(data stored in ACNUC9435 zone)

SWISSPROT: MTMRD_HUMAN

ID   MTMRD_HUMAN             Reviewed;        1849 AA.
AC   Q86WG5; Q3MJF0; Q68DQ3; Q6P459; Q6PJD1; Q7Z325; Q7Z621; Q86VE2;
AC   Q96FE2; Q9C097;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 143.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN CMT4B2, AND
RP   TISSUE 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
RT   myotubularin family, in Charcot-Marie-Tooth neuropathy type
RT   4B2/11p15.";
RL   Hum. Mol. Genet. 12:349-356(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   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
RT   project: 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.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Ravazzolo R., Brice A., Laporte J., LeGuern E.;
RT   "Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and
RT   Sbf1, in two families with an autosomal recessive demyelinating form
RT   of Charcot-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.,
RA   Okamoto Y., Nakagawa M., Boerkoel C.F., Lupski J.R., Osame M.,
RA   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
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1279, AND IDENTIFICATION
RP   BY 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
RT   promote 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).
CC       Promotes the exchange of GDP to GTP, converting inactive GDP-bound
CC       Rab proteins into their active GTP-bound form (PubMed:20937701,
CC       PubMed:25648148). In response to starvation-induced autophagy,
CC       activates RAB21 which in turn binds to and regulates SNARE protein
CC       VAMP8 endolysosomal transport required for SNARE-mediated
CC       autophagosome-lysosome fusion (PubMed:25648148). Acts as an
CC       adapter for the phosphatase MTMR2 (By similarity). Increases MTMR2
CC       catalytic activity towards phosphatidylinositol 3,5-bisphosphate
CC       and to a lesser extent towards phosphatidylinositol 3-phosphate
CC       (By similarity). {ECO:0000250|UniProtKB:E9PXF8,
CC       ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:25648148}.
CC   -!- SUBUNIT: Homodimer (By similarity). Heterotetramer consisting of
CC       one MTMR2 dimer and one SBF2/MTMR13 dimer (PubMed:15998640).
CC       Interacts with class II PI3-kinase PIK3C2A (By similarity).
CC       Interacts (via DENN domain) with RAB21 (in GDP-bound form) in
CC       response to starvation; the interaction activates RAB21
CC       (PubMed:25648148). Interacts with VAMP8 in response to starvation
CC       (PubMed:25648148). {ECO:0000250|UniProtKB:E9PXF8,
CC       ECO:0000269|PubMed:15998640, ECO:0000269|PubMed:25648148}.
CC   -!- INTERACTION:
CC       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}.
CC       Membrane {ECO:0000269|PubMed:15998640}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:15998640}. Endosome membrane
CC       {ECO:0000250|UniProtKB:E9PXF8}; Peripheral membrane protein
CC       {ECO:0000305}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:E9PXF8}. Note=Associated with membranes
CC       (PubMed:15998640). Localizes to vacuoles in hypo-osmotic
CC       conditions (By similarity). Membrane localization is likely to be
CC       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         Note=No experimental confirmation available.;
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
CC       4-phosphate, phosphatidylinositol 5-phosphate,
CC       phosphatidylinositol 3,5-biphosphate and phosphatidylinositol
CC       3,4,5-trisphosphate. {ECO:0000250|UniProtKB:E9PXF8}.
CC   -!- DOMAIN: The PH domain binds preferentially phosphatidylinositol
CC       3,4,5-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
CC       disorder of the peripheral nervous system, characterized by
CC       progressive weakness and atrophy, initially of the peroneal
CC       muscles and later of the distal muscles of the arms. Charcot-
CC       Marie-Tooth disease is classified in two main groups on the basis
CC       of electrophysiologic properties and histopathology: primary
CC       peripheral demyelinating neuropathies (designated CMT1 when they
CC       are dominantly inherited) and primary peripheral axonal
CC       neuropathies (CMT2). Demyelinating neuropathies are characterized
CC       by severely reduced nerve conduction velocities (less than 38
CC       m/sec), segmental demyelination and remyelination with onion bulb
CC       formations on nerve biopsy, slowly progressive distal muscle
CC       atrophy and weakness, absent deep tendon reflexes, and hollow
CC       feet. By convention autosomal recessive forms of demyelinating
CC       Charcot-Marie-Tooth disease are designated CMT4.
CC       {ECO:0000269|PubMed:12554688, ECO:0000269|PubMed:12687498,
CC       ECO:0000269|PubMed:15304601, ECO:0000269|PubMed:15477569}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the non-receptor class
CC       myotubularin subfamily, lacks the conserved active site cysteine
CC       residue at position 1410 in the dsPTPase catalytic loop,
CC       suggesting that it has no phosphatase activity. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC       URL="http://www.molgen.ua.ac.be/CMTMutations/";
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   SMR; Q86WG5; -.
DR   BioGrid; 123597; 26.
DR   IntAct; Q86WG5; 10.
DR   STRING; 9606.ENSP00000256190; -.
DR   DEPOD; Q86WG5; -.
DR   iPTMnet; Q86WG5; -.
DR   PhosphoSitePlus; Q86WG5; -.
DR   BioMuta; SBF2; -.
DR   DMDM; 74750502; -.
DR   EPD; Q86WG5; -.
DR   jPOST; Q86WG5; -.
DR   MaxQB; Q86WG5; -.
DR   PaxDb; Q86WG5; -.
DR   PeptideAtlas; Q86WG5; -.
DR   PRIDE; Q86WG5; -.
DR   ProteomicsDB; 70158; -.
DR   ProteomicsDB; 70159; -. [Q86WG5-3]
DR   Ensembl; ENST00000256190; ENSP00000256190; ENSG00000133812. [Q86WG5-1]
DR   GeneID; 81846; -.
DR   KEGG; hsa:81846; -.
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; HPA050933; -.
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   eggNOG; KOG1090; Eukaryota.
DR   eggNOG; KOG4471; Eukaryota.
DR   eggNOG; ENOG410XTJ1; LUCA.
DR   GeneTree; ENSGT00940000155385; -.
DR   InParanoid; Q86WG5; -.
DR   KO; K18061; -.
DR   OMA; PNAYVCL; -.
DR   PhylomeDB; Q86WG5; -.
DR   TreeFam; TF318583; -.
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   ChiTaRS; SBF2; human.
DR   GeneWiki; SBF2; -.
DR   GenomeRNAi; 81846; -.
DR   PRO; PR:Q86WG5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000133812; Expressed in 196 organ(s), highest expression level in epithelial cell of pancreas.
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: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:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0042552; P:myelination; NAS:UniProtKB.
DR   GO; GO:0051262; P:protein tetramerization; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   CDD; cd13339; PH-GRAM_MTMR13; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
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;
DR   PRODOM; Q96FE2.
DR   SWISS-2DPAGE; Q96FE2.
KW   Alternative splicing; Autophagy; Cell projection;
KW   Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm; Endosome;
KW   Guanine-nucleotide releasing factor; Membrane; Neurodegeneration;
KW   Neuropathy; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1   1849       Myotubularin-related protein 13.
FT                                /FTId=PRO_0000094945.
FT   DOMAIN        7    172       uDENN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00304}.
FT   DOMAIN      191    324       cDENN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00304}.
FT   DOMAIN      326    427       dDENN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00304}.
FT   DOMAIN      871    957       GRAM. {ECO:0000255}.
FT   DOMAIN     1108   1584       Myotubularin phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00669}.
FT   DOMAIN     1743   1847       PH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00145}.
FT   REGION     1629   1682       Required for homodimerization and
FT                                interaction with MTMR2.
FT                                {ECO:0000250|UniProtKB:E9PXF8,
FT                                ECO:0000269|PubMed:15998640}.
FT   MOD_RES    1127   1127       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1279   1279       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ    1152   1152       S -> R (in isoform 3).
FT                                {ECO:0000303|PubMed:11214970}.
FT                                /FTId=VSP_017157.
FT   VAR_SEQ    1153   1849       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11214970}.
FT                                /FTId=VSP_017158.
FT   VARIANT     303    303       P -> L (in dbSNP:rs16907355).
FT                                /FTId=VAR_051766.
FT   VARIANT     679    679       E -> K (in dbSNP:rs7102464).
FT                                /FTId=VAR_051767.
FT   VARIANT    1216   1216       Q -> E (in dbSNP:rs12574508).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_051768.
FT   CONFLICT   1586   1586       E -> G (in Ref. 4; CAH18167).
FT                                {ECO:0000305}.
FT   CONFLICT   1665   1665       E -> V (in Ref. 4; CAH18167).
FT                                {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
//

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