MTMR3

Protein identityUniProt · HPA

UniProt accession

Q13615

Gene

MTMR3

Ensembl

ENSG00000100330

Chromosome

22

Canonical length

1198 aa

Protein class

Enzymes, Plasma proteins, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Cytosol

OverviewNCBI Gene

This gene encodes a member of the myotubularin dual specificity protein phosphatase gene family. The encoded protein is structurally similar to myotubularin but in addition contains a FYVE domain and an N-terminal PH-GRAM domain. The protein can self-associate and also form heteromers with another myotubularin related protein. The protein binds to phosphoinositide lipids through the PH-GRAM domain, and can hydrolyze phosphatidylinositol(3)-phosphate and phosphatidylinositol(3,5)-biphosphate in vitro. The encoded protein has been observed to have a perinuclear, possibly membrane-bound, distribution in cells, but it has also been found free in the cytoplasm. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1198 residues, UniProt reviewed canonical sequence.

>Q13615|MTMR3
     1  MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED AIIALSNYRL
    61  HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQEW LKRLNNAIRP
   121  PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN
   181  INEKYKLCGS YPQELIVPAW ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV
   241  SWWGWRNADD EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS
   301  GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ
   361  SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH AVDQDQRPVL VHCSDGWDRT
   421  PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL
   481  DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL
   541  RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP
   601  DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL SSLAGPGEDP
   661  LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE SGVEEPAHRA GIEIQEGKED
   721  PLLEKESRRK TPEASAIGLH QDPELGDAAL RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ
   781  VPPRGEDSLE VPVEQFRIEE IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP
   841  NVDSSTDMLV EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH
   901  RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM YPTPNGHCAN
   961  GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR PSATSSPDQP SRSHLDDDGM
  1021  SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ ELKSRLESQY LTSSLHFNGD FGDEVTSIPD
  1081  SESNLDQNCL SRCSTEIFSE ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH
  1141  CRNCGNVFCS SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MTMR3 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.46

Highest tissue expression

77 nTPM

Expression across tissuesHPA

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.26

gnomAD pLI

1

gnomAD missense Z

2

DepMap mean gene effect

-0.09

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to glucose starvation
• macroautophagy
• midbody abscission
• phosphatidylinositol 5-phosphate metabolic process
• phosphatidylinositol biosynthetic process
• phosphatidylinositol dephosphorylation
• protein dephosphorylation
• regulation of autophagosome assembly
• regulation of phosphatidylinositol dephosphorylation

Molecular functions

• molecular adaptor activity
• phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity
• phosphatidylinositol-3-phosphate phosphatase activity
• protein phosphatase binding
• protein serine/threonine phosphatase activity
• protein tyrosine phosphatase activity
• protein tyrosine/serine/threonine phosphatase activity
• zinc ion binding

Cellular components

• cytoplasm
• cytosol
• membrane

Protein domainsUniProt · Pfam · InterPro

• FYVE zinc finger
• Protein-tyrosine phosphatase, catalytic
• Myotubularin-like, phosphatase domain
• Zinc finger, FYVE/PHD-type
• Zinc finger, RING/FYVE/PHD-type
• Protein-tyrosine phosphatase, active site
• Zinc finger, FYVE-related
• Protein-tyrosine phosphatase-like
• Myotubularin
• FYVE zinc finger
• Myotubularin-like phosphatase domain
• MTMR3, PH-GRAM domain
• MTMR3, protein tyrosine phosphatase domain

KeywordsUniProt

• Coiled coil
• Cytoplasm
• Hydrolase
• Lipid metabolism
• Membrane
• Metal-binding
• Phosphoprotein
• Zinc
• Zinc-finger

InteractionsUniProt · HPA

Protein binding partners of MTMR3 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• MTOR
• YWHAB
• YWHAG
• YWHAH