RMD2_MACFA
ID RMD2_MACFA Reviewed; 410 AA.
AC Q95LL7; Q95JM7; Q95JS8; Q95K01;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Regulator of microtubule dynamics protein 2;
DE Short=RMD-2;
DE AltName: Full=Protein FAM82A1;
GN Name=RMDN2; Synonyms=FAM82A, FAM82A1;
GN ORFNames=QtsA-11631, QtsA-13801, QtsA-15186, QtsA-20236;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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=4;
CC Name=1;
CC IsoId=Q95LL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95LL7-2; Sequence=VSP_025528;
CC Name=3;
CC IsoId=Q95LL7-3; Sequence=VSP_025528, VSP_025530;
CC Name=4;
CC IsoId=Q95LL7-4; Sequence=VSP_025528, VSP_025529;
CC -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=BAB63046.1; Type=Miscellaneous discrepancy; Note=a stop codon at position 16 which was translated as Arg to extend the sequence and a stop codon at position 125 which was translated as Arg to extend the sequence.; Evidence={ECO:0000305};
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DR EMBL; AB070101; BAB63046.1; ALT_SEQ; mRNA.
DR EMBL; AB070026; BAB62971.1; -; mRNA.
DR EMBL; AB070154; BAB63099.1; -; mRNA.
DR EMBL; AB072771; BAB69740.1; -; mRNA.
DR AlphaFoldDB; Q95LL7; -.
DR SMR; Q95LL7; -.
DR STRING; 9541.XP_005576156.1; -.
DR eggNOG; ENOG502QS2U; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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 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_0000287505"
FT TRANSMEM 10..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 122..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..110
FT /evidence="ECO:0000255"
FT COMPBIAS 132..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSE0"
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="MPHSTNKELIFGIMVGTAGISLLLLWYHKVRKPEKTMKLPKFLSLDNTFNSI
FT TLQDEVHNDQGTTVIFQERQLQILEKLNELLTNMEELKEEIRFLKETVPKLEEYIQDEL
FT GGKITVHKVSPQHRARKRRLPTIQSSATSNSSEEAESEGG -> MGKCLSCCKEDQSFQ
FT RCSPEDQVTTDAQHRGASSISQPNISLGHKTSYSPITRKVNSAKASRRLLSLSSPSFSE
FT RRCSLFVGFQNRNASSYRQQSTANFDSEEDTSFTDLKSSSDHFGSFMSCRRRFSSRKLS
FT IVSYYKSANFFDPQASGQNVFNLKEIEIFSKTSNNTDAKKHITISAPEYNTKNFKNFET
FT NTTFPAFGNTIDTASYQQSTSSFFSLANDVSSPDQQNGIATDIQQRGQLCKDLKDFLHP
FT GTESYSTDRSAITIQQHPSQSGTFPFLHKAGFSSSYKNSGCFIPFQNEVTSGPSEDEDF
FT AVLFQDEDRSSPIEIPKIR (in isoform 2, isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:12498619, ECO:0000303|Ref.2"
FT /id="VSP_025528"
FT VAR_SEQ 394..410
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025529"
FT VAR_SEQ 404..410
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12498619"
FT /id="VSP_025530"
FT CONFLICT 161
FT /note="E -> K (in Ref. 2; BAB69740)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="K -> E (in Ref. 2; BAB62971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 47493 MW; 67143F7486B5A5F7 CRC64;
MPHSTNKELI FGIMVGTAGI SLLLLWYHKV RKPEKTMKLP KFLSLDNTFN SITLQDEVHN
DQGTTVIFQE RQLQILEKLN ELLTNMEELK EEIRFLKETV PKLEEYIQDE LGGKITVHKV
SPQHRARKRR LPTIQSSATS NSSEEAESEG GYITANTDTE EQSFPVPKAF NTHVEELNLD
VLLQKVDHLR MSESGKSESF ELLCDHKEKF RDKIEFMWRF ARAYGDMYEL STNTQEKKHY
ANIGRTLSER AINRAPMNGH CHLWYAVLCG YVSEFEGLQN KINYGHLFKE HLDIAIKLLP
EEPFLYYLKG RYCYTVSKLS WIEKKMAATL FGKIPSSTVQ EALHNFLKAE ELCPGYSNPN
YMYLAKCYAD LEENQNALKF CNLALLLPTV TKEDKEAQKE MQKIMTSLKR
