RMD3_PONAB
ID RMD3_PONAB Reviewed; 470 AA.
AC Q5R6Z1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR859250; CAH91430.1; -; mRNA.
DR EMBL; CR860332; CAH92469.1; -; mRNA.
DR RefSeq; NP_001125839.1; NM_001132367.1.
DR RefSeq; XP_009247991.1; XM_009249716.1.
DR RefSeq; XP_009247992.1; XM_009249717.1.
DR RefSeq; XP_009247993.1; XM_009249718.1.
DR AlphaFoldDB; Q5R6Z1; -.
DR SMR; Q5R6Z1; -.
DR STRING; 9601.ENSPPYP00000007199; -.
DR Ensembl; ENSPPYT00000007498; ENSPPYP00000007199; ENSPPYG00000006358.
DR GeneID; 100172768; -.
DR KEGG; pon:100172768; -.
DR CTD; 55177; -.
DR eggNOG; ENOG502QWUP; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_2_1; -.
DR InParanoid; Q5R6Z1; -.
DR OMA; QHESMHS; -.
DR OrthoDB; 1380644at2759; -.
DR TreeFam; TF315854; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript 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_0000287512"
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 167..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:0000250|UniProtKB:Q96TC7"
FT COMPBIAS 167..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:0000250|UniProtKB:Q96TC7"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
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 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
SQ SEQUENCE 470 AA; 52061 MW; 0149FCBFEC42091C CRC64;
MSRLGALGGA RAGLGLLLGT AAGLGFLCLL YSQRWKRTQR HGRSQSLPNS LGYTQTSDPG
RQVMLLRAVP GGAGDASVLP SLPREGQEKV LDRLDFVLTS LVALRREVEE LRSSLRGLAG
EIVGEVRSHM EENQRVARRR RFPFVRERSD STGSSSVYFT ASSGATFTDA ESEGGYTTAN
AESDNERDSD KESEDGEDEV SCETVKMGRK DSLDLEEEAA SGASSALEAG GSSGLEDVLP
LLQQADELHR GDEQGKREGF QLLLNNKLVY GSRQDFLWRL ARAYSDMCEL TEEVSEKKSY
ALDGKEEAEA ALEKGDESAD CHLWYAVLCG QLAEHESIQR RIQSGFSFKE HVDKAIALQP
ENPMAYFLLG RWCYQVSHLS WLEKKTATAL LESPLSATVE DALQSFLKAE ELQPGFSKAG
RVYISKCYRE LGKNSEARWW MKLALELPDV TKEDLALQKD LEELEVILRD
