RMD2_BOVIN
ID RMD2_BOVIN Reviewed; 410 AA.
AC Q2TBQ7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Regulator of microtubule dynamics protein 2;
DE Short=RMD-2;
DE AltName: Full=Protein FAM82A1;
GN Name=RMDN2; Synonyms=FAM82A, FAM82A1;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-213 (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC Note=In interphase localizes in the cytoplasm, and during mitosis
CC localizes to the spindle microtubules and spindle poles. Also detected
CC as large dots in the perinuclear region (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2TBQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TBQ7-2; Sequence=VSP_025523;
CC -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DV832064; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC109797; AAI09798.1; -; mRNA.
DR EMBL; DV832064; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001035598.1; NM_001040508.1. [Q2TBQ7-2]
DR RefSeq; XP_010808221.1; XM_010809919.2.
DR AlphaFoldDB; Q2TBQ7; -.
DR SMR; Q2TBQ7; -.
DR STRING; 9913.ENSBTAP00000043981; -.
DR PaxDb; Q2TBQ7; -.
DR PRIDE; Q2TBQ7; -.
DR Ensembl; ENSBTAT00000046712; ENSBTAP00000043981; ENSBTAG00000032905. [Q2TBQ7-2]
DR Ensembl; ENSBTAT00000082938; ENSBTAP00000066743; ENSBTAG00000032905. [Q2TBQ7-1]
DR GeneID; 506362; -.
DR KEGG; bta:506362; -.
DR CTD; 151393; -.
DR VEuPathDB; HostDB:ENSBTAG00000032905; -.
DR eggNOG; ENOG502QS2U; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_046369_0_0_1; -.
DR InParanoid; Q2TBQ7; -.
DR OMA; DLGQKNN; -.
DR OrthoDB; 1380644at2759; -.
DR TreeFam; TF315854; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000032905; Expressed in diaphragm and 106 other tissues.
DR ExpressionAtlas; Q2TBQ7; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
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 Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..410
FT /note="Regulator of microtubule dynamics protein 2"
FT /id="PRO_0000287503"
FT TRANSMEM 10..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 122..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..109
FT /evidence="ECO:0000255"
FT COMPBIAS 132..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q498D5"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT VAR_SEQ 1..151
FT /note="MPHSTNREMILGIVVGTAGISLLLLWYHKVRKPRTAMSLPKFLSLGNSLDLM
FT TLQDEMPSGQGTTAIFQGRQLQILEKLNELLTHMEELKEEIRVLKEAIPKLEEYIQGEL
FT GGKVTVHKISPQHRARKRRLATVQSSATSNSSEEAESEGG -> MGKCLSCYKEEQNCQ
FT PKCPADQLPSDLLHRGASSVIQPTKFLDFKAARPTPMLKGSSHKGSKISSPSSNVSFYA
FT TFLERRHSLFPKFQKSSTSLHTVQSRANFDSEEKRSFIDLKSASEHFRFRSRSVFSAPK
FT LSIISCYENAGTFDASSSCIFNPNEVEVISKNSNITGAEKYIHSYSAEYDTTYFMKSKS
FT KANSSACRDTVATLYQSTATMLTLPSIISYSSEQHGIDNDIQERDQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025523"
SQ SEQUENCE 410 AA; 47067 MW; FFCCBD355505E688 CRC64;
MPHSTNREMI LGIVVGTAGI SLLLLWYHKV RKPRTAMSLP KFLSLGNSLD LMTLQDEMPS
GQGTTAIFQG RQLQILEKLN ELLTHMEELK EEIRVLKEAI PKLEEYIQGE LGGKVTVHKI
SPQHRARKRR LATVQSSATS NSSEEAESEG GYVTANTDTE EQSFPVPKEF NTHVEELNLD
ALIQRADNLR VNESRKVESF ELLCDHKEKF RDEIEFIWRF ARAYGDMYEL STNIQEKKHY
ANIGKTLGEK AIMRAPKNGY CHLWYAVLCG YVSEFEGLQN KINYGYRFKE HLDKAIEFLP
EEPFLYYLKG RYCYAVSKLS WIERKMAATL FGNIPSSTVQ EALQNFLKVE ELQPGFSKSN
YMFMAKCYAD LNQIDSAMKF CNLAVLLPCI TKEDKDAQKE VKKISTSLKR
