R -> W (in Ref. 4; BAC36139)"
FT /evidence="ECO:0000305"
FT STRAND 1762..1770
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1774..1776
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1779..1786
FT /evidence="ECO:0007829|PDB:1V5U"
FT TURN 1787..1790
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1791..1799
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1806..1808
FT /evidence="ECO:0007829|PDB:1V5U"
FT HELIX 1809..1811
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1812..1816
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1826..1828
FT /evidence="ECO:0007829|PDB:1V5U"
FT TURN 1830..1832
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1834..1840
FT /evidence="ECO:0007829|PDB:1V5U"
FT STRAND 1842..1846
FT /evidence="ECO:0007829|PDB:1V5U"
FT HELIX 1850..1861
FT /evidence="ECO:0007829|PDB:1V5U"
SQ SEQUENCE 1867 AA; 208693 MW; 16C7033FAA62CB1A CRC64;
MARLADYFVL VAFGPHPRGS GEGQGQILQR FPEKDWEDNP FPQGIELFCQ PSGWQLCPER
NPPTFFVAVL TDINSERHYC ACLTFWEPVE STQEVVCTDN ATEKEEEADG GGQARLSSTA
PAQPGQLFAP KTLVLVSRLD HAEVFRNSLG LIYAIHVEGL NVSLENVIGN LLTCTVPLAG
GSQRTISLGA GDRQVIQTPL VDSLPVSRCS VALLFRQLGI TNVLSLFCAA LTEHKVLFLS
RSYQRLADAC RGLLALLFPL RYSFTYVPIL PAQLLEVLST PTPFIIGVNA AFQAETQELL
DVIVADLDGG TVTVPECVHI PPLPEPLQSQ THNVLSMVLD PELELADLAF PPPTTSASSL
KMQDKELRAV FLRLFAQLLQ GYRWCLHIVR IHPEPVIRFH KAAFLGQRGL VEDDFLMKVL
EGMAFAGFVS ERGVPYRATD LFDELVAHEV ARMRADESHP HRVLRHVQEL AEQLYKNENP
YPAVAMHKVQ RPGEASHLRR THRPFPRLDE GTIQWIVDQA AAKMQGAPPA VKAERRSTVP
SGPPMTAILE RCSGPHINSA RRLEVVRNCI SYVFEGKMLE AKKLLPAVLR ALKGRAARRC
LAHELHLHVQ QNRAVLDHQQ FDFVVRMMNC CLQDCTSLDE HGIASALLPL VTAFCRKLSP
GVTQFAYSCV QEHVVWSTPQ FWEAMFYGDV QTHIRALYLE PSDGVSPTQE TGEAQSQDDE
RSALDVASEQ RRLWPTLSRE KQQELVQKEE STVFSQAIHY ANRMSYLLLP LDSSKSRLLR
ERAGLGDLES ASNSLVTNSM AGSVAESYDT ESGFEDAETC DVAGAVVRFI NRFVDKVCTE
SGVTSDHLKG LHVMVPDIVQ MHIETLEAVH RESKRLPPIQ KPKLLRPRLL PGEECVLDGL
RVYLLPDGRE EGVGGSGGGP ALLPAEGAVF LTTYRVIFTG MPTDPLVGEQ VVVRSFPVAA
LTKEKRISVQ TPVDQLLQDG LQLRSCTFQL LKMAFDEEVG SDSAELFRKQ LHKLRYPPDI
RATFAFTLGS AHTPGRPPRV TKDKGPSFRT LSRNLMKNAK KTIGRQYVTR KKYNPPGWEH
RGQPPPEDQE DEISVSEELE PSTLTPSSAL KPSDRMTMSS LVERACCRDY QRLGLGTLSS
SLSRAKSEPF RISPVNRMYA ICRSYPGLLI VPQSIQDNAL QRVSRCYRQN RFPVVCWRSG
RSKAVLLRSG GLHGKGVVGL FKAQNTPSPG QAQADSSSLE QEKYLQAVVS SMPRYADSSG
RNTLSSFSSA HMGGHGKWSS VRASGRSSGL GSDVGSRLAG RDLLSTPHTN GAPPDSGFLR
PQRAALYIIG DKAQLKGVRP DPLQQWELVP IEVFEARQVK ASFKKLLKAC VPGCPATEPS
PASFLRSLED SEWLIQIHKL LQISVLVVEL LDSGSSVLVS LEDGWDITTQ VVSLVQLLSD
PFYRTLEGFR LLVEKEWLSF GHRFSHRGAH TLAGQSSGFT PVFLQFLDCV HQVHLQFPME
FEFSQFYLKF LGYHHTSRRF RTFLLDSDYE RIELGLLYEE KGERRGQLAC KSVWEYVDRL
SKRTPMFYNY TYAPEDTEVL RPYSNVSNLK VWDFYTEETL AEGPPYDWEL AQGPPEPPEE
ERPDGGAPQS RRRVVWPCYD SRPRVQPDAI SRLLEELQRL ETELGRPSER WKDTWDRVKA
AQRLESRQDG RGTPSSLLVS AVPHHRRSLG VYLQEGPVGS TLSLSLDSDQ SSGSTTSSSR
QAARRSTSTL YSQFQTAESE NRSYEGILYK KGAFMKPWKA RWFVLDKTKH QLRYYDHRMD
TECKGVIDLA EVEAVAPGTP TIGAPKTVDE KAFFDVKTTR RVYNFCAQDV PSAQQWVDRI
QSCLSDA
//
