MTMRC_MOUSE
ID MTMRC_MOUSE Reviewed; 747 AA.
AC Q80TA6; Q8BVX4; Q8C0P1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Myotubularin-related protein 12;
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 12 {ECO:0000305};
GN Name=Mtmr12; Synonyms=Kiaa1682;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH MTM1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=23818870; DOI=10.1371/journal.pgen.1003583;
RA Gupta V.A., Hnia K., Smith L.L., Gundry S.R., McIntire J.E., Shimazu J.,
RA Bass J.R., Talbot E.A., Amoasii L., Goldman N.E., Laporte J., Beggs A.H.;
RT "Loss of catalytically inactive lipid phosphatase myotubularin-related
RT protein 12 impairs myotubularin stability and promotes centronuclear
RT myopathy in zebrafish.";
RL PLoS Genet. 9:E1003583-E1003583(2013).
CC -!- FUNCTION: Acts as an adapter for the myotubularin-related phosphatases
CC (PubMed:23818870). Regulates phosphatase MTM1 protein stability and
CC possibly its intracellular location (PubMed:23818870). By stabilizing
CC MTM1 protein levels, required for skeletal muscle maintenance but not
CC for myogenesis (PubMed:23818870). {ECO:0000269|PubMed:23818870}.
CC -!- SUBUNIT: Heterodimer with lipid phosphatase MTM1 (PubMed:23818870).
CC Heterodimer with lipid phosphatase MTMR2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9C0I1, ECO:0000269|PubMed:23818870}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C0I1}.
CC Sarcoplasmic reticulum {ECO:0000269|PubMed:23818870}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000269|PubMed:23818870}. 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 (PubMed:23818870). In skeletal muscles, co-
CC localizes with MTM1 in the sarcomere (PubMed:23818870). Partially
CC localizes to the sarcoplasmic reticulum in skeletal muscles
CC (PubMed:23818870). {ECO:0000250|UniProtKB:Q9C0I1,
CC ECO:0000269|PubMed:23818870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TA6-2; Sequence=VSP_030723;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscles (at protein level).
CC {ECO:0000269|PubMed:23818870}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during skeletal muscle cell
CC differentiation followed by a decrease at later stages of
CC differentiation. {ECO:0000269|PubMed:23818870}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122539; BAC65821.1; ALT_INIT; mRNA.
DR EMBL; AK030139; BAC26803.1; -; mRNA.
DR EMBL; AK076161; BAC36227.1; ALT_INIT; mRNA.
DR EMBL; BC054352; AAH54352.1; -; mRNA.
DR CCDS; CCDS27388.1; -. [Q80TA6-1]
DR RefSeq; NP_766546.1; NM_172958.3. [Q80TA6-1]
DR AlphaFoldDB; Q80TA6; -.
DR SMR; Q80TA6; -.
DR BioGRID; 234557; 6.
DR STRING; 10090.ENSMUSP00000041227; -.
DR iPTMnet; Q80TA6; -.
DR PhosphoSitePlus; Q80TA6; -.
DR EPD; Q80TA6; -.
DR jPOST; Q80TA6; -.
DR MaxQB; Q80TA6; -.
DR PaxDb; Q80TA6; -.
DR PeptideAtlas; Q80TA6; -.
DR PRIDE; Q80TA6; -.
DR ProteomicsDB; 286080; -. [Q80TA6-1]
DR ProteomicsDB; 286081; -. [Q80TA6-2]
DR Antibodypedia; 9766; 111 antibodies from 21 providers.
DR DNASU; 268783; -.
DR Ensembl; ENSMUST00000038172; ENSMUSP00000041227; ENSMUSG00000039458. [Q80TA6-1]
DR Ensembl; ENSMUST00000071993; ENSMUSP00000071883; ENSMUSG00000039458. [Q80TA6-2]
DR GeneID; 268783; -.
DR KEGG; mmu:268783; -.
DR UCSC; uc007vhl.1; mouse. [Q80TA6-1]
DR UCSC; uc011zrl.1; mouse. [Q80TA6-2]
DR CTD; 54545; -.
DR MGI; MGI:2443034; Mtmr12.
DR VEuPathDB; HostDB:ENSMUSG00000039458; -.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000160263; -.
DR HOGENOM; CLU_021912_2_0_1; -.
DR InParanoid; Q80TA6; -.
DR OMA; LRFQGHG; -.
DR OrthoDB; 620702at2759; -.
DR PhylomeDB; Q80TA6; -.
DR TreeFam; TF315197; -.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR BioGRID-ORCS; 268783; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mtmr12; mouse.
DR PRO; PR:Q80TA6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80TA6; protein.
DR Bgee; ENSMUSG00000039458; Expressed in spermatid and 220 other tissues.
DR ExpressionAtlas; Q80TA6; baseline and differential.
DR Genevisible; Q80TA6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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 GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum.
FT CHAIN 1..747
FT /note="Myotubularin-related protein 12"
FT /id="PRO_0000315826"
FT DOMAIN 205..643
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 449..558
FT /note="Interaction with MTM1"
FT /evidence="ECO:0000250"
FT REGION 548..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VAR_SEQ 48..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030723"
SQ SEQUENCE 747 AA; 85516 MW; D4D2AE2E8772500E CRC64;
MLGKGGVGGG GGTKAPKPSF VSYVRPEEIH TDEKEVTEKE VTLHLLPGEQ LLCEASTVLK
YVQEDSCQRG VYGRLVCTDF KISFLGDEDS ALDNGGEAQF KNKIIGVNDV PLHCVDQIYG
VFDEKKKPLF GQLKKYPEKL VIHCKDLRVL HFCLRYTKEE EVKRIVSGII HHTQSPKLLK
RLFLFSYAAA VHGTATDSRN CTVMFDTPKD WCWELERTKG SVKYRTVSVN EGYRVSDRLP
AYFVVPTPLP EDDVRRFQGH GIPIWCWSCH NGSALLKMSA LPKEQDDGAL QVQKSFLDGI
YKTIHRPPYE MVKTEDLSSN FLSLQEIQSA YCKFKQLFLI DNSSEFWDTD IKWFSLLESS
SWLDIIRRCL KKAIEITECL EAQNVNVLLL EENASDLCCL LSSLVQVMMD AHCRTRTGFQ
SLIQKEWVMG GHSFLDRCNH LHQSDKEEVP IFLLFLDCVW QLVHQYPPAF EFTETYLTVL
SDSLYIPIFS TFFFNSPHQK DTNMGRENLD AQSKPLTLLT VWDWSVQFEP KAQTLLRNPL
YVEKPKLDRG QQKGSRFKHQ RQLSLPLTQS KSSPKRGFFR EETDHLIKNL LGKRISKLIN
SSDDLQDSSR EFYDSWHSKP TDYHGLLLPH IEGPEIKVWA QRYLRWIPEA QILGGGRVAT
MGKLLEMMEE VQSLQEKIEA RHHRQEAVHA EAPGLLRNSV RLSSLFPFAL LQRHSAKPVL
PTSGWKALGG EDDLAKREDE FVDLGDV
