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,
RC   Pancreas, 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};
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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   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.
DR   Genevisible; Q6ZPE2; MM.
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
//