RMD3_MOUSE
ID RMD3_MOUSE Reviewed; 470 AA.
AC Q3UJU9; A9UN03; Q3U5Y8; Q3UB61; Q6P8M2; Q7TNF2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Regulator of microtubule dynamics protein 3;
DE Short=RMD-3;
DE Short=mRMD-3;
DE AltName: Full=Protein FAM82A2;
DE AltName: Full=Protein FAM82C;
GN Name=Rmdn3; Synonyms=Fam82a2, Fam82c;
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].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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.
RX PubMed=18070910; DOI=10.1083/jcb.200705108;
RA Oishi K., Okano H., Sawa H.;
RT "RMD-1, a novel microtubule-associated protein, functions in chromosome
RT segregation in Caenorhabditis elegans.";
RL J. Cell Biol. 179:1149-1162(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Involved in cellular calcium homeostasis regulation (By
CC similarity). May participate in differentiation and apoptosis of
CC keratinocytes. Overexpression induces apoptosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPN2. Interacts with microtubules. Interacts
CC with VAPB. Interacts (FFAT motif) with MOSPD2 (via MSP domain).
CC {ECO:0000250|UniProtKB:Q96TC7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96TC7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96TC7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96TC7}. Nucleus {ECO:0000250|UniProtKB:Q96TC7}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96TC7}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96TC7}.
CC Note=In interphase localizes in the cytoplasm, and during mitosis
CC localizes to the spindle microtubules and spindle poles.
CC {ECO:0000250|UniProtKB:Q96TC7}.
CC -!- DOMAIN: The transmembrane region is required for mitochondrial
CC localization. {ECO:0000250}.
CC -!- DOMAIN: The FFAT motif is required for interaction with MOSPD2.
CC {ECO:0000250|UniProtKB:Q96TC7}.
CC -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55754.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH61186.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=FAA00420.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK146299; BAE27056.1; -; mRNA.
DR EMBL; AK151090; BAE30103.1; -; mRNA.
DR EMBL; AK153369; BAE31937.1; -; mRNA.
DR EMBL; AK153322; BAE31902.1; -; mRNA.
DR EMBL; AL772264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055754; AAH55754.1; ALT_INIT; mRNA.
DR EMBL; BC061186; AAH61186.1; ALT_SEQ; mRNA.
DR EMBL; BR000695; FAA00420.1; ALT_INIT; mRNA.
DR CCDS; CCDS16591.1; -.
DR RefSeq; NP_001028308.1; NM_001033136.3.
DR AlphaFoldDB; Q3UJU9; -.
DR SMR; Q3UJU9; -.
DR BioGRID; 212454; 83.
DR IntAct; Q3UJU9; 79.
DR MINT; Q3UJU9; -.
DR STRING; 10090.ENSMUSP00000092283; -.
DR iPTMnet; Q3UJU9; -.
DR PhosphoSitePlus; Q3UJU9; -.
DR EPD; Q3UJU9; -.
DR jPOST; Q3UJU9; -.
DR MaxQB; Q3UJU9; -.
DR PaxDb; Q3UJU9; -.
DR PeptideAtlas; Q3UJU9; -.
DR PRIDE; Q3UJU9; -.
DR ProteomicsDB; 299835; -.
DR Antibodypedia; 2473; 198 antibodies from 22 providers.
DR Ensembl; ENSMUST00000094695; ENSMUSP00000092283; ENSMUSG00000070730.
DR GeneID; 67809; -.
DR KEGG; mmu:67809; -.
DR UCSC; uc008lte.2; mouse.
DR CTD; 55177; -.
DR MGI; MGI:1915059; Rmdn3.
DR VEuPathDB; HostDB:ENSMUSG00000070730; -.
DR eggNOG; ENOG502QWUP; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_2_1; -.
DR InParanoid; Q3UJU9; -.
DR OMA; QHESMHS; -.
DR OrthoDB; 1380644at2759; -.
DR PhylomeDB; Q3UJU9; -.
DR TreeFam; TF315854; -.
DR BioGRID-ORCS; 67809; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Rmdn3; mouse.
DR PRO; PR:Q3UJU9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UJU9; protein.
DR Bgee; ENSMUSG00000070730; Expressed in pigmented layer of retina and 261 other tissues.
DR ExpressionAtlas; Q3UJU9; baseline and differential.
DR Genevisible; Q3UJU9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044232; C:organelle membrane contact site; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Membrane;
KW Microtubule; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Regulator of microtubule dynamics protein 3"
FT /id="PRO_0000287511"
FT TOPO_DOM 1..12
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 168..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..125
FT /evidence="ECO:0000255"
FT MOTIF 157..172
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT CONFLICT 210
FT /note="K -> R (in Ref. 1; BAE31902/BAE31937)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> S (in Ref. 3; AAH61186)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="K -> E (in Ref. 1; BAE27056 and 3; AAH61186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52029 MW; BA82C57843985A1B CRC64;
MSRLGALGGS RAGLGLLLGT AAGLGFLCVL YSQRWKRTQR HGRSHSLPNS LDYAQASERG
RQVTQFRAIP GEAGDAAILP SLSQEGQEKV LDRLDFVLTS LMALRREVEE LQRSLQGLAG
EIVGEVRSHI EENQRVARRR RFPFARERSD STGSSSVYFT ASSGAALTDA ESEGGYTTAN
AESDYERDSD KESGDAEDEV SCETVRMGRK DSLDLDVEAA SSPAAAALEE DDSSGREDVQ
LVLLQADELH QGSKQDKREG FQLLLNNKLA YGSRQDFLWR LARAYSDMSD LTEEESGKKS
YALNGKEEAE AALKKGDESA ACHLWYAVLC GQLAEHEGIS KRIQSGFSFK EHVDKAIELQ
PEDPRGHFLL GRWCYQVSHL NWLEKKTATA LFESPLSATV QDALQSFLKA EELQPGFSKA
GRVYISKCYR ELGKNSEARK WMKLAQELPD VTNEDSAFQK DLEELEVILG
