MTMR8_CHICK
ID MTMR8_CHICK Reviewed; 629 AA.
AC Q5F452;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Myotubularin-related protein 8;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000305};
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q96EF0};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305};
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q96EF0};
GN Name=MTMR8; ORFNames=RCJMB04_3d12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup (By similarity). Has phosphatase activity towards
CC phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-
CC bisphosphate (By similarity). {ECO:0000250|UniProtKB:Q96EF0}.
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:0000250|UniProtKB:Q96EF0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:57923; EC=3.1.3.95;
CC Evidence={ECO:0000250|UniProtKB:Q96EF0};
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q96EF0}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {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; AJ851448; CAH65082.1; -; mRNA.
DR RefSeq; NP_001012717.1; NM_001012699.1.
DR AlphaFoldDB; Q5F452; -.
DR SMR; Q5F452; -.
DR STRING; 9031.ENSGALP00000012257; -.
DR PaxDb; Q5F452; -.
DR GeneID; 422312; -.
DR KEGG; gga:422312; -.
DR CTD; 55613; -.
DR VEuPathDB; HostDB:geneid_422312; -.
DR eggNOG; KOG1089; Eukaryota.
DR InParanoid; Q5F452; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q5F452; -.
DR PRO; PR:Q5F452; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030591; MTMR8.
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 InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF36; PTHR10807:SF36; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Hydrolase; Lipid metabolism; Nucleus; Reference proteome.
FT CHAIN 1..629
FT /note="Myotubularin-related protein 8"
FT /id="PRO_0000330035"
FT DOMAIN 126..500
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT COILED 517..543
FT /evidence="ECO:0000255"
FT ACT_SITE 338
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 275..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 338..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
SQ SEQUENCE 629 AA; 71967 MW; 40530390FCC9BCB2 CRC64;
MEHITTPKVE NVKLLDRYTN RKAASGTLYL TATHLIYVDA SAEVRKETWI LHHHIATVEK
LPLTTAGCPL LIHCKNFHVA HFVIGQERDC HEVYTSLLKL SQPVKPEELY AFSYNPKMSK
DNREIGWKLI DLKVDYQRMG IPNDYWEITD LNKDYEVCNT YPPEIVVPRA ASKATVIGSS
RFRSRGRIPV LSYLYKENNA AICRCSQPLS GFSARCLEDE QMLQAIREAN PGSPFMYVVD
TRPKLNAMAN RAAGKGYENE DNYDNIRFKF IGIENIHVMR SSLQKLLEVC ETKSPSMSDF
LTGLENSGWL RHIKAVMDAS VFLAKAVKDE KASVLVHCSD GWDRTAQVCS LASLLLDPFY
RAFKGFMVLI EKEWIAMGHK FSHRCGHLDG DPKEVSPVFT QFIECVWQLM QQFPCTFEFN
EHFLLEIHDH VYSCQFGNFL GTCHKEREDL KIFEKTHSLW PFLLQKKQEL RNPLYRGFTA
YKELQPNTLP FSFQFWCGMY NRFDKGMHPK QCVLDHLLSC MNQKIKLEDN ASELENKLPF
LDGPLPNEAC FLSKVGCAAS KTPMLNTPQD YEGEAPPVLT NGISVGDINV TSDVDQRNKE
NLANHRDLHL NDSVDVLNSE AKDGKPQHH
