TPTE2_HUMAN
ID TPTE2_HUMAN Reviewed; 522 AA.
AC Q6XPS3; A1A4X0; A1A4X1; A8MX64; B1AQ16; B4DWZ2; Q5VUH2; Q8WWL4; Q8WWL5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2;
DE EC=3.1.3.67 {ECO:0000269|PubMed:11716755};
DE AltName: Full=Lipid phosphatase TPIP;
DE AltName: Full=TPTE and PTEN homologous inositol lipid phosphatase {ECO:0000303|PubMed:11716755};
GN Name=TPTE2; Synonyms=TPIP {ECO:0000303|PubMed:11716755};
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] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-320, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RC TISSUE=Testis;
RX PubMed=11716755; DOI=10.1042/0264-6021:3600277;
RA Walker S.M., Downes C.P., Leslie N.R.;
RT "TPIP: a novel phosphoinositide 3-phosphatase.";
RL Biochem. J. 360:277-283(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-444, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14659893; DOI=10.1016/j.gene.2003.09.038;
RA Tapparel C., Reymond A., Girardet C., Guillou L., Lyle R., Lamon C.,
RA Hutter P., Antonarakis S.E.;
RT "The TPTE gene family: cellular expression, subcellular localization and
RT alternative splicing.";
RL Gene 323:189-199(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND VARIANT VAL-444.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND VARIANT VAL-444.
RX PubMed=22164291; DOI=10.1371/journal.pone.0028433;
RA Mishra R.R., Chaudhary J.K., Bajaj G.D., Rath P.C.;
RT "A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and
RT mouse tissues, strongly inhibits cell growth in HeLa cells.";
RL PLoS ONE 6:E28433-E28433(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND VARIANT
RP VAL-444.
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).
CC -!- FUNCTION: Acts as a lipid phosphatase, removing the phosphate in the D3
CC position of the inositol ring from phosphatidylinositol 3,4,5-
CC trisphosphate. {ECO:0000269|PubMed:11716755}.
CC -!- FUNCTION: [Isoform 4]: Shows no phosphoinositide phosphatase activity.
CC {ECO:0000269|PubMed:11716755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456; EC=3.1.3.67;
CC Evidence={ECO:0000269|PubMed:11716755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25018;
CC Evidence={ECO:0000305|PubMed:11716755};
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11716755}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14659893}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14659893};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:11716755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=TPIP gamma;
CC IsoId=Q6XPS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6XPS3-2; Sequence=VSP_017324;
CC Name=3; Synonyms=TPIP alpha;
CC IsoId=Q6XPS3-3; Sequence=VSP_017323, VSP_017324;
CC Name=4; Synonyms=TPIP beta;
CC IsoId=Q6XPS3-4; Sequence=VSP_017322, VSP_017325;
CC Name=5;
CC IsoId=Q6XPS3-5; Sequence=VSP_044506;
CC Name=6; Synonyms=TPIP-C2;
CC IsoId=Q6XPS3-6; Sequence=VSP_047569;
CC Name=7;
CC IsoId=Q6XPS3-7; Sequence=VSP_053978;
CC -!- TISSUE SPECIFICITY: Isoform 3 is expressed in testis, brain and stomach
CC while isoform 4 seems to be testis-specific.
CC {ECO:0000269|PubMed:11716755}.
CC -!- MISCELLANEOUS: [Isoform 6]: Expressed in testis, strongly inhibits cell
CC growth in HeLa cells. {ECO:0000305}.
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DR EMBL; AJ421032; CAD13144.1; -; mRNA.
DR EMBL; AJ421033; CAD13145.1; -; mRNA.
DR EMBL; AY219890; AAP45146.1; -; mRNA.
DR EMBL; FJ969729; ACT21090.1; -; mRNA.
DR EMBL; AK301741; BAG63204.1; -; mRNA.
DR EMBL; AL590076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08219.1; -; Genomic_DNA.
DR EMBL; BC128146; AAI28147.1; -; mRNA.
DR EMBL; BC128147; AAI28148.1; -; mRNA.
DR CCDS; CCDS45013.1; -. [Q6XPS3-5]
DR CCDS; CCDS45014.1; -. [Q6XPS3-1]
DR CCDS; CCDS9285.1; -. [Q6XPS3-3]
DR RefSeq; NP_001135440.1; NM_001141968.1. [Q6XPS3-5]
DR RefSeq; NP_001258779.1; NM_001271850.1. [Q6XPS3-6]
DR RefSeq; NP_570141.3; NM_130785.3. [Q6XPS3-3]
DR RefSeq; NP_954863.2; NM_199254.2. [Q6XPS3-1]
DR AlphaFoldDB; Q6XPS3; -.
DR SMR; Q6XPS3; -.
DR BioGRID; 125031; 86.
DR IntAct; Q6XPS3; 52.
DR MINT; Q6XPS3; -.
DR STRING; 9606.ENSP00000383089; -.
DR SwissLipids; SLP:000000884; -. [Q6XPS3-3]
DR DEPOD; TPTE2; -.
DR iPTMnet; Q6XPS3; -.
DR PhosphoSitePlus; Q6XPS3; -.
DR BioMuta; TPTE2; -.
DR DMDM; 215273973; -.
DR jPOST; Q6XPS3; -.
DR MassIVE; Q6XPS3; -.
DR MaxQB; Q6XPS3; -.
DR PaxDb; Q6XPS3; -.
DR PeptideAtlas; Q6XPS3; -.
DR PRIDE; Q6XPS3; -.
DR Antibodypedia; 22226; 63 antibodies from 23 providers.
DR DNASU; 93492; -.
DR Ensembl; ENST00000255310.10; ENSP00000255310.6; ENSG00000132958.17. [Q6XPS3-3]
DR Ensembl; ENST00000382978.5; ENSP00000372438.1; ENSG00000132958.17. [Q6XPS3-2]
DR Ensembl; ENST00000390680.2; ENSP00000375098.2; ENSG00000132958.17. [Q6XPS3-3]
DR Ensembl; ENST00000400103.6; ENSP00000382974.2; ENSG00000132958.17. [Q6XPS3-5]
DR Ensembl; ENST00000400230.6; ENSP00000383089.2; ENSG00000132958.17. [Q6XPS3-1]
DR GeneID; 93492; -.
DR KEGG; hsa:93492; -.
DR UCSC; uc001ume.4; human. [Q6XPS3-1]
DR CTD; 93492; -.
DR DisGeNET; 93492; -.
DR GeneCards; TPTE2; -.
DR HGNC; HGNC:17299; TPTE2.
DR HPA; ENSG00000132958; Tissue enriched (testis).
DR MIM; 606791; gene.
DR neXtProt; NX_Q6XPS3; -.
DR OpenTargets; ENSG00000132958; -.
DR PharmGKB; PA134917664; -.
DR VEuPathDB; HostDB:ENSG00000132958; -.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000154335; -.
DR HOGENOM; CLU_020105_3_0_1; -.
DR InParanoid; Q6XPS3; -.
DR OMA; LLIFVDM; -.
DR OrthoDB; 639380at2759; -.
DR PhylomeDB; Q6XPS3; -.
DR TreeFam; TF354329; -.
DR PathwayCommons; Q6XPS3; -.
DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
DR SignaLink; Q6XPS3; -.
DR BioGRID-ORCS; 93492; 27 hits in 1030 CRISPR screens.
DR ChiTaRS; TPTE2; human.
DR GenomeRNAi; 93492; -.
DR Pharos; Q6XPS3; Tbio.
DR PRO; PR:Q6XPS3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6XPS3; protein.
DR Bgee; ENSG00000132958; Expressed in right testis and 86 other tissues.
DR ExpressionAtlas; Q6XPS3; baseline and differential.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; TAS:Reactome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR CDD; cd14510; PTP_VSP_TPTE; 1.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR045102; PTP_VSP_TPTE.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW Hydrolase; Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..522
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase TPTE2"
FT /id="PRO_0000224187"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 210..386
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 393..522
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..329
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:22164291"
FT /id="VSP_047569"
FT VAR_SEQ 40..170
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11716755"
FT /id="VSP_017322"
FT VAR_SEQ 40..77
FT /note="SMLERLSKFEVEDAENVASYDSKIKKIVHSIVSSFAFG -> R (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11716755"
FT /id="VSP_017323"
FT VAR_SEQ 60..171
FT /note="DSKIKKIVHSIVSSFAFGIFGVFLVLLDVTLLLADLIFTDSKLYIPLEYRSI
FT SLAIGLFFLMDVLLRVFVEGRQQYFSDLFNILDTAIIVIPLLVDVIYIFFDIKLLRNIP
FT R -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044506"
FT VAR_SEQ 132..171
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11716755"
FT /id="VSP_017324"
FT VAR_SEQ 435..522
FT /note="ILHDIETDKILINVYDGPPLYDDVKVQFFSSNLPKYYDNCPFFFWFNTSFIQ
FT NNRLCLPRNELDNPHKQKAWKIYPPEFAVEILFGEK -> REEGSTLRRANWKGEPSRR
FT PVLD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11716755"
FT /id="VSP_017325"
FT VAR_SEQ 466..522
FT /note="NLPKYYDNCPFFFWFNTSFIQNNRLCLPRNELDNPHKQKAWKIYPPEFAVEI
FT LFGEK -> REEGSTLRRANWKGEPSRRPVLD (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053978"
FT VARIANT 367
FT /note="V -> I (in dbSNP:rs2497218)"
FT /id="VAR_047501"
FT VARIANT 444
FT /note="I -> V (in dbSNP:rs2497218)"
FT /evidence="ECO:0000269|PubMed:14659893,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:22164291"
FT /id="VAR_057349"
FT MUTAGEN 320
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11716755"
FT CONFLICT 521
FT /note="E -> K (in Ref. 1; CAD13144 and 2; AAP45146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 61112 MW; 4CC42349355EDA9F CRC64;
MNESPQTNEF KGTTEEAPAK ESPHTSEFKG AALVSPISKS MLERLSKFEV EDAENVASYD
SKIKKIVHSI VSSFAFGIFG VFLVLLDVTL LLADLIFTDS KLYIPLEYRS ISLAIGLFFL
MDVLLRVFVE GRQQYFSDLF NILDTAIIVI PLLVDVIYIF FDIKLLRNIP RWTHLVRLLR
LIILIRIFHL LHQKRQLEKL MRRLVSENKR RYTRDGFDLD LTYVTERIIA MSFPSSGRQS
FYRNPIEEVV RFLDKKHRNH YRVYNLCSER AYDPKHFHNR VSRIMIDDHN VPTLHEMVVF
TKEVNEWMAQ DLENIVAIHC KGGKGRTGTM VCALLIASEI FLTAEESLYY FGERRTNKTH
SNKFQGVETP SQNRYVGYFA QVKHLYNWNL PPRRILFIKR FIIYSIRGDV CDLKVQVVME
KKVVFSSTSL GNCSILHDIE TDKILINVYD GPPLYDDVKV QFFSSNLPKY YDNCPFFFWF
NTSFIQNNRL CLPRNELDNP HKQKAWKIYP PEFAVEILFG EK
