MTMR5_CAEEL
ID MTMR5_CAEEL Reviewed; 1744 AA.
AC Q9TXP3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Myotubularin-related protein 5 {ECO:0000305};
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 5 {ECO:0000305};
GN Name=mtm-5 {ECO:0000312|WormBase:H28G03.6};
GN ORFNames=H28G03.6 {ECO:0000312|WormBase:H28G03.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=21076391; DOI=10.1038/emboj.2010.278;
RA Silhankova M., Port F., Harterink M., Basler K., Korswagen H.C.;
RT "Wnt signalling requires MTM-6 and MTM-9 myotubularin lipid-phosphatase
RT function in Wnt-producing cells.";
RL EMBO J. 29:4094-4105(2010).
CC -!- FUNCTION: Probably acts as an adapter for other myotubularin-like
CC phosphatases (Probable). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no obvious
CC phenotype. {ECO:0000269|PubMed:21076391}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 1284 in the dsPTPase catalytic loop and does not have phosphatase
CC activity (By similarity). The pocket is however sufficiently preserved
CC to bind phosphorylated substrates, and maybe protect them from
CC phosphatases. {ECO:0000250|UniProtKB:O95248, ECO:0000305}.
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DR EMBL; BX284606; CCD72477.1; -; Genomic_DNA.
DR PIR; A89531; A89531.
DR RefSeq; NP_508888.2; NM_076487.3.
DR AlphaFoldDB; Q9TXP3; -.
DR SMR; Q9TXP3; -.
DR STRING; 6239.H28G03.6; -.
DR EPD; Q9TXP3; -.
DR PaxDb; Q9TXP3; -.
DR PeptideAtlas; Q9TXP3; -.
DR PRIDE; Q9TXP3; -.
DR EnsemblMetazoa; H28G03.6.1; H28G03.6.1; WBGene00003477.
DR GeneID; 180792; -.
DR KEGG; cel:CELE_H28G03.6; -.
DR UCSC; H28G03.6; c. elegans.
DR CTD; 180792; -.
DR WormBase; H28G03.6; CE35733; WBGene00003477; mtm-5.
DR eggNOG; KOG1090; Eukaryota.
DR GeneTree; ENSGT00940000168586; -.
DR HOGENOM; CLU_002298_1_1_1; -.
DR InParanoid; Q9TXP3; -.
DR OMA; CAERNPP; -.
DR OrthoDB; 45015at2759; -.
DR PhylomeDB; Q9TXP3; -.
DR Reactome; R-CEL-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q9TXP3; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003477; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR002219; PE/DAG-bd.
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 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 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.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1744
FT /note="Myotubularin-related protein 5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436267"
FT DOMAIN 14..150
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 165..304
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 306..412
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 787..871
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 996..1447
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT DOMAIN 1643..1743
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1540..1590
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1102..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1744 AA; 200188 MW; 20F8378C824FCA02 CRC64;
MRDPDKVKSG PICDTVAVIV LEESDDENAL PDVLHEVQSP HTSDNIPTSS IKKFARPRGW
YNQSVSSPSE FFYQILTTER GTRRIAYVLS TWEEDEKTLN FKAVSIVLIS QNFHPKAFKE
ILLEISNDLR TPEFSSSSEL IRFLTYELVE EGSTIEIRTK TLHVELGFEL IPISPVTGKD
VAMLFKMLGF QNVIKIIHAL LSDCRIVLAS SSLMRLSRCQ NAILSLLYPF EYVHSCVTIL
PDSLAEVLES PTPFLIGVLS EFVTSFGDEN IVVYLDNGEV HVPDHAEIYK SDDYYYNSLH
QRLRDVMFTT TSQEDLSIPN EERIEVDDFI LDKKLRACFI YYFAELLYGY QYYILYTRIK
GNFEKKLTTS LTFHVGAFRG FRKLTDMMSS SLLKSVYFQT FILTRALPRR KHDLFDEISC
FKELDQLIFK QNSTSSESKK IIEHISCELI QKERYMEKCS ARKQEIFTKI HWISGKELAQ
NNNSIIHTVK PKMRSNVILQ AMLPVVNTHA EYHANQFEAY AHRIEALRNC LAAIFEGKVA
FASKSLDAVK SSMRFAPLRI ELCRLLNQKC SHDKLTDKQF EDIALLMNAA LQAECEEDKD
GVVRSLMYLS NVYSRKVAQG MQQYMYTAVQ EHKVWKNQRF WTSCFYYEVH EMLFSEMLQK
DRKITESLWC HTLRPCAMEM INTDDTDQEE LVKQENEMIQ AQAKHFANIL ISLQIPLSEE
FFEHEDAHRS VLNEKCKWIV NTLDSILGVT GRINGLSLSR IQTYVEAHVE SLRDVYVEMS
TGEHLKKGNF DPVLAHGEFL ISDPIDCYLL TSIEESEMSL NRLENLLPAD GSLFLTNYRV
IFKGKSVDIN ATNGTIVQTI PLYSMESFKK LTNKKLIPTQ LIEKGVKIEH IISIRSSCAS
SIIIAFDEDE INNMAIEKFL EVIETNSHNS FAFYNTRKDM KVVENGSHKF GTLNSAIRGF
TKKKTDTRRI RSHSSHRGSI QLSFDKMEEL DYLKKNAHIR YAVIDYPRIG LNSKIVKLRM
SHSNLDYTIC PSYPGNFIVP SETNESELAK VAKGFVEHRL PVVVWMNENG ALLVRASAFT
SIDMVKKLKK VVNYRRNASK LTGSMTGSQQ TLHSKASSNE ESSSNIVAGA EIKSAEVQMN
YIAKLSNSSQ RAVSYALPTQ YADKFSTFND GCTLTQNNAN GFPTTRIHRK ALYVLLEKGH
GVKIPIDSNA EAIMVRSVKE SELRRSLQRA RQICSSEFQV ENRTSFLESW NASNWPQCVS
RMIELSNSIV ALMNLYNSSV AICLEAGRSI TTILSSLSQL LSDPYYRTCD GFQVLVEKEW
LAFGHYFHKD TETSSPSFIC FLDCVYQISQ QYPTAFEFSY FYISFLAYHS TAGYFRTFID
DCEEKRLQSD ANEFYLPDNL ATINVWEFIK LRNRVSAAFY NELYEQIGDI VIPSSSIPQI
HMWPFLAETH LKYGSPYDIE PASHEQQLVD PDYEEEEDWS KLNNTDIDER HLNRRVRSPE
RDPANMDMIR LLQKSYLTEL FDASDRKTTT NGESNGKETI HELTPFTVGA RPVQCCYCTN
ILTRWSKAVH CKKCRIHVHE GCVNRNITIG NITHTWDAKP FEDIKMPSGA IQIGTPQAEK
MLHSPNNTLT RESMSPPTAN TIPPLCTGYL SKRGAKLKLW VPRFFVLYPD SPKVYYYEDF
ENWKTAEKPS GCIDLVDFKS FNLEQTGRRG LIELHMKNKT HRLLSENINE AIRWKECIEQ
VIRD
