ID   RMD3_XENLA              Reviewed;         463 AA.
AC   Q5EAU9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in cellular calcium homeostasis regulation.
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 FFAT motif is required for interaction with MOSPD2.
CC       {ECO:0000250|UniProtKB:Q96TC7}.
CC   -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
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DR   EMBL; BC090235; AAH90235.1; -; mRNA.
DR   RefSeq; NP_001089993.1; NM_001096524.1.
DR   AlphaFoldDB; Q5EAU9; -.
DR   SMR; Q5EAU9; -.
DR   GeneID; 735064; -.
DR   CTD; 735064; -.
DR   Xenbase; XB-GENE-5892561; rmdn3.L.
DR   OrthoDB; 1380644at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 735064; Expressed in brain and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..463
FT                   /note="Regulator of microtubule dynamics protein 3"
FT                   /id="PRO_0000287514"
FT   TOPO_DOM        1..4
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..463
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          153..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          279..302
FT                   /evidence="ECO:0000255"
FT   MOTIF           146..161
FT                   /note="FFAT"
FT                   /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT   COMPBIAS        173..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  52020 MW;  EAC151BB68502F73 CRC64;
     MSKLILSYRI GLGLVVGAAA GAVIYIVFRR NRKKTRKWTS KQNGYYSQKG DELDTSNNLQ
     AIPGEADILT GSRGEQLDLL NRLDYVLSSI VELHQEVETL RSSLHGLAED IVGEVRTHLE
     ENQRTLRRRR FLPHRERTDS TGSSSIYFTA TSGAAHTDAE SEGGYSTAYA ESDFERESSR
     ASEAEEEDEV SCETIRTMRR DSVDLVTDDD DDEATTIATD PVDEELTLLL QKSDELHSGS
     TEQQREGFQL LLNNKLLYGD HQEFLWRLAR SYSDMCTIAE DAQEKKSFAS EGKEEAEAAL
     QKGDQNAECH KWFAILCGQL SEHEGIQKRI QTGYLFKEHI EKAISLKPGD ARCYYLLGRW
     CYEVSNLGWL ERKTASALYE NPPTATVHEA LQNFLKAEDL TPGFSKAARV LIAKCYKDLG
     NNATAAHWLK LAADLPNVTQ EDRESTTTIE EMLPATAEEE LLV