MYOME_MOUSE
ID MYOME_MOUSE Reviewed; 2224 AA.
AC Q80YT7; C4IXU1; Q05CH5; Q80U00; Q8K240;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Myomegalin;
DE AltName: Full=Phosphodiesterase 4D-interacting protein;
GN Name=Pde4dip; Synonyms=Kiaa0454;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as an anchor sequestering components of the cAMP-
CC dependent pathway to Golgi and/or centrosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q9WUJ3}.
CC -!- FUNCTION: [Isoform 2]: Participates in microtubule dynamics, promoting
CC microtubule assembly. Depending upon the cell context, may act at the
CC level of the Golgi apparatus or that of the centrosome. In complex with
CC 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.
CC {ECO:0000250|UniProtKB:Q5VU43}.
CC -!- SUBUNIT: Interacts with PDE4D (By similarity). Isoform 2 interacts with
CC MAPRE1 and MAPRE3. Isoform 2 forms a pericentrosomal complex with
CC AKAP9, CDK5RAP2 and EB1/MAPRE1; within this complex, may mediate
CC MAPRE1-binding to CDK5RAP2. Interaction with AKAP9 stabilizes both
CC proteins. Isoform 2 interacts (via N-terminus) with CAMSAP2; this
CC interaction is much stronger in the presence of AKAP9. In complex with
CC AKAP9, Isoform 2 recruits CAMSAP2 to the Golgi apparatus. Isoform 2
CC interacts with unglycosylated LGALS3BP; this interaction may connect
CC the pericentrosomal complex to the gamma-tubulin ring complex (gamma-
CC TuRC) to promote microtubule assembly and acetylation (By similarity).
CC {ECO:0000250|UniProtKB:Q5VU43, ECO:0000250|UniProtKB:Q9WUJ3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q5VU43}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5VU43}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q5VU43}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YT7-1; Sequence=Displayed;
CC Name=2; Synonyms=Myomegalin variant 8, MMG, MMG8, Short myomegalin-like
CC EB1 binding protein, SMYLE;
CC IsoId=Q80YT7-2; Sequence=VSP_028784, VSP_028785, VSP_028786;
CC -!- DOMAIN: [Isoform 2]: Residues 1-150 are involved in AKAP9-binding.
CC {ECO:0000250|UniProtKB:Q5VU43}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25653.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC65568.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122286; BAC65568.1; ALT_INIT; mRNA.
DR EMBL; AC130541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025653; AAH25653.1; ALT_SEQ; mRNA.
DR EMBL; BC034266; AAH34266.1; -; mRNA.
DR EMBL; BC050783; AAH50783.1; -; mRNA.
DR EMBL; BC141172; AAI41173.1; -; mRNA.
DR CCDS; CCDS38562.1; -. [Q80YT7-2]
DR RefSeq; NP_001034465.2; NM_001039376.2.
DR RefSeq; NP_835181.2; NM_178080.4. [Q80YT7-2]
DR AlphaFoldDB; Q80YT7; -.
DR SMR; Q80YT7; -.
DR BioGRID; 219963; 185.
DR IntAct; Q80YT7; 179.
DR MINT; Q80YT7; -.
DR STRING; 10090.ENSMUSP00000040905; -.
DR iPTMnet; Q80YT7; -.
DR PhosphoSitePlus; Q80YT7; -.
DR EPD; Q80YT7; -.
DR MaxQB; Q80YT7; -.
DR PaxDb; Q80YT7; -.
DR PRIDE; Q80YT7; -.
DR ProteomicsDB; 287595; -. [Q80YT7-1]
DR ProteomicsDB; 287596; -. [Q80YT7-2]
DR Antibodypedia; 2152; 128 antibodies from 23 providers.
DR DNASU; 83679; -.
DR Ensembl; ENSMUST00000045243; ENSMUSP00000040905; ENSMUSG00000038170. [Q80YT7-2]
DR GeneID; 83679; -.
DR KEGG; mmu:83679; -.
DR UCSC; uc008qpg.1; mouse. [Q80YT7-2]
DR CTD; 9659; -.
DR MGI; MGI:1891434; Pde4dip.
DR VEuPathDB; HostDB:ENSMUSG00000038170; -.
DR eggNOG; ENOG502QPV2; Eukaryota.
DR GeneTree; ENSGT00950000183190; -.
DR HOGENOM; CLU_302801_0_0_1; -.
DR InParanoid; Q80YT7; -.
DR OrthoDB; 15127at2759; -.
DR PhylomeDB; Q80YT7; -.
DR TreeFam; TF329233; -.
DR BioGRID-ORCS; 83679; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Pde4dip; mouse.
DR PRO; PR:Q80YT7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80YT7; protein.
DR Bgee; ENSMUSG00000038170; Expressed in hindlimb stylopod muscle and 243 other tissues.
DR ExpressionAtlas; Q80YT7; baseline and differential.
DR Genevisible; Q80YT7; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:1903754; C:cortical microtubule plus-end; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
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 Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..2224
FT /note="Myomegalin"
FT /id="PRO_0000307691"
FT DOMAIN 1497..1588
FT /note="Olduvai"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00647"
FT REGION 206..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..97
FT /evidence="ECO:0000255"
FT COILED 162..205
FT /evidence="ECO:0000255"
FT COILED 236..318
FT /evidence="ECO:0000255"
FT COILED 350..682
FT /evidence="ECO:0000255"
FT COILED 745..822
FT /evidence="ECO:0000255"
FT COILED 856..886
FT /evidence="ECO:0000255"
FT COILED 949..986
FT /evidence="ECO:0000255"
FT COILED 1159..1187
FT /evidence="ECO:0000255"
FT COILED 1295..1331
FT /evidence="ECO:0000255"
FT COILED 1377..1401
FT /evidence="ECO:0000255"
FT COILED 1769..1958
FT /evidence="ECO:0000255"
FT COILED 2148..2191
FT /evidence="ECO:0000255"
FT COMPBIAS 703..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 705
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VU43"
FT VAR_SEQ 1..211
FT /note="MSNGYRTLSQHLNDLKKENFSLKLRIYFLEERMQQKYEVSREDVYKRNIELK
FT VEVESLKRELQDRKQHLDKTWADAEDLNSQNEAELRRQVEERQQETEHVYELLGNKIQL
FT LQEEPRLAKNEATEMETLVEAEKRCNLELSERWTNAAKNREDAAGDQEKPDQYSEALAQ
FT RDRRIEELRQSLAAQEGLVEQLSQEKRQLLHLLEEPASMEV -> MKEICRICARELCG
FT NQRRWIFHTASKLNLQVLLSHVLGKDVSRDGKAEFACSKCAFMLDRIYRFDTVIARIEA
FT LSLERLQKLLLEKDRLKFCIASMYRKNNDDSGEENKAGSGTVDISGLPDMRYAALLQED
FT FAYSGFECWVENEDQINDSHSCHASEGPGNRPRRCRGCAALRVADSDYEAICKVPRKVA
FT RSISYAPSSRWSTSICTEEPALSEVGPPDLASTKVPPDGESMEEGTPGSSVESLDASVQ
FT ASPPQQKDEETERSAKELVKCDYCSDEQAPQHLCNHKLELALSMIKGLDYKPIQSPRGS
FT KLPIPVKSILPGAKPGHILTNGVSSSFLNRPLKPLYRTPVSYPWEISDGQELWDDLCDE
FT YLPIGF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028784"
FT VAR_SEQ 950..955
FT /note="QEMLHL -> RHKHAF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028785"
FT VAR_SEQ 956..2224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028786"
FT CONFLICT 695
FT /note="T -> A (in Ref. 3; AAI41173)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="M -> V (in Ref. 3; AAI41173)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="G -> R (in Ref. 3; AAI41173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2224 AA; 250631 MW; D3EA6F593ACD2445 CRC64;
MSNGYRTLSQ HLNDLKKENF SLKLRIYFLE ERMQQKYEVS REDVYKRNIE LKVEVESLKR
ELQDRKQHLD KTWADAEDLN SQNEAELRRQ VEERQQETEH VYELLGNKIQ LLQEEPRLAK
NEATEMETLV EAEKRCNLEL SERWTNAAKN REDAAGDQEK PDQYSEALAQ RDRRIEELRQ
SLAAQEGLVE QLSQEKRQLL HLLEEPASME VQPVPKGLPT QQKPDLHETP TTQPPVSESH
LAELQDKIQQ TEATNKILQE KLNDLSCELK SAQESSQKQD TTIQSLKEML KSRESETEEL
YQVIEGQNDT MAKLREMLHQ SQLGQLHSSE GIAPAQQQVA LLDLQSALFC SQLEIQRLQR
LVRQKERQLA DGKRCVQLVE AAAQEREHQK EAAWKHNQEL RKALQHLQGE LHSKSQQLHV
LEAEKYNEIR TQGQNIQHLS HSLSHKEQLI QELQELLQYR DNADKTLDTN EVFLEKLRQR
IQDRAVALER VIDEKFSALE EKDKELRQLR LAVRDRDHDL ERLRCVLSAN EATMQSMESL
LRARGLEVEQ LTATCQNLQW LKEELETKFG HWQKEQESII QQLQTSLHDR NKEVEDLSAT
LLCKLGPGQS EVAEELCQRL QRKERMLQDL LSDRNKQAVE HEMEIQGLLQ SMGTREQERQ
AAAEKMVQAF MERNSELQAL RQYLGGKELM TSSQTFISNQ PAGVTSIGPH HGEQTDQGSM
QMPSRDDSTS LTAREEASIP RSTLGDSDTV AGLEKELSNA KEELELMAKK ERESQMELSA
LQSMMAMQEE ELQVQAADLE SLTRNVQIKE DLIKDLQMQL VDPEDIPAME RLTQEVLLLR
EKVASVEPQG QEVSGNKRQQ LLLMLEGLVD ERSRLNEALQ AERQLYSSLV KFHAQPENSE
RDGTLQVELE GAQVLRTRLE EVLGRSLERL SRLESLAAIG GGELESVQAQ EMLHLRAEIH
QHLEEKRKAE VELKELKAQI EEAGFSSVSH ISRNTMLSLC LENAELKEQM GEAMSDGWEV
EEDKEKGEVM LETVVAKGCL NENSLQAEFR KVQGKLKSAY NIINLLKEQL LLRSSEGNSK
EMPELLVRLA REVDRMNTGL PSLGKHQHQE QENTTTARPG SRPQSLPLGA ALSVDGYQLE
NKSQAQDSGH QPEFSLPGST KHLRSQLAQC RQRYQDLQEK LLISEATVFA QANQLEKYRA
VFSESLVKQD SKQIQVDLQD LGYETCGRSE NEAEREETTS PECEEHNNLR PVVLMEGLCS
EQGYLDPVLV SPPAKKPLEN KPGKQEEFRA HGTPDDSSLL RKDIRDLKAQ LQNANKVIQN
LRSRVRSLSA TSDYSSSLER PRKLRAVATL EGASPHSVTD EDEGWLSDGT GAFYPPGLQA
KKDLESLIQR VSQLEAQLPK TGLEGKLAEE LRCASWPGKY DSLIQDQARE LSYLRQKIRE
GRGICYLLTQ HAKDTVKSFE DLLRSNDIDY YLGQSFREQL AQGGQLTERL TSKLSTKDHK
SEKEEAGLEP LALRLSRELQ EKEKVIEVLQ AKLDTRSLSP PSSHAVSDSH RSASTTSFLS
DDIEACSDMD VASEYTHYDE KKPSPSHSAA SASQGLKGES SSSPISLPTP QNPPKEASQA
HPGFHFHSIP KPASLSQTPM HSALPSFVPF SPSGPPLLGC CETPMVSLAE AQQELQMLQK
QLGESVSIAP PASTSTLLSN QTEASSPHYI NPAQPHTPTR STIELGRILE PGYLGSSGQW
DMMRPQKGSV SGELSSGSSM YQLNSKPTGA DLLEEHLGEI RNLRQRLEES ICVNDRLREQ
LQHRLSSTAR ENGSTSHFYS QGLESMPQLY NENRALREEN QSLQTRLSHA SRGHSQEVDH
LREALLSSRS QLQELEKELE QQKAERQQLS LQSELQIYES LCENPKKALK AFSLDSCHQV
PGELSCLVAE IRALRGQLEQ SIEVNNRLRL QLEQQMDRGA GKASLGPIAV GQSFPDKAEP
ANLHQGSAAS PPVRDVGLNS PAMVLPNSSC SAPGSDHAIV TRTNNELSSD DSAAMKNPPK
LEVDATDGPF ANKHGRHVIG HVDDYDALQQ QIGEGKLLIQ KILSLMRSAR SIPGQEAQDT
EAPGNISAHE LRSSAKALNH ALEESTSLLN MFWRAALPNT HGPVLVGKEG QLMEKELLDL
RAQVSQQEQI LQNTAARLKR ANQRKKSMEQ FIVSHLTRTH DVLKKARTNL EMKSFRALTC
TPAL
