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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
 
 
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