ID A0A452IYG1_9SAUR Unreviewed; 384 AA.
AC A0A452IYG1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000033097.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000033097.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR AlphaFoldDB; A0A452IYG1; -.
DR STRING; 38772.ENSGAGP00000033097; -.
DR Ensembl; ENSGAGT00000037517.1; ENSGAGP00000033097.1; ENSGAGG00000023622.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF34; MYOTUBULARIN-RELATED PROTEIN 6; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 1..262
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT COILED 279..313
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 98
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 35..36
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 98..104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 384 AA; 44318 MW; 2F2E11A34230EF74 CRC64;
MCVLLNAMAN RAAGKGYENE DNYANIRFQF VGIENIHVMR SSLQKLLEVS GTKALSINSF
LSGLENSGWL RHIKAVLDAA IFLAKAIAVE NATVLVHCSD GWDRTSQVCS LGSLLLDSHY
RTIKGFMVLI EKDWISFGHK FSDRCGQLDG DPKEISPVFT QFLEGVWHLT EQFPQAFEYN
EAFLLQIHEH VHSCQFGNFL GNCQKEREEL KLKERTYSLW PFLLDEQKKY LNPLYNRDFS
QKLVLLEPNT ASFNFKFWRN MYHQFDRTMH PRQSVFNLIM TISEQNKQLE KDFKELEAKM
KQRNRQSEEL LTKEPLQSVH PASPALKTSP CFKKEQSLLP MKDSIRTIEG SNTADNRYSE
YMEELSKAEP AVVSLEYGVA RMTC
//
