LOCUS       NP_599162               2626 aa            linear   ROD 03-APR-2024
DEFINITION  unconventional myosin-IXa [Rattus norvegicus].
ACCESSION   NP_599162
VERSION     NP_599162.2
DBSOURCE    REFSEQ: accession NM_134335.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2626)
  AUTHORS   O'Connor,E., Topf,A., Muller,J.S., Cox,D., Evangelista,T.,
            Colomer,J., Abicht,A., Senderek,J., Hasselmann,O., Yaramis,A.,
            Laval,S.H. and Lochmuller,H.
  TITLE     Identification of mutations in the MYO9A gene in patients with
            congenital myasthenic syndrome
  JOURNAL   Brain 139 (Pt 8), 2143-2153 (2016)
   PUBMED   27259756
REFERENCE   2  (residues 1 to 2626)
  AUTHORS   Folci,A., Murru,L., Vezzoli,E., Ponzoni,L., Gerosa,L., Moretto,E.,
            Longo,F., Zapata,J., Braida,D., Pistillo,F., Bahler,M.,
            Francolini,M., Sala,M. and Bassani,S.
  TITLE     Myosin IXa Binds AMPAR and Regulates Synaptic Structure, LTP, and
            Cognitive Function
  JOURNAL   Front Mol Neurosci 9, 1 (2016)
   PUBMED   26834556
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2626)
  AUTHORS   Elbediwy,A., Zihni,C., Terry,S.J., Clark,P., Matter,K. and
            Balda,M.S.
  TITLE     Epithelial junction formation requires confinement of Cdc42
            activity by a novel SH3BP1 complex
  JOURNAL   J Cell Biol 198 (4), 677-693 (2012)
   PUBMED   22891260
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 10, 2021 this sequence version replaced NP_599162.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ001713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2626
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..2626
                     /product="unconventional myosin-IXa"
                     /note="myosin-IXa; unconventional myosin-9a"
                     /calculated_mol_wt=301297
     Region          15..110
                     /region_name="RA_Myosin-IXa"
                     /note="Ras-associating (RA) domain found in Myosin-IXa;
                     cd17216"
                     /db_xref="CDD:340736"
     Region          160..1005
                     /region_name="MYSc_Myo9"
                     /note="class IX myosin, motor domain; cd01385"
                     /db_xref="CDD:276836"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            order(187..195,239..246,285..295,537..542)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276836"
     Site            187..195
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276836"
     Site            239..246
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276836"
     Site            285..295
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276836"
     Site            480
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:276836"
     Site            537..542
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276836"
     Site            order(566..577,580..589)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276836"
     Site            755
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          908..919
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            941..950
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276836"
     Site            order(953..980,984..1005)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276836"
     Region          1022..1163
                     /region_name="Neck or regulatory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1115..1137
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          1164..2589
                     /region_name="Tail. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1221..1276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            1243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C170; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            1245
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8C170; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            1259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            1300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RTY4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RTY4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1360..1397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1562..1602
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1618..1673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1689..1726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1765..1784
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          1872..1907
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            2016
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          2063..2120
                     /region_name="C1_Myosin-IXa"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in unconventional myosin-IXa and similar proteins;
                     cd20883"
                     /db_xref="CDD:410433"
     Region          2129..2314
                     /region_name="RhoGAP_myosin_IXA"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in myosins IXA. Class IX
                     myosins contain a characteristic head domain, a neck
                     domain and a tail domain which contains a C6H2-zinc
                     binding motif and a Rho-GAP domain. Class...; cd04406"
                     /db_xref="CDD:239871"
     Site            order(2166,2203,2207,2276,2279..2280,2305)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239871"
     Site            2166
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239871"
     Region          2365..2385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            2380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RTY4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          2449..2527
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Site            2542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B2RTY4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     Region          2552..2614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1N3.1)"
     CDS             1..2626
                     /gene="Myo9a"
                     /gene_synonym="myr 7"
                     /coded_by="NM_134335.2:404..8284"
                     /db_xref="GeneID:171296"
                     /db_xref="RGD:621395"
ORIGIN      
        1 mnvsdggrrr fednehtlri ypgtisegti ycpiparkns taaevidsli nrlhldktkc
       61 yvlaevkefg geewilnptd cpvqrmmlwp rmalenrlsg edyrfllrek nldgsihygs
      121 lqswlrvtee rrrmmergfl pqpqqkdfdd lcslpdlnek tllenlrnrf khekiytyvg
      181 siliainpfk flpiynpkyv kmydnhqlgk lephiyavad vayhamlqrk knqcivisge
      241 sgsgktqstn flihhltals qkgfasgveq iilgagpvle afgnaktahn nnssrfgkfi
      301 qvnyqetgtv lgayvekyll eksrlvyqeh nernyhvfyy llagaseeer lafhlkqpee
      361 yhflnqitkk plrqswddyc ydsepdcftv egedlrhdfe rlqlamemvg flpktrrqif
      421 sllsailhlg nisykkktyr ddsidicnpe vlpivselle vkeemlfeal vtrktvtvge
      481 klilpyklae avtvrnsmak slysalfdwi vfrinhalln skdlekdtkt lsigvldifg
      541 fedyennsfe qfcinfaner lqhyfnqhif kleqeeyrte giswhnidyi dntccinlis
      601 kkptgllhll deesnfpqat nqtlldkfkh qheensyief pavmepafii khyagkvkyg
      661 vkdfrekntd hmrpdivall rssrnafvsg mtgidpvavf rwavlraffr avvafreagk
      721 rhiqrksghd dttpctilks mdsfsflqhp vhqrsleilq rckeekysit rknprtplsd
      781 lqgmntlnek nqhdtfdiaw nvrtgirqsr lptnntslld kdgifansas skllerahgi
      841 ltrnknfrsk pvlpkhllev nslkhltrlt lqdritksll hlhkkkkpps isaqfqvsls
      901 klmetldqae pyfvkcirsn aeklplrfsd alvlrqlryt gmletvrirq sgysskysfq
      961 dfvshfhvll pqhiipskfn iqdffrkini npdnyqvgkt mvflkeherq hlqdllhqev
     1021 lrriillqrw frvllsrqqf lhlrqasvii qrfwrnylnq kqvrnaavek dafimasaas
     1081 llqaswrahl erqrylelra aaviiqqrwr elcrrrhraa tciqsrwrgy rqskkykeqr
     1141 nkiillqsiy rgfrarqryk alkeerlket klehglaqik tcgpleiqgs dpsewedrsf
     1201 anrvkaieec ksviesnris ressmdfske spdkqqergr sqsgtdlqgd vivrqrpksl
     1261 edlhqkkvgr akresrrmre leqaifslel lkvrslggms pseerrwste lmpeglqspq
     1321 gtpdsessqg slelltcden qkskpeslil ddgelkissp stftnpkfds qnnalsasse
     1381 tsstfsgkga ssdsehlkng taeeklvyss qpitcksqlr dsfvssslpt ffyiphqepl
     1441 ktssqldtsi qrnklperet tlkttltldi nrearkcqfs gqvtplnpds sctvlkklek
     1501 lniekekrqk qlqqqnekem meqirqqtdi lekerkafkt ieqsrteasl lapsfyqsrq
     1561 kverpsslhi qntpskgeag vlgspsalat kdspsihlpp kdrpvtlffe rkgspcqsrt
     1621 vkeltkterm gtqhdaacrl snnrntereh fksthsyshr sddpsregss rpifftpkdn
     1681 vitplvhsgn pqvhkqdepa wksklagpgq revarpahkk karmartrsd fltrgtfadg
     1741 egdteeddyd diiepllsld qashselgpv sslgqashsd semtsqrfss vdeqarlhka
     1801 msqgeitkla grqkssdldi rpqrakmrfw akgkqgekkt trvkpapqse vsslfagsdv
     1861 tpvhpfsdel tqyhptppls pelpgscrke fkenkepspk akrkrgvkis svaldsmhwq
     1921 ndsvqiiasa ndlksmdefl lkkmndldne dskkdtlvdv vfkkalkefr qnifssyssa
     1981 lamddgksir ykdlyalfeq ilektmrfeq rdwnespvrv wvntfkvfld eymnefktld
     2041 stapkvlkte rkkrrkketd lveehnghmf katqysipty ceycssliwi mdrasvcklc
     2101 kyachkkccl kttakcskky dpelssrqfg velsrltsed ravplvvekl inyiemhgly
     2161 tegiyrksgs tnkikelrqg ldtdaesvnl ddynihvias vfkqwlrdlp nplmtfelye
     2221 eflramglqe rketirgvys vidqlsrthl stlerlifhl vrialqedtn rmsanalaiv
     2281 fapcilrcpd ttdplqsvqd isktttcvel ivveqmnkyk arlkdissle faenkaktrl
     2341 slirrsmkpv liavrfmsit rssvsgkgrl hrgshpnpss pvivrlpsms dvpeetltse
     2401 tamdtdvtdq qqaamqqeek vlteqienlq kekeeltfem lvleprasdd ealeseasig
     2461 tadslenlnm dpeerslals slkaagksep sskfrkqlrk qpdsldsvss svssclsntt
     2521 sshgtrkrfq iyskspfyra asaceaqgme gplgqaksle drpqfisrgt fnpekgkqkl
     2581 knvknspqkt ketpegtvss grkktvdsdc sstqqlplfg nnefmv
//
