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   27-MAR-2024, entry version 129.
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; 188.
DR   IntAct; Q80YT7; 179.
DR   MINT; Q80YT7; -.
DR   STRING; 10090.ENSMUSP00000088254; -.
DR   iPTMnet; Q80YT7; -.
DR   PhosphoSitePlus; Q80YT7; -.
DR   EPD; Q80YT7; -.
DR   MaxQB; Q80YT7; -.
DR   PaxDb; 10090-ENSMUSP00000040905; -.
DR   ProteomicsDB; 287595; -. [Q80YT7-1]
DR   ProteomicsDB; 287596; -. [Q80YT7-2]
DR   Pumba; Q80YT7; -.
DR   Antibodypedia; 2152; 151 antibodies from 23 providers.
DR   DNASU; 83679; -.
DR   Ensembl; ENSMUST00000045243.15; ENSMUSP00000040905.9; ENSMUSG00000038170.16. [Q80YT7-2]
DR   GeneID; 83679; -.
DR   KEGG; mmu:83679; -.
DR   UCSC; uc008qpg.1; mouse. [Q80YT7-2]
DR   AGR; MGI:1891434; -.
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; 5323352at2759; -.
DR   PhylomeDB; Q80YT7; -.
DR   TreeFam; TF329233; -.
DR   BioGRID-ORCS; 83679; 4 hits in 78 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 245 other cell types or tissues.
DR   ExpressionAtlas; Q80YT7; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
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   PANTHER; PTHR46501; MYOMEGALIN; 1.
DR   PANTHER; PTHR46501:SF2; MYOMEGALIN; 1.
DR   Pfam; PF07989; Cnn_1N; 1.
DR   SMART; SM01148; DUF1220; 1.
DR   PROSITE; PS51316; ODV; 1.
DR   Genevisible; Q80YT7; MM.
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
//