ID TPTE_HUMAN Reviewed; 551 AA. AC P56180; B2RAP7; C9J6D6; C9JKK8; Q6XPS4; Q6XPS5; Q71JA8; Q8NCS8; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 189. DE RecName: Full=Putative tyrosine-protein phosphatase TPTE; DE EC=3.1.3.48; DE AltName: Full=Cancer/testis antigen 44; DE Short=CT44; DE AltName: Full=Transmembrane phosphatase with tensin homology; DE AltName: Full=Tumor antigen BJ-HCC-5; GN Name=TPTE; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP GLU-386 AND PRO-470. RC TISSUE=Testis; RX PubMed=10598804; DOI=10.1007/s004390051122; RA Chen H., Rossier C., Morris M.A., Scott H.S., Gos A., Bairoch A., RA Antonarakis S.E.; RT "A testis-specific gene, TPTE, encodes a putative transmembrane tyrosine RT phosphatase and maps to the pericentromeric region of human chromosomes 21 RT and 13, and to chromosomes 15, 22, and Y."; RL Hum. Genet. 105:399-409(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANTS GLU-386 AND RP PRO-470. 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 [MRNA] (ISOFORM 2), AND VARIANT GLU-386. RC TISSUE=Hepatoma; RA Dong X.-Y., Chen W.-F.; RT "Cloning and identification of genes which are differentially expressed in RT hepatocellular carcinoma."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-386. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-386 RP AND PRO-470. RC TISSUE=Testis; 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 [7] RP VARIANT [LARGE SCALE ANALYSIS] GLN-144. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Could be involved in signal transduction. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; CC -!- INTERACTION: CC P56180-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11960323, EBI-16439278; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Alpha; CC IsoId=P56180-1; Sequence=Displayed; CC Name=2; Synonyms=Beta; CC IsoId=P56180-2; Sequence=VSP_017321; CC Name=3; Synonyms=Gamma; CC IsoId=P56180-3; Sequence=VSP_017320; CC Name=4; Synonyms=Delta; CC IsoId=P56180-4; Sequence=VSP_017319; CC -!- TISSUE SPECIFICITY: Exclusively expressed in testis. CC {ECO:0000269|PubMed:10598804}. 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; AF007118; AAC34574.1; -; mRNA. DR EMBL; AY219886; AAP45143.1; -; mRNA. DR EMBL; AY219887; AAP45144.1; -; mRNA. DR EMBL; AY219888; AAP45145.1; -; mRNA. DR EMBL; AF495908; AAQ06674.1; -; mRNA. DR EMBL; AK314285; BAG36944.1; -; mRNA. DR EMBL; AF254982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF254983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL078471; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL163201; CAB90528.1; -; Genomic_DNA. DR EMBL; BC028719; AAH28719.1; -; mRNA. DR CCDS; CCDS74771.1; -. [P56180-1] DR CCDS; CCDS74772.1; -. [P56180-2] DR CCDS; CCDS74773.1; -. [P56180-3] DR CCDS; CCDS77617.1; -. [P56180-4] DR RefSeq; NP_001277153.1; NM_001290224.1. [P56180-4] DR RefSeq; NP_954868.1; NM_199259.3. [P56180-2] DR RefSeq; NP_954869.1; NM_199260.3. [P56180-3] DR RefSeq; NP_954870.2; NM_199261.3. [P56180-1] DR AlphaFoldDB; P56180; -. DR SMR; P56180; -. DR BioGRID; 113031; 129. DR IntAct; P56180; 85. DR MINT; P56180; -. DR STRING; 9606.ENSP00000484403; -. DR DEPOD; TPTE; -. DR iPTMnet; P56180; -. DR PhosphoSitePlus; P56180; -. DR BioMuta; TPTE; -. DR DMDM; 313104272; -. DR jPOST; P56180; -. DR MassIVE; P56180; -. DR PaxDb; 9606-ENSP00000484403; -. DR PeptideAtlas; P56180; -. DR ProteomicsDB; 56895; -. [P56180-1] DR ProteomicsDB; 56896; -. [P56180-2] DR ProteomicsDB; 56897; -. [P56180-3] DR ProteomicsDB; 56898; -. [P56180-4] DR Antibodypedia; 73437; 335 antibodies from 34 providers. DR DNASU; 7179; -. DR Ensembl; ENST00000427445.6; ENSP00000482488.1; ENSG00000274391.5. [P56180-3] DR Ensembl; ENST00000612746.1; ENSP00000483087.1; ENSG00000274391.5. [P56180-4] DR Ensembl; ENST00000618007.5; ENSP00000484403.1; ENSG00000274391.5. [P56180-1] DR Ensembl; ENST00000622113.4; ENSP00000482040.1; ENSG00000274391.5. [P56180-2] DR GeneID; 7179; -. DR KEGG; hsa:7179; -. DR MANE-Select; ENST00000618007.5; ENSP00000484403.1; NM_199261.4; NP_954870.3. DR UCSC; uc002yip.2; human. [P56180-1] DR AGR; HGNC:12023; -. DR CTD; 7179; -. DR DisGeNET; 7179; -. DR GeneCards; TPTE; -. DR HGNC; HGNC:12023; TPTE. DR HPA; ENSG00000274391; Tissue enriched (testis). DR MIM; 604336; gene. DR neXtProt; NX_P56180; -. DR OpenTargets; ENSG00000274391; -. DR PharmGKB; PA36702; -. DR VEuPathDB; HostDB:ENSG00000274391; -. DR eggNOG; KOG2283; Eukaryota. DR GeneTree; ENSGT00940000154335; -. DR HOGENOM; CLU_020105_3_0_1; -. DR InParanoid; P56180; -. DR OMA; CPKFAND; -. DR OrthoDB; 5477362at2759; -. DR PhylomeDB; P56180; -. DR TreeFam; TF354329; -. DR PathwayCommons; P56180; -. DR Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane. DR SignaLink; P56180; -. DR BioGRID-ORCS; 7179; 29 hits in 1124 CRISPR screens. DR ChiTaRS; TPTE; human. DR GeneWiki; TPTE; -. DR GenomeRNAi; 7179; -. DR Pharos; P56180; Tbio. DR PRO; PR:P56180; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P56180; Protein. DR Bgee; ENSG00000274391; Expressed in right testis and 27 other cell types or tissues. DR ExpressionAtlas; P56180; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro. DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd14510; PTP_VSP_TPTE; 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; IPR005821; Ion_trans_dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. 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; PF00102; Y_phosphatase; 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. DR Genevisible; P56180; HS. PE 1: Evidence at protein level; KW Alternative splicing; Hydrolase; Membrane; Protein phosphatase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..551 FT /note="Putative tyrosine-protein phosphatase TPTE" FT /id="PRO_0000215907" FT TRANSMEM 91..111 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 228..404 FT /note="Phosphatase tensin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590" FT DOMAIN 411..540 FT /note="C2 tensin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 338 FT /evidence="ECO:0000255" FT VAR_SEQ 1..138 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14659893" FT /id="VSP_017319" FT VAR_SEQ 41..78 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14659893" FT /id="VSP_017320" FT VAR_SEQ 41..58 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14659893, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_017321" FT VARIANT 144 FT /note="R -> Q (in a breast cancer sample; somatic mutation; FT dbSNP:rs144333919)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036516" FT VARIANT 195 FT /note="R -> Q (in dbSNP:rs1810856)" FT /id="VAR_057347" FT VARIANT 386 FT /note="K -> E (in dbSNP:rs212146)" FT /evidence="ECO:0000269|PubMed:10598804, FT ECO:0000269|PubMed:14659893, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_065097" FT VARIANT 470 FT /note="L -> P (in dbSNP:rs150482)" FT /evidence="ECO:0000269|PubMed:10598804, FT ECO:0000269|PubMed:14659893, ECO:0000269|PubMed:15489334" FT /id="VAR_025400" FT VARIANT 482 FT /note="Y -> S (in dbSNP:rs9996)" FT /id="VAR_061895" FT VARIANT 549 FT /note="G -> E (in dbSNP:rs169758)" FT /id="VAR_057348" SQ SEQUENCE 551 AA; 64322 MW; 48C2F28BEAA0DDA6 CRC64; MNESPDPTDL AGVIIELGPN DSPQTSEFKG ATEEAPAKES PHTSEFKGAA RVSPISESVL ARLSKFEVED AENVASYDSK IKKIVHSIVS SFAFGLFGVF LVLLDVTLIL ADLIFTDSKL YIPLEYRSIS LAIALFFLMD VLLRVFVERR QQYFSDLFNI LDTAIIVILL LVDVVYIFFD IKLLRNIPRW THLLRLLRLI ILLRIFHLFH QKRQLEKLIR RRVSENKRRY TRDGFDLDLT YVTERIIAMS FPSSGRQSFY RNPIKEVVRF LDKKHRNHYR VYNLCSERAY DPKHFHNRVV RIMIDDHNVP TLHQMVVFTK EVNEWMAQDL ENIVAIHCKG GTDRTGTMVC AFLIASEICS TAKESLYYFG ERRTDKTHSE KFQGVKTPSQ KRYVAYFAQV KHLYNWNLPP RRILFIKHFI IYSIPRYVRD LKIQIEMEKK VVFSTISLGK CSVLDNITTD KILIDVFDGL PLYDDVKVQF FYSNLPTYYD NCSFYFWLHT SFIENNRLYL PKNELDNLHK QKARRIYPSD FAVEILFGEK MTSSDVVAGS D //