MYOME_RAT
ID MYOME_RAT Reviewed; 2324 AA.
AC Q9WUJ3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Myomegalin;
DE AltName: Full=Phosphodiesterase 4D-interacting protein;
DE AltName: Full=Phosphodiesterase-binding protein clone 46;
GN Name=Pde4dip; Synonyms=Pbp46;
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 [MRNA], FUNCTION, INTERACTION WITH PDE4D, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=11134006; DOI=10.1074/jbc.m006546200;
RA Verde I., Pahlke G., Salanova M., Zhang G., Wang S., Coletti D.,
RA Onuffer J., Jin S.-L.C., Conti M.;
RT "Myomegalin is a novel protein of the Golgi/centrosome that interacts with
RT a cyclic nucleotide phosphodiesterase.";
RL J. Biol. Chem. 276:11189-11198(2001).
CC -!- FUNCTION: Functions as an anchor sequestering components of the cAMP-
CC dependent pathway to Golgi and/or centrosomes (PubMed:11134006). May
CC participate in microtubule dynamics, promoting microtubule assembly, in
CC an isoform-specific manner. Depending upon the cell context, may act at
CC the level of the Golgi apparatus or that of the centrosome. In complex
CC with AKAP9, recruits CAMSAP2 to the Golgi apparatus and tethers non-
CC centrosomal minus-end microtubules to the Golgi, an important step for
CC polarized cell movement. In complex with AKAP9, EB1/MAPRE1 and
CC CDK5RAP2, contributes to microtubules nucleation and extension from the
CC centrosome to the cell periphery, a crucial process for directed cell
CC migration, mitotic spindle orientation and cell-cycle progression (By
CC similarity). {ECO:0000250|UniProtKB:Q5VU43,
CC ECO:0000269|PubMed:11134006}.
CC -!- SUBUNIT: Interacts with PDE4D (PubMed:11134006). May interact with
CC MAPRE1 and MAPRE3. May form a pericentrosomal complex with AKAP9,
CC CDK5RAP2 and EB1/MAPRE1 in an isoform-specific manner; within this
CC complex, may mediate MAPRE1-binding to CDK5RAP2. Interaction with AKAP9
CC stabilizes both proteins. May interact with CAMSAP2 in an isoform-
CC specific manner; this interaction is much stronger in the presence of
CC AKAP9. In complex with AKAP9, recruits CAMSAP2 to the Golgi apparatus.
CC May interact with unglycosylated LGALS3BP in an isoform-specific
CC manner; this interaction may connect the pericentrosomal complex to the
CC gamma-tubulin ring complex (gamma-TuRC) to promote microtubule assembly
CC and acetylation (By similarity). {ECO:0000250|UniProtKB:Q5VU43,
CC ECO:0000269|PubMed:11134006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:11134006}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q5VU43}. Golgi apparatus
CC {ECO:0000269|PubMed:11134006}. Note=Associated with the microtubule
CC network at the growing distal tip of microtubules. Targeting to the
CC Golgi apparatus requires AKAP9. {ECO:0000250|UniProtKB:Q5VU43}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle
CC and to a lower extent in brain, lung and liver. Expressed in heart,
CC skeletal muscle and testis (at protein level).
CC {ECO:0000269|PubMed:11134006}.
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DR EMBL; AF139185; AAD29427.1; -; mRNA.
DR RefSeq; NP_071777.1; NM_022382.1.
DR AlphaFoldDB; Q9WUJ3; -.
DR SMR; Q9WUJ3; -.
DR BioGRID; 248991; 1.
DR IntAct; Q9WUJ3; 1.
DR STRING; 10116.ENSRNOP00000024900; -.
DR iPTMnet; Q9WUJ3; -.
DR PhosphoSitePlus; Q9WUJ3; -.
DR jPOST; Q9WUJ3; -.
DR PaxDb; Q9WUJ3; -.
DR PRIDE; Q9WUJ3; -.
DR GeneID; 64183; -.
DR KEGG; rno:64183; -.
DR UCSC; RGD:708410; rat.
DR CTD; 9659; -.
DR RGD; 708410; Pde4dip.
DR eggNOG; ENOG502QPV2; Eukaryota.
DR InParanoid; Q9WUJ3; -.
DR OrthoDB; 15127at2759; -.
DR PhylomeDB; Q9WUJ3; -.
DR PRO; PR:Q9WUJ3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR InterPro; IPR012943; Cnn_1N.
DR InterPro; IPR010630; Olduvai_dom.
DR Pfam; PF07989; Cnn_1N; 1.
DR Pfam; PF06758; Olduvai; 1.
DR SMART; SM01148; DUF1220; 1.
DR PROSITE; PS51316; ODV; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2324
FT /note="Myomegalin"
FT /id="PRO_0000307692"
FT DOMAIN 1550..1641
FT /note="Olduvai"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00647"
FT REGION 72..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..132
FT /evidence="ECO:0000255"
FT COILED 158..205
FT /evidence="ECO:0000255"
FT COILED 238..288
FT /evidence="ECO:0000255"
FT COILED 348..638
FT /evidence="ECO:0000255"
FT COILED 745..822
FT /evidence="ECO:0000255"
FT COILED 855..923
FT /evidence="ECO:0000255"
FT COILED 1011..1043
FT /evidence="ECO:0000255"
FT COILED 1213..1241
FT /evidence="ECO:0000255"
FT COILED 1346..1384
FT /evidence="ECO:0000255"
FT COILED 1430..1455
FT /evidence="ECO:0000255"
FT COILED 1821..2056
FT /evidence="ECO:0000255"
FT COILED 2248..2274
FT /evidence="ECO:0000255"
FT COMPBIAS 222..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 705
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VU43"
SQ SEQUENCE 2324 AA; 262042 MW; 305EE824A44D38B9 CRC64;
MSNGYRTLSQ HLNDLKKENF SLKLRIYFLE ERMQQKYEVS REDVYKRNIE LKVEVESLKR
ELQDRKQHLH KTWADEEDLN SQNEAELRRQ VEEPQQETEH VYELLDNNIQ LLQEESRFAK
DEATQMETLV EAEKGCNLEL SERWKDATKN REDAPGDQVK LDQYSAALAQ RDRRIEELRQ
SLAAQEGLVE QLSREKQQLL HLLEEPGGME VQPMPKGLPT QQKPDLNETP TTQPSVSDSH
LAELQDKIQQ TEVTNKILQE KLNDMSCELR SAQESSQKQD TTIQSLKEML KSRESETEEL
YQVIEGQNDT MAKLPEMLHQ SQLGQLQSSE GIAPAQQQVA LLDLQSALFC SQLEIQKLQR
LLRQKERQLA DGKRCMQFVE AAAQEREQQK EAAWKHNQEL RKALQHLQGE LHSKSQQLHV
LEAEKYNEIR TQGQNIQHLS HSLSHKEQLI QELQELLQYR DTTDKTLDTN EVFLEKLRQR
IQDRAVALER VIDEKFSALE EKDKELRQLR LAVRDRDHDL ERLRCVLSAN EATMQSMESL
LRARGLEVEQ LIATCQNLQW LKEELETKFG HWQKEQESII QQLQTSLHDR NKEVEDLSAT
LLHKLGPGQS EVAEELCQRL QRKERVLQDL LSDRNKQAME HEMEVQGLLQ SMGTREQERQ
AVAEKMVQAF MERNSELQAL RQYLGGKELM AASQAFISNQ PAGATSVGPH HGEQTDQGST
QMPSRDDSTS LTAREEASIP RSTLGDSDTV AGLEKELSNA KEELELMAKK ERESQIELSA
LQSMMAVQEE ELQVQAADLE SLTRNIQIKE DLIKDLQMQL VDPEDMPAME RLTQEVLLLR
EKVASVEPQG QEGSENRRQQ LLLMLEGLVD ERSRLNEALQ AERQLYSSLV KFHAQPETFE
RDRTLQVELE GAQVLRSRLE EVLGRSLERL SRLETLAAIG GATAGDETED TSTQFTDSIE
EEAAHNSHQQ LIKVSLEKSL TTMETQNTCL QPPSPVGEDG NRHLQEEMLH LRAEIHQPLE
EKRKAEAELK ELKAQIEEAG FSSVSHIRNT MLSLCLENAE LKEQMGEAMS DGWEVEEDKE
KGEVMVETVV AKGGLSEDSL QAEFRKVQGR LKSAYNIINL LKEQLVLRSS EGNTKEMPEF
LVRLAREVDR MNMGLPSSEK HQHQEQENMT ARPGPRPQSL KLGTALSVDG YQLENKSQAQ
DSGHQPEFSL PGSTKHLRSQ LAQCRQRYQD LQEKLLISEA TVFAQANQLE KYRAILSESL
VKQDSKQIQV DLQDLGYETC GRSENEAERE ETTSPECEEH GNLKPVVLVE GLCSEQGYLD
PVLVSSPVKN PWRTSQEARG VQAQGTSDDS SLLRKDIRDL KAQLQNAYKV IQNLRSRVRS
LSATSDYSSS LERPRKLRAV ATLEGASPHS VTDEDEGLLS DGTGAFYPPG LQAKKNLENL
IQRVSQLEAQ LPKTGLEGKL AEELKSASWP GKYDSLIQDQ ARKTVISASE NTKREKDLFS
SHPTFERYVK SFEDLLRNND LTTYLGQSFR EQLSSRRSVT DRLTSKFSTK DHKSEKEEAG
LEPLALRLSR ELQEKEKVIE VLQAKLDTRF SSPPSSHAAS DSHRSASSTS FLSDDIEACS
DMDVASEYTH YEEKKPSPSN SAASASQGLK GEPRSSSISL PTPQNPPKEA SQAQPGFHFN
SIPKPASLSQ APMHFTVPSF MPFGPSGPPL LGCCETPVVS LAEAQQELQM LQKQLGRSVS
IAPPTSTSTL LSNHTEASSP RYSNPAQPHS PARGTIELGR ILEPGYLGSG QWDMMRPQKG
SISGELSSGS SMYQLNSKPT GADLLEEHLG EIRNLRQRLE ESICVNDRLR EQLQHRLSST
ARENGSTSHF YSQGLESMPQ LYNENRALRE ENQSLQTRLS HASRGHSQEV DHLREALLSS
SSQLQELEKE LEQQKAERRQ LLEDLQEKQD EIVHFREERL SLQENNSRLQ HKLALLQQQC
EEKQQLSLSL QSELQIYESL YENPKKGLKA FSLDSCYQVP GELSCLVAEI RALRVQLEQS
IQVNNRLRLQ LEQQMDHGAG KASLSSCPVN QSFSAKAELA NQQPPFQGSA ASPPVRDVGL
NSPPVVLPSN SCSVPGSDSA IISRTNNGSD ESAATKTPPK MEVDAADGPF ASGHGRHVIG
HVDDYDALQQ QIGEGKLLIQ KILSLTRPAR SVPALDAQGT EAPGTKSVHE LRSSARALNH
SLEESASLLT MFWRAALPNS HGSVLVGEEG NLMEKELLDL RAQVSQQQQL LQSTAVRLKT
ANQRKKSMEQ FIVSHLTRTH DVLKKARTNL EMKSFRALMC TPAL
