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 02-SEP-2026, entry version 172. 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}. 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; 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_001141968.2. [Q6XPS3-5] DR RefSeq; NP_001258779.1; NM_001271850.2. [Q6XPS3-6] DR RefSeq; NP_001382907.1; NM_001395978.1. [Q6XPS3-1] DR RefSeq; NP_570141.3; NM_130785.4. [Q6XPS3-3] DR RefSeq; NP_954863.2; NM_199254.3. [Q6XPS3-1] DR AlphaFoldDB; Q6XPS3; -. DR SMR; Q6XPS3; -. DR BioGRID; 125031; 89. DR FunCoup; Q6XPS3; 57. DR IntAct; Q6XPS3; 59. DR MINT; Q6XPS3; -. DR NDEx; IQUERY-CP-TPTE2; 1 NDEx IQuery Curated Pathway. 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 PaxDb; 9606-ENSP00000383089; -. DR PeptideAtlas; Q6XPS3; -. DR ProteomicsDB; 2297; -. DR ProteomicsDB; 67806; -. [Q6XPS3-1] DR ProteomicsDB; 67807; -. [Q6XPS3-2] DR ProteomicsDB; 67808; -. [Q6XPS3-3] DR ProteomicsDB; 67809; -. [Q6XPS3-4] DR Antibodypedia; 22226; 60 antibodies from 23 providers. DR DNASU; 93492; -. DR Ensembl; ENST00000382978.5; ENSP00000372438.1; ENSG00000132958.19. [Q6XPS3-2] DR Ensembl; ENST00000390680.2; ENSP00000375098.2; ENSG00000132958.19. [Q6XPS3-3] DR Ensembl; ENST00000400103.7; ENSP00000382974.2; ENSG00000132958.19. [Q6XPS3-5] DR Ensembl; ENST00000696858.2; ENSP00000512931.1; ENSG00000132958.19. [Q6XPS3-1] DR Ensembl; ENST00000696988.1; ENSP00000513024.1; ENSG00000132958.19. [Q6XPS3-1] DR Ensembl; ENST00000697147.1; ENSP00000513136.1; ENSG00000132958.19. [Q6XPS3-1] DR GeneID; 93492; -. DR KEGG; hsa:93492; -. DR MANE-Select; ENST00000697147.1; ENSP00000513136.1; NM_001395978.1; NP_001382907.1. DR UCSC; uc001ume.4; human. [Q6XPS3-1] DR AGR; HGNC:17299; -. DR ClinPGx; PA134917664; -. 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 OpenTargets; ENSG00000132958; -. DR VEuPathDB; HostDB:ENSG00000132958; -. DR eggNOG; KOG2283; Eukaryota. DR GeneTree; ENSGT00940000154335; -. DR HOGENOM; CLU_020105_3_0_1; -. DR InParanoid; Q6XPS3; -. DR OMA; ISPCVMS; -. DR OrthoDB; 9527935at2759; -. DR PAN-GO; Q6XPS3; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q6XPS3; -. DR PathwayCommons; Q6XPS3; -. DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane. DR SignaLink; Q6XPS3; -. DR Agora; ENSG00000132958; -. DR BioGRID-ORCS; 93492; 27 hits in 1109 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. 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 male germ line stem cell (sensu Vertebrata) in testis and 88 other cell types or tissues. DR ExpressionAtlas; Q6XPS3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB. DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro. DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; EXP:UniProtKB. DR GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; TAS:Reactome. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. DR CDD; cd14510; PTP_VSP_TPTE; 1. DR FunFam; 3.90.190.10:FF:000053; Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2; 1. DR FunFam; 1.20.120.350:FF:000067; Transmembrane phosphatase with tensin homology; 1. DR FunFam; 2.60.40.1110:FF:000004; Voltage-sensor containing phosphatase; 1. DR Gene3D; 2.60.40.1110; -; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR051281; Dual-spec_lipid-protein_phosph. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR057023; PTP-SAK. 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 PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1. DR PANTHER; PTHR12305:SF60; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE TPTE2-RELATED; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF10409; PTEN_C2; 1. DR Pfam; PF22784; PTP-SAK; 1. DR SMART; SM01326; PTEN_C2; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 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; Proteomics identification; KW Reference proteome; Transmembrane; 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 COMPBIAS 1..11 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..27 FT /note="Basic and acidic residues" 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 //