ID   MTMRC_PONAB             Reviewed;         747 AA.
AC   Q5R989;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Myotubularin-related protein 12;
DE   AltName: Full=Inactive phosphatidylinositol 3-phosphatase 12 {ECO:0000305};
GN   Name=MTMR12;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q80TA6}.
CC   -!- SUBUNIT: Heterodimer with lipid phosphatase MTM1 (By similarity).
CC       Heterodimer with lipid phosphatase MTMR2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q80TA6, ECO:0000250|UniProtKB:Q9C0I1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0I1}.
CC       Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q80TA6}. Cytoplasm,
CC       myofibril, sarcomere {ECO:0000250|UniProtKB:Q80TA6}. Note=Localizes to
CC       punctate vesicles when associated with MTM1 (By similarity). Localizes
CC       to triads, a structure formed by a T tubule and two sarcoplasmic
CC       reticulum terminal cisterna. In skeletal muscles, co-localizes with
CC       MTM1 in the sarcomere. Partially localizes to the sarcoplasmic
CC       reticulum in skeletal muscles (By similarity).
CC       {ECO:0000250|UniProtKB:Q80TA6, ECO:0000250|UniProtKB:Q9C0I1}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC       subfamily, lacks the conserved active site cysteine residue at position
CC       391 in the dsPTPase catalytic loop and does not have phosphatase
CC       activity. {ECO:0000250|UniProtKB:Q9C0I1}.
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DR   EMBL; CR859502; CAH91671.1; -; mRNA.
DR   RefSeq; NP_001128988.1; NM_001135516.1.
DR   AlphaFoldDB; Q5R989; -.
DR   SMR; Q5R989; -.
DR   STRING; 9601.ENSPPYP00000017173; -.
DR   GeneID; 100190828; -.
DR   KEGG; pon:100190828; -.
DR   CTD; 54545; -.
DR   eggNOG; KOG1089; Eukaryota.
DR   InParanoid; Q5R989; -.
DR   OrthoDB; 620702at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR030576; MTMR12.
DR   InterPro; IPR022587; MTMR12-like_C.
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   PANTHER; PTHR10807; PTHR10807; 1.
DR   PANTHER; PTHR10807:SF37; PTHR10807:SF37; 1.
DR   Pfam; PF12578; 3-PAP; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum.
FT   CHAIN           1..747
FT                   /note="Myotubularin-related protein 12"
FT                   /id="PRO_0000315828"
FT   DOMAIN          205..643
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..558
FT                   /note="Interaction with MTM1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         564
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0I1"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5FVM6"
FT   MOD_RES         716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0I1"
SQ   SEQUENCE   747 AA;  85946 MW;  5F49F1D13ED3A558 CRC64;
     MLGKGVVGGG GGTKGPKPSF VSYVRPEEIH TNEKEVTEKE VTLHLLPGEQ LLCEASTVLK
     YVQEDSCQHG VYGRLVCTDF KIAFLGDDES ALDNDETQFK NKVIGENDIT LHCVDQIYGV
     FDEKKKTLFG QLKKYPGKLI IHCKDFRVFQ FCLGYTKEEE VKRIVSGIIH HTQAPKLLKR
     LFLFSYATAA QNNTVTDPKN HTVMFDTLKD WCWELERTKG NMKYKAVSVN EGYKVCERLP
     AYFVVPTPLP EENVQRFQGH GIPIWCWSCH NGSALLKMSA LPKEQDDGIL QIQKSFLDGI
     YKTIHRSPYE IVKTEDVSSN FLSLQEIQTA YSKFKQLFLT DNSTEFWDTD IKWFSLLESS
     SWLDIIRRCL KKAIEITECM EAQNMNVLLL EENASDLCCL ISSLVQLMMD PHCRTRIGFQ
     SLIQKEWVMG GHCFLDRCNH LRQNDKEEVP VFLLFLDCVW QLVHQHPPAF EFTETYLTVL
     SDSLYIPIFS TFFFNSPHQK DANMGREGQD AQSKPLNLLT VWDWSVQFEP KAQTLLKNPL
     YVEKPKLDKG QRKGMRFKHQ RQLSLPLTQS KSSPKRGFFR EETDHLIKNL LGKRISKLIN
     SSDELQDNFR EFYDSWHSKS TDYHGLLLPH IEGPEIKVWA QRYLRWIPEA QILGGGQVAT
     MSKLLEMMEE VQSLQEKIDE RHHSQQVPQA EAPCLLRNSA RLSSLFPFAL LQRHSSKPVL
     PTSGWKALGD EDDLAKREDE FVDLGDV