RMD3_BOVIN
ID RMD3_BOVIN Reviewed; 471 AA.
AC Q1JQC5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; BC116057; AAI16058.1; -; mRNA.
DR RefSeq; NP_001069147.1; NM_001075679.1.
DR RefSeq; XP_005211622.1; XM_005211565.3.
DR AlphaFoldDB; Q1JQC5; -.
DR SMR; Q1JQC5; -.
DR STRING; 9913.ENSBTAP00000003795; -.
DR PaxDb; Q1JQC5; -.
DR PRIDE; Q1JQC5; -.
DR Ensembl; ENSBTAT00000003795; ENSBTAP00000003795; ENSBTAG00000002921.
DR GeneID; 514748; -.
DR KEGG; bta:514748; -.
DR CTD; 55177; -.
DR VEuPathDB; HostDB:ENSBTAG00000002921; -.
DR VGNC; VGNC:33993; RMDN3.
DR eggNOG; ENOG502QWUP; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_2_1; -.
DR InParanoid; Q1JQC5; -.
DR OMA; QHESMHS; -.
DR OrthoDB; 1380644at2759; -.
DR TreeFam; TF315854; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000002921; Expressed in semen and 106 other tissues.
DR ExpressionAtlas; Q1JQC5; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044232; C:organelle membrane contact site; IEA:Ensembl.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
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..471
FT /note="Regulator of microtubule dynamics protein 3"
FT /id="PRO_0000287509"
FT TOPO_DOM 1..9
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 39..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..123
FT /evidence="ECO:0000255"
FT MOTIF 156..171
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT COMPBIAS 39..61
FT /note="Polar 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 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TC7"
FT MOD_RES 192
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; 51906 MW; 6FF0AB93C4F1157A CRC64;
MSSLGTLGGA RAGLGLLLGT AAGLGFLCAL YSQRWKRTQR RGQSQSQSNS LDYTQTSEPG
RQVRPLRAAP GEAGDAAVLS SLPRGQEVVL DRLEFVLTSL VALRREVEEL RSSLQGLAGQ
IVGEVRSHME ENQKVARRRR FPFARERSDS TGSSSVYFTA ASGATFTDAE SEGGYTTANA
ESDYERDSER ESDGDGEDEV SCETVKMGRK DSLDLEVEVA LGLEPEAPEA GGSPGQEDVM
PLLQQADELH QGSEQGKREG FQLLLNNKLV HGSRQDFLWR LARAYSDMCE LTEEASEKRS
YALSGKEEAE VALEKGNENA ECHQWYAVLC GQLAEHEGIQ RRIQSGFSFK EHVDKAIALK
PENPMAHFLL GRWCYQVSHL SWLEKKTATA LSESPLGATV QDALSSFLKA EELQPGFSKA
GRIYICKCYK ELGKNPEAKE WMKLALELPN VTKEDSAFQK DLEELEVILG E
