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UniProtKB/Swiss-Prot entry P42345


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FRAP_HUMAN
Primary accession number P42345
Secondary accession numbers Q5TER1 Q6LE87 Q96QG3 Q9Y4I3
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 92)
Name and origin of the protein
Protein name FKBP12-rapamycin complex-associated protein
Synonyms FK506-binding protein 12-rapamycin complex-associated protein 1
Rapamycin target protein
RAPT1
Mammalian target of rapamycin
mTOR
Gene name
Name: FRAP1
Synonyms: FRAP, FRAP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1038/369756a0; PubMed=8008069 [NCBI, ExPASy, EBI, Israel, Japan]
Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T., Lane W.S., Schreiber S.L.;
"A mammalian protein targeted by G1-arresting rapamycin-receptor complex.";
Nature 369:756-758(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/geno.1997.5186; PubMed=9653645 [NCBI, ExPASy, EBI, Israel, Japan]
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
"Molecular cloning and expression analysis of five novel genes in chromosome 1p36.";
Genomics 50:187-198(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1362-2549.
DOI=10.1038/sj.gene.6363745; PubMed=11426320 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.;
"The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3.";
Genes Immun. 2:119-127(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, AND TISSUE SPECIFICITY.
TISSUE=B-cell;
DOI=10.1073/pnas.91.26.12574; PubMed=7809080 [NCBI, ExPASy, EBI, Israel, Japan]
Chiu M.I., Katz H., Berlin V.;
"RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.";
Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994).
[7]
INTERACTION WITH UBQLN1.
DOI=10.1016/S0167-4889(01)00164-1; PubMed=11853878 [NCBI, ExPASy, EBI, Israel, Japan]
Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.;
"Characterization of ubiquilin 1, an mTOR-interacting protein.";
Biochim. Biophys. Acta 1542:41-56(2002).
[8]
FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, AND INTERACTION WITH RICTOR.
DOI=10.1016/j.cub.2004.06.054; PubMed=15268862 [NCBI, ExPASy, EBI, Israel, Japan]
Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.;
"Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton.";
Curr. Biol. 14:1296-1302(2004).
[9]
FUNCTION.
DOI=10.1126/science.1106148; PubMed=15718470 [NCBI, ExPASy, EBI, Israel, Japan]
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex.";
Science 307:1098-1101(2005).
[10]
IDENTIFICATION IN TORC2 COMPLEX, AND INTERACTION WITH PRR5.
DOI=10.1074/jbc.M704343200; PubMed=17599906 [NCBI, ExPASy, EBI, Israel, Japan]
Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.;
"PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling.";
J. Biol. Chem. 282:25604-25612(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1162, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND SER-1261, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112.
DOI=10.1126/science.273.5272.239; PubMed=8662507 [NCBI, ExPASy, EBI, Israel, Japan]
Choi J., Chen J., Schreiber S.L., Clardy J.;
"Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP.";
Science 273:239-242(1996).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112.
DOI=10.1107/S0907444998014747; PubMed=10089303 [NCBI, ExPASy, EBI, Israel, Japan]
Liang J., Choi J., Clardy J.;
"Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution.";
Acta Crystallogr. D 55:736-744(1999).
[17]
VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134; PHE-1178; VAL-2011; TYR-2215 AND LEU-2476.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L34075; AAA58486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U88966; AAC39933.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109811; CAI22105.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049653; CAI22105.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391561; CAI22105.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391561; CAI17228.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049653; CAI17228.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109811; CAI17228.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049653; CAI22145.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109811; CAI22145.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391561; CAI22145.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117166; AAI17167.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ300188; CAC15570.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L35478; AAC41713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00031410; -.
PIR S45340; S45340.
RefSeq NP_004949.1; -.
UniGene Hs.338207
3D structure databases
PDB
1AUE; X-ray; 2.33 A; A/B=2015-2114.[ExPASy / RCSB / EBI]
1FAP; X-ray; 2.70 A; B=2018-2112.[ExPASy / RCSB / EBI]
1NSG; X-ray; 2.20 A; B=2019-2112.[ExPASy / RCSB / EBI]
2FAP; X-ray; 2.20 A; B=2019-2112.[ExPASy / RCSB / EBI]
2GAQ; NMR; -; A=2015-2114.[ExPASy / RCSB / EBI]
2NPU; NMR; -; A=2015-2114.[ExPASy / RCSB / EBI]
3FAP; X-ray; 1.85 A; B=2019-2112.[ExPASy / RCSB / EBI]
4FAP; X-ray; 2.80 A; B=2019-2112.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AUE; -.
1FAP; -.
1NSG; -.
2FAP; -.
2GAQ; -.
2NPU; -.
3FAP; -.
4FAP; -.
ModBase P42345.
Protein-protein interaction databases
DIP DIP:790N; -.
IntAct P42345; 24.
PTM databases
PhosphoSite P42345; -.
Enzyme and pathway databases
Pathway_Interaction_DB pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
endothelinpathway; Endothelins.
ifngpathway; IFN-gamma pathway.
il12_2pathway; IL12-mediated signaling events.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il4_2pathway; IL4-mediated signaling events.
mtor_4pathway; mTOR signaling pathway.
telomerasepathway; Regulation of Telomerase.
Reactome REACT_11061; Signalling by NGF.
REACT_498; Signaling by Insulin receptor.
Organism-specific databases
GeneCards GC01M011100; -.
H-InvDB HIX0021581; -.
HGNC HGNC:3942; FRAP1.
GenAtlas FRAP1.
HPA CAB005057; -.
MIM 601231; gene. [NCBI / EBI]
PharmGKB PA28360; -.
Gene expression databases
ArrayExpress P42345; -.
Bgee P42345; -.
CleanEx HS_FRAP1; -.
GermOnline ENSG00000198793; Homo sapiens.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from direct assay from UniProtKB).
GO:0005942; Cellular component: phosphoinositide 3-kinase complex (non-traceable author statement from UniProtKB).
GO:0031931; Cellular component: TORC1 complex (inferred from direct assay from MGI).
GO:0031932; Cellular component: TORC2 complex (inferred from direct assay from MGI).
GO:0051219; Molecular function: phosphoprotein binding (inferred from physical interaction from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from experiment from Reactome).
GO:0016049; Biological process: cell growth (traceable author statement from UniProtKB).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from direct assay from MGI).
GO:0030163; Biological process: protein catabolic process (traceable author statement from UniProtKB).
GO:0007584; Biological process: response to nutrient (non-traceable author statement from UniProtKB).
GO:0007165; Biological process: signal transduction (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR003152; FATC.
IPR009076; FKBP_rapamycin-assoc_FKBP12-bd.
IPR000403; PI3/4_kinase_cat.
IPR018936; PI3/4_kinase_CS.
IPR003151; PIK-rel_kinase_FAT.
IPR014009; PIK_FAT.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 2.
G3DSA:1.20.120.150; FRAP_FKBP12_bd; 1.
G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
Pfam PF02259; FAT; 1.
PF02260; FATC; 1.
PF00454; PI3_PI4_kinase; 1.
PF08771; Rapamycin_bind; 1.
Pfam graphical view of domain structure.
SMART SM00146; PI3Kc; 1.
SMART graphical view of domain structure.
PROSITE PS51189; FAT; 1.
PS51190; FATC; 1.
PS50077; HEAT_REPEAT; FALSE_NEG.
PS00915; PI3_4_KINASE_1; 1.
PS00916; PI3_4_KINASE_2; 1.
PS50290; PI3_4_KINASE_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P42345; -.
Genome annotation databases
Ensembl ENSG00000198793; Homo sapiens. [Contig view]
GeneID 2475; -.
KEGG hsa:2475; -.
Phylogenomic databases
HOVERGEN P42345; -.
OMA P42345; VFMHDNS.
Other
NextBio 9805; -.
SOURCE FRAP1; Homo sapiens.
ProtoNet P42345.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Kinase; Phosphoprotein; Polymorphism; Repeat; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2549  2549     FKBP12-rapamycin complex-associated protein. PRO_0000088808
REPEAT   16     53  38     HEAT 1. 
REPEAT   650    688  39     HEAT 2. 
REPEAT   859    897  39     HEAT 3. 
REPEAT   988   1025  38     HEAT 4. 
REPEAT   1069   1106  38     HEAT 5. 
REPEAT   1109   1148  40     HEAT 6. 
REPEAT   1150   1186  37     HEAT 7. 
DOMAIN   1382   1982  601     FAT. 
DOMAIN   2182   2516  335     PI3K/PI4K. 
DOMAIN   2517   2549  33     FATC. 
MOD_RES   567    567        Phosphoserine. 
MOD_RES   1162   1162        Phosphothreonine. 
MOD_RES   1261   1261        Phosphoserine. 
MOD_RES   2478   2478        Phosphoserine. 
MOD_RES   2481   2481        Phosphoserine. 
VARIANT   8      8  1     A -> S (in a lung large cell carcinoma sample; somatic mutation). VAR_041537 
VARIANT   135    135  1     M -> T (in a metastatic melanoma sample; somatic mutation). VAR_041538 
VARIANT   1083   1083  1     M -> V. VAR_041539 
VARIANT   1134   1134  1     A -> V. VAR_041540 
VARIANT   1178   1178  1     S -> F. VAR_041541 
VARIANT   2011   2011  1     M -> V (in an ovarian mucinous carcinoma sample; somatic mutation). VAR_041542 
VARIANT   2215   2215  1     S -> Y (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041543 
VARIANT   2476   2476  1     P -> L (in a glioblastoma multiforme sample; somatic mutation). VAR_041544 
CONFLICT   353    353        K -> N (in Ref. 2; AAC39933). 
CONFLICT   359    359        S -> N (in Ref. 2; AAC39933). 
CONFLICT   364    364        D -> N (in Ref. 2; AAC39933). 
CONFLICT   390    390        M -> L (in Ref. 2; AAC39933). 
CONFLICT   430    430        R -> L (in Ref. 2; AAC39933). 
CONFLICT   455    457        VLD -> GVE (in Ref. 2; AAC39933). 
CONFLICT   461    461        A -> G (in Ref. 2; AAC39933). 
CONFLICT   482    484        VFT -> FFN (in Ref. 2; AAC39933). 
CONFLICT   489    489        L -> V (in Ref. 2; AAC39933). 
CONFLICT   513    513        L -> I (in Ref. 2; AAC39933). 
CONFLICT   539    539        L -> V (in Ref. 2; AAC39933). 
CONFLICT   553    553        R -> C (in Ref. 2; AAC39933). 
CONFLICT   1075   1075        I -> S (in Ref. 2; AAC39933). 
HELIX   2023   2039  17      
HELIX   2044   2059  16      
HELIX   2065   2091  27      
HELIX   2095   2110  16      
Sequence information
Length: 2549 AA [This is the length of the unprocessed precursor] Molecular weight: 288892 Da [This is the MW of the unprocessed precursor] CRC64: 7D9AD6E784882AB4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 

        70         80         90        100        110        120 
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP 

       130        140        150        160        170        180 
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP 

       190        200        210        220        230        240 
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE 

       250        260        270        280        290        300 
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 

       310        320        330        340        350        360 
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS PAKSTLVESR 

       370        380        390        400        410        420 
CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 

       430        440        450        460        470        480 
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA 

       490        500        510        520        530        540 
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 

       550        560        570        580        590        600 
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT 

       610        620        630        640        650        660 
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL 

       670        680        690        700        710        720 
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS 

       730        740        750        760        770        780 
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI 

       790        800        810        820        830        840 
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA 

       850        860        870        880        890        900 
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 

       910        920        930        940        950        960 
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR 

       970        980        990       1000       1010       1020 
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV 

      1030       1040       1050       1060       1070       1080 
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR 

      1090       1100       1110       1120       1130       1140 
VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD 

      1150       1160       1170       1180       1190       1200 
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 

      1210       1220       1230       1240       1250       1260 
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV ETGPMKKLHV 

      1270       1280       1290       1300       1310       1320 
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA 

      1330       1340       1350       1360       1370       1380 
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI 

      1390       1400       1410       1420       1430       1440 
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF 

      1450       1460       1470       1480       1490       1500 
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 

      1510       1520       1530       1540       1550       1560 
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA 

      1570       1580       1590       1600       1610       1620 
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW 

      1630       1640       1650       1660       1670       1680 
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD 

      1690       1700       1710       1720       1730       1740 
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK 

      1750       1760       1770       1780       1790       1800 
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 

      1810       1820       1830       1840       1850       1860 
VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE SEAESTENSP 

      1870       1880       1890       1900       1910       1920 
TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN 

      1930       1940       1950       1960       1970       1980 
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS 

      1990       2000       2010       2020       2030       2040 
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG 

      2050       2060       2070       2080       2090       2100 
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 

      2110       2120       2130       2140       2150       2160 
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL 

      2170       2180       2190       2200       2210       2220 
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL 

      2230       2240       2250       2260       2270       2280 
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL 

      2290       2300       2310       2320       2330       2340 
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH 

      2350       2360       2370       2380       2390       2400 
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC 

      2410       2420       2430       2440       2450       2460 
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG 

      2470       2480       2490       2500       2510       2520 
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 

      2530       2540 
VPTQVELLIK QATSHENLCQ CYIGWCPFW 

P42345 in FASTA format

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