RMD3_HUMAN
ID RMD3_HUMAN Reviewed; 470 AA.
AC Q96TC7; A9UMZ9; B3KRR3; Q6ZWE9; Q96H23; Q96SD6; Q9H6G1; Q9NVQ6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Regulator of microtubule dynamics protein 3;
DE Short=RMD-3;
DE Short=hRMD-3;
DE AltName: Full=Cerebral protein 10;
DE AltName: Full=Protein FAM82A2;
DE AltName: Full=Protein FAM82C;
DE AltName: Full=Protein tyrosine phosphatase-interacting protein 51;
DE AltName: Full=TCPTP-interacting protein 51;
GN Name=RMDN3; Synonyms=FAM82A2, FAM82C, PTPIP51;
GN ORFNames=hucep-10, UNQ3122/PRO10274;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.;
RT "Molecular cloning of a novel gene expressed in human cerebral cortex.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-470.
RA Porsche A., Hofer W.H.;
RT "A protein interacting with T-cell tyrosine phosphatase.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
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 [8]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PTPN2.
RX PubMed=15609043; DOI=10.1007/s00418-004-0732-7;
RA Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W.,
RA Steger K., Wimmer M.;
RT "The novel protein PTPIP51 exhibits tissue- and cell-specific expression.";
RL Histochem. Cell Biol. 123:19-28(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16820967; DOI=10.1007/s10495-006-8882-9;
RA Lv B.F., Yu C.F., Chen Y.Y., Lu Y., Guo J.H., Song Q.S., Ma D.L., Shi T.P.,
RA Wang L.;
RT "Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel
RT mitochondria protein with an N-terminal mitochondrial targeting sequence
RT and induces apoptosis.";
RL Apoptosis 11:1489-1501(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17361080; DOI=10.1159/000098949;
RA Stenzinger A., Schreiner D., Pfeiffer T., Tag C., Hofer H.W., Wimmer M.;
RT "Epidermal growth factor-, transforming growth factor-beta-, retinoic
RT acid- and 1,25-dihydroxyvitamin D(3)-regulated expression of the novel
RT protein PTPIP51 in keratinocytes.";
RL Cells Tissues Organs 184:76-87(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS REGULATION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH VAPB.
RX PubMed=22131369; DOI=10.1093/hmg/ddr559;
RA De Vos K.J., Morotz G.M., Stoica R., Tudor E.L., Lau K.F., Ackerley S.,
RA Warley A., Shaw C.E., Miller C.C.;
RT "VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium
RT homeostasis.";
RL Hum. Mol. Genet. 21:1299-1311(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-183; SER-193; SER-212
RP AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MOSPD2, SUBCELLULAR
RP LOCATION, DOMAIN, FFAT MOTIF, AND MUTAGENESIS OF 157-VAL--SER-172.
RX PubMed=29858488; DOI=10.15252/embr.201745453;
RA Di Mattia T., Wilhelm L.P., Ikhlef S., Wendling C., Spehner D., Nomine Y.,
RA Giordano F., Mathelin C., Drin G., Tomasetto C., Alpy F.;
RT "Identification of MOSPD2, a novel scaffold for endoplasmic reticulum
RT membrane contact sites.";
RL EMBO Rep. 19:0-0(2018).
CC -!- FUNCTION: Involved in cellular calcium homeostasis regulation. May
CC participate in differentiation and apoptosis of keratinocytes.
CC Overexpression induces apoptosis. {ECO:0000269|PubMed:16820967,
CC ECO:0000269|PubMed:22131369}.
CC -!- SUBUNIT: Interacts with PTPN2. Interacts with microtubules. Interacts
CC with VAPB. Interacts (FFAT motif) with MOSPD2 (via MSP domain)
CC (PubMed:29858488). {ECO:0000269|PubMed:15609043,
CC ECO:0000269|PubMed:18070910, ECO:0000269|PubMed:22131369,
CC ECO:0000269|PubMed:29858488}.
CC -!- INTERACTION:
CC Q96TC7; O14569: CYB561D2; NbExp=3; IntAct=EBI-1056589, EBI-717654;
CC Q96TC7; P54852: EMP3; NbExp=3; IntAct=EBI-1056589, EBI-3907816;
CC Q96TC7; Q92520: FAM3C; NbExp=3; IntAct=EBI-1056589, EBI-2876774;
CC Q96TC7; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-1056589, EBI-11991950;
CC Q96TC7; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-1056589, EBI-2820517;
CC Q96TC7; Q8NHP6: MOSPD2; NbExp=4; IntAct=EBI-1056589, EBI-2812848;
CC Q96TC7; Q8IXM6: NRM; NbExp=3; IntAct=EBI-1056589, EBI-10262547;
CC Q96TC7; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-1056589, EBI-448407;
CC Q96TC7; P60201-2: PLP1; NbExp=3; IntAct=EBI-1056589, EBI-12188331;
CC Q96TC7; Q8WWT9: SLC13A3; NbExp=3; IntAct=EBI-1056589, EBI-12938720;
CC Q96TC7; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-1056589, EBI-10262251;
CC Q96TC7; P32856-2: STX2; NbExp=3; IntAct=EBI-1056589, EBI-11956649;
CC Q96TC7; Q13277: STX3; NbExp=3; IntAct=EBI-1056589, EBI-1394295;
CC Q96TC7; P02787: TF; NbExp=3; IntAct=EBI-1056589, EBI-714319;
CC Q96TC7; P02786: TFRC; NbExp=3; IntAct=EBI-1056589, EBI-355727;
CC Q96TC7; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-1056589, EBI-8644968;
CC Q96TC7; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-1056589, EBI-2844246;
CC Q96TC7; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-1056589, EBI-348587;
CC Q96TC7; Q969S6: TMEM203; NbExp=3; IntAct=EBI-1056589, EBI-12274070;
CC Q96TC7; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-1056589, EBI-12887458;
CC Q96TC7; Q15836: VAMP3; NbExp=3; IntAct=EBI-1056589, EBI-722343;
CC Q96TC7; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-1056589, EBI-6256462;
CC Q96TC7; P31946: YWHAB; NbExp=5; IntAct=EBI-1056589, EBI-359815;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16820967, ECO:0000269|PubMed:17361080,
CC ECO:0000269|PubMed:22131369, ECO:0000269|PubMed:29858488}; Single-pass
CC membrane protein {ECO:0000269|PubMed:16820967}. Cytoplasm
CC {ECO:0000269|PubMed:17361080}. Nucleus {ECO:0000269|PubMed:17361080}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}.
CC Note=In interphase localizes in the cytoplasm, and during mitosis
CC localizes to the spindle microtubules and spindle poles.
CC {ECO:0000269|PubMed:18070910}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96TC7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96TC7-2; Sequence=VSP_025531;
CC -!- TISSUE SPECIFICITY: Present at high level in epidermis and seminiferous
CC epithelium: while basal cells in the epidermis and spermatogonia show
CC no perceptible amount, keratinocytes of suprabasal layers and
CC differentiating first-order spermatocytes up to spermatids exhibit high
CC expression. In skeletal muscle, its presence is restricted to fibers of
CC the fast twitch type. In surface epithelia containing ciliated cells,
CC it is associated with the microtubular structures responsible for
CC ciliary movement. Also present in specific structures of the central
CC nervous system such as neurons of the hippocampal region, ganglion
CC cells of the autonomic nervous system, and axons of the peripheral
CC nervous system (at protein level). Widely expressed.
CC {ECO:0000269|PubMed:15609043, ECO:0000269|PubMed:16820967}.
CC -!- INDUCTION: By EGF, TGFB1, retinoic acid- and 1,25-dihydroxyvitamin
CC D(3). {ECO:0000269|PubMed:17361080}.
CC -!- DOMAIN: The transmembrane region is required for mitochondrial
CC localization.
CC -!- DOMAIN: The FFAT motif is required for interaction with MOSPD2.
CC {ECO:0000269|PubMed:29858488}.
CC -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15298.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85554.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB000782; BAB46923.1; -; mRNA.
DR EMBL; AY358793; AAQ89153.1; -; mRNA.
DR EMBL; AK001441; BAA91693.1; -; mRNA.
DR EMBL; AK025963; BAB15298.1; ALT_SEQ; mRNA.
DR EMBL; AK092058; BAG52475.1; -; mRNA.
DR EMBL; AK123282; BAG53885.1; -; mRNA.
DR EMBL; AK123192; BAC85554.1; ALT_FRAME; mRNA.
DR EMBL; CH471125; EAW92436.1; -; Genomic_DNA.
DR EMBL; BC008970; AAH08970.2; -; mRNA.
DR EMBL; BC063844; AAH63844.1; -; mRNA.
DR EMBL; AJ242719; CAC39480.1; -; Genomic_DNA.
DR EMBL; BR000691; FAA00416.1; -; mRNA.
DR CCDS; CCDS10063.1; -. [Q96TC7-1]
DR RefSeq; NP_001291731.1; NM_001304802.1. [Q96TC7-1]
DR RefSeq; NP_001310823.1; NM_001323894.1. [Q96TC7-1]
DR RefSeq; NP_001310824.1; NM_001323895.1. [Q96TC7-2]
DR RefSeq; NP_060615.1; NM_018145.2. [Q96TC7-1]
DR PDB; 7CC7; X-ray; 1.45 A; A=236-470.
DR PDBsum; 7CC7; -.
DR AlphaFoldDB; Q96TC7; -.
DR SMR; Q96TC7; -.
DR BioGRID; 120476; 347.
DR IntAct; Q96TC7; 51.
DR MINT; Q96TC7; -.
DR STRING; 9606.ENSP00000260385; -.
DR iPTMnet; Q96TC7; -.
DR PhosphoSitePlus; Q96TC7; -.
DR SwissPalm; Q96TC7; -.
DR BioMuta; RMDN3; -.
DR DMDM; 147643203; -.
DR EPD; Q96TC7; -.
DR jPOST; Q96TC7; -.
DR MassIVE; Q96TC7; -.
DR MaxQB; Q96TC7; -.
DR PaxDb; Q96TC7; -.
DR PeptideAtlas; Q96TC7; -.
DR PRIDE; Q96TC7; -.
DR ProteomicsDB; 78224; -. [Q96TC7-1]
DR ProteomicsDB; 78225; -. [Q96TC7-2]
DR TopDownProteomics; Q96TC7-1; -. [Q96TC7-1]
DR TopDownProteomics; Q96TC7-2; -. [Q96TC7-2]
DR Antibodypedia; 2473; 198 antibodies from 22 providers.
DR DNASU; 55177; -.
DR Ensembl; ENST00000260385.10; ENSP00000260385.6; ENSG00000137824.16. [Q96TC7-1]
DR Ensembl; ENST00000338376.8; ENSP00000342493.3; ENSG00000137824.16. [Q96TC7-1]
DR GeneID; 55177; -.
DR KEGG; hsa:55177; -.
DR MANE-Select; ENST00000338376.8; ENSP00000342493.3; NM_018145.3; NP_060615.1.
DR UCSC; uc001zmp.1; human. [Q96TC7-1]
DR CTD; 55177; -.
DR DisGeNET; 55177; -.
DR GeneCards; RMDN3; -.
DR HGNC; HGNC:25550; RMDN3.
DR HPA; ENSG00000137824; Low tissue specificity.
DR MIM; 611873; gene.
DR neXtProt; NX_Q96TC7; -.
DR OpenTargets; ENSG00000137824; -.
DR PharmGKB; PA162387926; -.
DR VEuPathDB; HostDB:ENSG00000137824; -.
DR eggNOG; ENOG502QWUP; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_2_1; -.
DR InParanoid; Q96TC7; -.
DR OMA; QHESMHS; -.
DR OrthoDB; 1380644at2759; -.
DR PhylomeDB; Q96TC7; -.
DR TreeFam; TF315854; -.
DR PathwayCommons; Q96TC7; -.
DR SignaLink; Q96TC7; -.
DR SIGNOR; Q96TC7; -.
DR BioGRID-ORCS; 55177; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; RMDN3; human.
DR GenomeRNAi; 55177; -.
DR Pharos; Q96TC7; Tbio.
DR PRO; PR:Q96TC7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96TC7; protein.
DR Bgee; ENSG00000137824; Expressed in ileal mucosa and 194 other tissues.
DR ExpressionAtlas; Q96TC7; baseline and differential.
DR Genevisible; Q96TC7; HS.
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; IDA:HPA.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
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; IMP: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 3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Membrane; Microtubule; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Regulator of microtubule dynamics protein 3"
FT /id="PRO_0000287510"
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..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..124
FT /evidence="ECO:0000255"
FT MOTIF 157..172
FT /note="FFAT"
FT /evidence="ECO:0000269|PubMed:29858488"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJU9"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025531"
FT VARIANT 33
FT /note="Q -> H (in dbSNP:rs11558807)"
FT /id="VAR_049029"
FT MUTAGEN 157..172
FT /note="Missing: Reduces interaction with MOSPD2."
FT /evidence="ECO:0000269|PubMed:29858488"
FT CONFLICT 416
FT /note="F -> V (in Ref. 1; BAB46923)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="R -> Q (in Ref. 3; BAC85554)"
FT /evidence="ECO:0000305"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 338..358
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 363..377
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 399..412
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 418..430
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:7CC7"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:7CC7"
SQ SEQUENCE 470 AA; 52118 MW; 1C8D1022E6CF7B6A CRC64;
MSRLGALGGA RAGLGLLLGT AAGLGFLCLL YSQRWKRTQR HGRSQSLPNS LDYTQTSDPG
RHVMLLRAVP GGAGDASVLP SLPREGQEKV LDRLDFVLTS LVALRREVEE LRSSLRGLAG
EIVGEVRCHM EENQRVARRR RFPFVRERSD STGSSSVYFT ASSGATFTDA ESEGGYTTAN
AESDNERDSD KESEDGEDEV SCETVKMGRK DSLDLEEEAA SGASSALEAG GSSGLEDVLP
LLQQADELHR GDEQGKREGF QLLLNNKLVY GSRQDFLWRL ARAYSDMCEL TEEVSEKKSY
ALDGKEEAEA ALEKGDESAD CHLWYAVLCG QLAEHESIQR RIQSGFSFKE HVDKAIALQP
ENPMAHFLLG RWCYQVSHLS WLEKKTATAL LESPLSATVE DALQSFLKAE ELQPGFSKAG
RVYISKCYRE LGKNSEARWW MKLALELPDV TKEDLAIQKD LEELEVILRD
