MYO9A_RAT
ID MYO9A_RAT Reviewed; 2626 AA.
AC Q9Z1N3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Unconventional myosin-IXa;
DE AltName: Full=Myr 7;
DE AltName: Full=Unconventional myosin-9a;
GN Name=Myo9a; Synonyms=Myr7;
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, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9819351; DOI=10.1242/jcs.111.24.3597;
RA Chieregatti E., Gaertner A., Stoeffler H.-E., Baehler M.;
RT "Myr 7 is a novel myosin IX-RhoGAP expressed in rat brain.";
RL J. Cell Sci. 111:3597-3608(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; SER-1259 AND SER-2016,
RP AND IDENTIFICATION BY 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 -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements
CC (PubMed:9819351). Regulates Rho by stimulating it's GTPase activity in
CC neurons (PubMed:9819351). Required for the regulation of neurite
CC branching and motor neuron axon guidance (By similarity).
CC {ECO:0000250|UniProtKB:Q8C170, ECO:0000269|PubMed:9819351}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:9819351}. Synapse
CC {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell
CC bodies, dendrites and axons with occasional hints of an enrichment near
CC the plasma membrane. Localized at the neuromuscular junction (By
CC similarity). {ECO:0000250|UniProtKB:Q8C170,
CC ECO:0000269|PubMed:9819351}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, followed by
CC testis and spleen. Expressed at very low levels, in kidney. Detected
CC abundantly in brain and testis and at lower levels in adrenal gland,
CC kidney, lung and spleen (at protein level). In adrenal gland it is
CC mostly found in the medulla but not in the cortex. In brain, it is
CC found in the cerebellum and the CA2-CA3 regions of the hippocampus.
CC {ECO:0000269|PubMed:9819351}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in developing forebrain.
CC This expression decreases slightly in embryonic and early postnatal
CC days. {ECO:0000269|PubMed:9819351}.
CC -!- PTM: Phosphorylated by ALPK1 following monosodium urate monohydrate
CC (MSU)-induced inflammation. {ECO:0000250|UniProtKB:B2RTY4}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-9 (MYH9). {ECO:0000305}.
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DR EMBL; AJ001713; CAA04946.1; -; mRNA.
DR PIR; T31099; T31099.
DR RefSeq; NP_599162.1; NM_134335.1.
DR AlphaFoldDB; Q9Z1N3; -.
DR SMR; Q9Z1N3; -.
DR STRING; 10116.ENSRNOP00000015963; -.
DR iPTMnet; Q9Z1N3; -.
DR PhosphoSitePlus; Q9Z1N3; -.
DR PaxDb; Q9Z1N3; -.
DR PRIDE; Q9Z1N3; -.
DR GeneID; 171296; -.
DR KEGG; rno:171296; -.
DR UCSC; RGD:621395; rat.
DR CTD; 4649; -.
DR RGD; 621395; Myo9a.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR InParanoid; Q9Z1N3; -.
DR OrthoDB; 14881at2759; -.
DR PhylomeDB; Q9Z1N3; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q9Z1N3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028558; MYO9A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; PTHR46184:SF3; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Coiled coil; Cytoplasm; GTPase activation;
KW Membrane; Metal-binding; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..2626
FT /note="Unconventional myosin-IXa"
FT /id="PRO_0000348442"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..112
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..1017
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1021..1041
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1043..1072
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1075..1104
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1116..1145
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1139..1168
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2131..2319
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 2067..2116
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 908..919
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1022..1163
FT /note="Neck or regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 1164..2589
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 1221..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2365..2385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2449..2527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2552..2614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1265..1292
FT /evidence="ECO:0000255"
FT COILED 1493..1540
FT /evidence="ECO:0000255"
FT COILED 2408..2444
FT /evidence="ECO:0000255"
FT COMPBIAS 1221..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1886..1900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2503..2527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2574..2588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2589..2614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C170"
FT MOD_RES 1245
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C170"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 2016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT MOD_RES 2542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
SQ SEQUENCE 2626 AA; 301382 MW; 3F70610271E4D791 CRC64;
MNVSDGGRRR FEDNEHTLRI YPGTISEGTI YCPIPARKNS TAAEVIDSLI NRLHLDKTKC
YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
SILIAINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEEER LAFHLKQPEE
YHFLNQITKK PLRQSWDDYC YDSEPDCFTV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
SLLSAILHLG NISYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEKDTKT LSIGVLDIFG
FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEENSYIEF PAVMEPAFII KHYAGKVKYG
VKDFREKNTD HMRPDIVALL RSSRNAFVSG MTGIDPVAVF RWAVLRAFFR AVVAFREAGK
RHIQRKSGHD DTTPCTILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD
LQGMNTLNEK NQHDTFDIAW NVRTGIRQSR LPTNNTSLLD KDGIFANSAS SKLLERAHGI
LTRNKNFRSK PVLPKHLLEV NSLKHLTRLT LQDRITKSLL HLHKKKKPPS ISAQFQVSLS
KLMETLDQAE PYFVKCIRSN AEKLPLRFSD ALVLRQLRYT GMLETVRIRQ SGYSSKYSFQ
DFVSHFHVLL PQHIIPSKFN IQDFFRKINI NPDNYQVGKT MVFLKEHERQ HLQDLLHQEV
LRRIILLQRW FRVLLSRQQF LHLRQASVII QRFWRNYLNQ KQVRNAAVEK DAFIMASAAS
LLQASWRAHL ERQRYLELRA AAVIIQQRWR ELCRRRHRAA TCIQSRWRGY RQSKKYKEQR
NKIILLQSIY RGFRARQRYK ALKEERLKET KLEHGLAQIK TCGPLEIQGS DPSEWEDRSF
ANRVKAIEEC KSVIESNRIS RESSMDFSKE SPDKQQERGR SQSGTDLQGD VIVRQRPKSL
EDLHQKKVGR AKRESRRMRE LEQAIFSLEL LKVRSLGGMS PSEERRWSTE LMPEGLQSPQ
GTPDSESSQG SLELLTCDEN QKSKPESLIL DDGELKISSP STFTNPKFDS QNNALSASSE
TSSTFSGKGA SSDSEHLKNG TAEEKLVYSS QPITCKSQLR DSFVSSSLPT FFYIPHQEPL
KTSSQLDTSI QRNKLPERET TLKTTLTLDI NREARKCQFS GQVTPLNPDS SCTVLKKLEK
LNIEKEKRQK QLQQQNEKEM MEQIRQQTDI LEKERKAFKT IEQSRTEASL LAPSFYQSRQ
KVERPSSLHI QNTPSKGEAG VLGSPSALAT KDSPSIHLPP KDRPVTLFFE RKGSPCQSRT
VKELTKTERM GTQHDAACRL SNNHNTEREH FKSTHSYSHR SDDPSREGSS RPIFFTPKDN
VITPLVHSGN PQVHKQDEPA WKSKLAGPGQ REVARPAHKK KARMARTRSD FLTRGTFADG
EGDTEEDDYD DIIEPLLSLD QASHSELGPV SSLGQASHSD SEMTSQRFSS VDEQARLHKA
MSQGEITKLA GRQKSSDLDI RPQRAKMRFW AKGKQGEKKT TRVKPAPQSE VSSLFAGSDV
TPVHPFSDEL TQYHPTPPLS PELPGSCRKE FKENKEPSPK AKRKRGVKIS SVALDSMHWQ
NDSVQIIASA NDLKSMDEFL LKKMNDLDNE DSKKDTLVDV VFKKALKEFR QNIFSSYSSA
LAMDDGKSIR YKDLYALFEQ ILEKTMRFEQ RDWNESPVRV WVNTFKVFLD EYMNEFKTLD
STAPKVLKTE RKKRRKKETD LVEEHNGHMF KATQYSIPTY CEYCSSLIWI MDRASVCKLC
KYACHKKCCL KTTAKCSKKY DPELSSRQFG VELSRLTSED RAVPLVVEKL INYIEMHGLY
TEGIYRKSGS TNKIKELRQG LDTDAESVNL DDYNIHVIAS VFKQWLRDLP NPLMTFELYE
EFLRAMGLQE RKETIRGVYS VIDQLSRTHL STLERLIFHL VRIALQEDTN RMSANALAIV
FAPCILRCPD TTDPLQSVQD ISKTTTCVEL IVVEQMNKYK ARLKDISSLE FAENKAKTRL
SLIRRSMKPV LIAVRFMSIT RSSVSGKGRL HRGSHPNPSS PVIVRLPSMS DVPEETLTSE
TAMDTDVTDQ QQAAMQQEEK VLTEQIENLQ KEKEELTFEM LVLEPRASDD EALESEASIG
TADSSENLNM DPEERSLALS SLKAAGKSEP SSKFRKQLRK QPDSLDSVSS SVSSCLSNTT
SSHGTRKRFQ IYSKSPFYRA ASACEAQGME GPLGQAKSLE DRPQFISRGT FNPEKGKQKL
KNVKNSPQKT KETPEGTVSS GRKKTVDSDC SSTQQLPLFG NNEFMV
