RMD3_RAT
ID RMD3_RAT Reviewed; 471 AA.
AC Q66H15;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Regulator of microtubule dynamics protein 3;
DE Short=RMD-3;
DE AltName: Full=Protein FAM82A2;
DE AltName: Full=Protein FAM82C;
GN Name=Rmdn3; Synonyms=Fam82a2, Fam82c;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC082081; AAH82081.1; -; mRNA.
DR RefSeq; NP_001014068.1; NM_001014046.2.
DR AlphaFoldDB; Q66H15; -.
DR SMR; Q66H15; -.
DR STRING; 10116.ENSRNOP00000016356; -.
DR iPTMnet; Q66H15; -.
DR PhosphoSitePlus; Q66H15; -.
DR jPOST; Q66H15; -.
DR PaxDb; Q66H15; -.
DR PRIDE; Q66H15; -.
DR Ensembl; ENSRNOT00000016356; ENSRNOP00000016356; ENSRNOG00000011690.
DR GeneID; 311328; -.
DR KEGG; rno:311328; -.
DR UCSC; RGD:1308697; rat.
DR CTD; 55177; -.
DR RGD; 1308697; Rmdn3.
DR eggNOG; ENOG502QWUP; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_2_1; -.
DR InParanoid; Q66H15; -.
DR OMA; QHESMHS; -.
DR OrthoDB; 1380644at2759; -.
DR PhylomeDB; Q66H15; -.
DR TreeFam; TF315854; -.
DR PRO; PR:Q66H15; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000011690; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q66H15; RN.
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; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044232; C:organelle membrane contact site; ISO:RGD.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
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..471
FT /note="Regulator of microtubule dynamics protein 3"
FT /id="PRO_0000287513"
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..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 168..203
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:22673903"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJU9"
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:0000250|UniProtKB:Q96TC7"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
SQ SEQUENCE 471 AA; 52312 MW; 6B3FA1CF970F8C55 CRC64;
MSRLGALGGS RAGLGLLLGT AAGLGFLCVL YSQRWKRTQR HGRSQSLPNS LDYAQTSERG
RQVTQLRAIP GEAGDAAMLS SLPQEGQEKV LDRLDFVLTS LMALRREVEE LQRSLQGLAG
EIVGEVRSHM EENQRVARRR RFPFARERSD STGSSSVYFT ASSGATLTDA ESEGGYTTAN
AESDYERDSD KESEDAEDEV SCETVKMGRK DSLDLDMEVA SSPASAALED DDSSGLEDVQ
LLLQQADELH QGSEQNKQEG FQLLLNNKLA YGSRQDFLWR LARAYSDMTE LTEEESEKKS
YALNGKEEAE AALKKGDESA ASHLWYAVLC GQLAEHEGIS KRIQSGFSFK EHVDKAIELQ
PEDPRGHFLL GRWCYQVSHL SWLEKKTATA LFESPLSATV QDALQSFLKA EELQPGFSKA
GRVYISKCYR ELGKNSEARK WLNLAQELPN ITNEDSAFQK DLEELEVILG K
