ID   RMD2_RAT                Reviewed;         412 AA.
AC   Q498D5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
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DR   EMBL; BC100261; AAI00262.1; -; mRNA.
DR   RefSeq; NP_001032277.1; NM_001037200.1.
DR   RefSeq; XP_006239697.1; XM_006239635.3.
DR   AlphaFoldDB; Q498D5; -.
DR   SMR; Q498D5; -.
DR   STRING; 10116.ENSRNOP00000008045; -.
DR   iPTMnet; Q498D5; -.
DR   PhosphoSitePlus; Q498D5; -.
DR   jPOST; Q498D5; -.
DR   PaxDb; Q498D5; -.
DR   PRIDE; Q498D5; -.
DR   Ensembl; ENSRNOT00000008045; ENSRNOP00000008045; ENSRNOG00000006082.
DR   GeneID; 313840; -.
DR   KEGG; rno:313840; -.
DR   UCSC; RGD:1559836; rat.
DR   CTD; 151393; -.
DR   RGD; 1559836; Rmdn2.
DR   eggNOG; ENOG502QS2U; Eukaryota.
DR   GeneTree; ENSGT00950000182992; -.
DR   HOGENOM; CLU_046369_0_0_1; -.
DR   InParanoid; Q498D5; -.
DR   OMA; WFERNIA; -.
DR   OrthoDB; 1380644at2759; -.
DR   PhylomeDB; Q498D5; -.
DR   TreeFam; TF315854; -.
DR   PRO; PR:Q498D5; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000006082; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q498D5; RN.
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; ISO:RGD.
DR   GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Regulator of microtubule dynamics protein 2"
FT                   /id="PRO_0000287507"
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          122..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        133..153
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:0007744|PubMed:22673903"
FT   MOD_RES         141
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   MOD_RES         154
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   MOD_RES         156
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   MOD_RES         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
SQ   SEQUENCE   412 AA;  47217 MW;  35F4936C0387830A CRC64;
     MPHSTHKELL LGIMAGTAGI SLLVLWYHKI LKPRTTMIFP KFLSLGKKSD SLTLQDESYS
     EQGTSVVFQR GQLQILEKLN ELLTNVEELK EEIKFLKETI PKLEECIQDE LGVRVTVHQV
     SPQHRARKKK TTTTTVQRPA TSNSSEEAES EGGYITANTD TEEQSFPVPK ALNTHIEDLK
     LDVLLQKVDH LRLNEAHKME SFELLCDHKE KFSEEIEFLW RLVRAYGDMY DLSTNTQEKK
     HYANVGKTLG ERAITRAPMN GHCHLWYALL CGYVSEFEGL QNKINCGHLF KKHLDIAIQL
     LPEEPVLYYL KGRYCYTVSK LSWIEKKMAA TLFGEIPSST VHEALHNFLK TEELQPGYSV
     SNYMYVAKCY VDLGESREAW KFCNLALLLP IVTKEDKDAH KEVKKIIGSL KR