ID   A0A8I5ZMD5_RAT          Unreviewed;       732 AA.
AC   A0A8I5ZMD5;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   10-JUN-2026, entry version 21.
DE   RecName: Full=Myotubularin-related protein 12 {ECO:0000256|ARBA:ARBA00018495};
DE   AltName: Full=Inactive phosphatidylinositol 3-phosphatase 12 {ECO:0000256|ARBA:ARBA00033343};
GN   Name=Mtmr12 {ECO:0000313|Ensembl:ENSRNOP00000078948.1,
GN   ECO:0000313|RGD:1307902};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000078948.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000078948.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000078948.1};
RA   Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT   "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT   reads and long range scaffolding.";
RL   Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000078948.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000078948.1};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Acts as an adapter for the myotubularin-related phosphatases.
CC       Regulates phosphatase MTM1 protein stability and possibly its
CC       intracellular location. By stabilizing MTM1 protein levels, required
CC       for skeletal muscle maintenance but not for myogenesis.
CC       {ECO:0000256|ARBA:ARBA00056705}.
CC   -!- SUBUNIT: Heterodimer with lipid phosphatase MTM1. Heterodimer with
CC       lipid phosphatase MTMR2. {ECO:0000256|ARBA:ARBA00062818}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000256|ARBA:ARBA00004204}. Sarcoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004369}.
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; A0A8I5ZMD5; -.
DR   Ensembl; ENSRNOT00000112203.2; ENSRNOP00000078948.1; ENSRNOG00000022929.6.
DR   RGD; 1307902; Mtmr12.
DR   GeneTree; ENSGT00940000160263; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   ExpressionAtlas; A0A8I5ZMD5; baseline and differential.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   CDD; cd14594; PTP-MTMR12; 1.
DR   FunFam; 2.30.29.30:FF:000188; Myotubularin related protein 12; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022587; MTMR12-like_C.
DR   InterPro; IPR030576; MTMR12_PTP.
DR   InterPro; IPR030564; Myotubularin.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF37; MYOTUBULARIN-RELATED PROTEIN 12; 1.
DR   Pfam; PF12578; 3-PAP; 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.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A8I5ZMD5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..732
FT                   /note="Myotubularin-related protein 12"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035204284"
FT   DOMAIN          190..628
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   REGION          533..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..546
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  84555 MW;  0B1BE7B2CDA60279 CRC64;
     MVVSWVIRKF LCFCCKVCFP FPGYPSFLSF PKPWRISLLP YTVLKYVQED SCQLGICGRL
     VCTDFRISFL GDEGSAVDNG AETHFKNKII GVNDIPLHCV DQIYGVFDEK KKPLFGQLKK
     YPEKLVIHCK DLRVLHFCLR YTKEEEVKRI VSGIIHHTQS PKLLKRLFLF SYAAAVHGTA
     ADPRNCTVMF DTPKDWCWEL ERTKGSVKYK TVSVNEGYRV CDRLPAYFVV PTPLLEDDVK
     RFQGRGIPIW CWSCHNGSAL LKMSALPKEQ DDSALQIQKS FLDGIYKTIH RPPYEMVKTE
     DLSSNFLSLQ EIQSSYCKFK QLFLIDSSSE FWDTDVKWFS LLESSGWLDI IRRCLKRAIE
     IIECLEAQNM NVLLLEENAS DLCCLLSSLV QVMMDAHCRT WTGFQSLIQK EWVMGGHSFL
     DRCNHLHQSD KEEVPVFLLF LDCVWQLVHQ HPPAFEFTET YLTVLSDSLY IPIFSTFFFN
     SPHQKDTNMG RESLDAQSKP LTLLTVWDWS VQFEPKAQTL LRNPLYVEKP KLDKGQRKGS
     RFKHQRQLSL PLTQSKSSPK RGFFREETDH LIKNLLGKRI SKLINSSDDL QDNSREFYDN
     WHSKPTDYHG LLLPHIEGPE IKVWAQRYLR WIPEAQILGG GRVATMGKLL EMMEEVQSLQ
     EKIEARHHRQ EAIHVQAPGL LRNSARLSSL FPFAMHQRHS AKPVLPTSGW KALGGEDDLA
     KREDEFVDLG DV
//