ID A0A2K1INK6_PHYPA Unreviewed; 876 AA.
AC A0A2K1INK6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN ORFNames=PHYPA_027177 {ECO:0000313|EMBL:PNR30861.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR30861.1};
RN [1] {ECO:0000313|EMBL:PNR30861.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c22_15020V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR30861.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c22_15020V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c22_15020V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) 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 EMBL; ABEU02000022; PNR30861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1INK6; -.
DR STRING; 3218.A0A2K1INK6; -.
DR PaxDb; 3218-PP1S71_215V6-1; -.
DR EnsemblPlants; Pp3c22_15020V3.1; Pp3c22_15020V3.1; Pp3c22_15020.
DR EnsemblPlants; Pp3c22_15020V3.4; Pp3c22_15020V3.4; Pp3c22_15020.
DR EnsemblPlants; Pp3c22_15020V3.5; Pp3c22_15020V3.5; Pp3c22_15020.
DR Gramene; Pp3c22_15020V3.1; Pp3c22_15020V3.1; Pp3c22_15020.
DR Gramene; Pp3c22_15020V3.4; Pp3c22_15020V3.4; Pp3c22_15020.
DR Gramene; Pp3c22_15020V3.5; Pp3c22_15020V3.5; Pp3c22_15020.
DR InParanoid; A0A2K1INK6; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000006727; Chromosome 22.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14507; PTP-MTM-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 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:UP000006727}.
FT DOMAIN 174..635
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 488..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 671..705
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 756..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 424
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 424..430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 876 AA; 95633 MW; E1145F2E22888514 CRC64;
MVGWHGVDIV STGESWIDGL DWTPVEVGNR VAQKSSGRSL ILAGDGFLLP AEAVVEEARG
AVLVNLEIAG TLFVTNFRLV FLGGGAKQPL PLGTIPLLTI ETFAKQVAKI PLSSSSAASR
RLLTIVGKDL RTITFGFLPH TKQRRKVREA LAYRTRPTRL WDLYTFSDAY PSSGDPRQRL
RAEYIRLMSG NTHGFQNMME QSKRGSAWRL SEVNSNYSIC PTYPSLLVMP ACISDHDVQQ
AALFRSRGRL AHLCWQHPDN GAVLARSSQP FTGFVSSRSK EDEQLVAAVC NTANQRRKLY
IADARPRKNA LANGVTGGGS ESSANYLQSE VIFLGIDNIH GMRDSLTKMR DFLDIHGAAS
SDGSSSLLRS GGRAWVGGNV ASVAGAASAL GDSGWLLHCH KILTSAVWIA ARIHLEGASV
LVHCSDGWDR TAQLVCLASL LLDPYYRTFQ GFQALIEKDW LAFGHMFSER LGIPTFTGTR
NLNNATSSVM RQAGQPSTSP VRAAVENSSS PAGNNSPGAQ SSQYSPIFLQ WMDAVAQLLR
IYPSAFEFTQ AFLVELLDCV LSCRFGNFLC NSEKERVQGG ITESTACVWA YLKQLRDQKG
REHEHYNLFY NSAQNAGVLL PPAAATAPSL WRQYFLRWSC PSLANSGGSP PVGWTHGGDL
ETAAHVLAER FSSVRNAKEK AEEKVQELLA EKRALMEQLR EEQQARLSAM AAAMRGRRET
AALKQVIEAV GCKIRINSVA PQLIDASDED SPDTGRGGNI GQNPSNQGGN SRENDSDEQQ
LSVSVSMRPD TDSTTDVIRR PCGAEYHSSC RLRPGETCRW PQTSCARIGS SFIGLRADFG
ALERLSILDS YFDSEQADIE GERDTPQPPS HISGVT
//
