MYO9B_RAT
ID MYO9B_RAT Reviewed; 1980 AA.
AC Q63358;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Unconventional myosin-IXb;
DE AltName: Full=Unconventional myosin-9b;
GN Name=Myo9b; Synonyms=Myr5 {ECO:0000303|PubMed:7882973};
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], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain stem, and Spinal cord;
RX PubMed=7882973; DOI=10.1002/j.1460-2075.1995.tb07048.x;
RA Reinhard J., Scheel A.A., Diekmann D., Hall A., Ruppert C., Baehler M.;
RT "A novel type of myosin implicated in signalling by rho family GTPases.";
RL EMBO J. 14:697-704(1995).
RN [2]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1046; SER-1177; SER-1220;
RP SER-1222; SER-1229; SER-1237; SER-1247; SER-1266; THR-1319; SER-1952 AND
RP SER-1959, 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. Binds actin
CC with high affinity both in the absence and presence of ATP and its
CC mechanochemical activity is inhibited by calcium ions (By similarity).
CC Also acts as a GTPase activator for RHOA (PubMed:7882973). Plays a role
CC in the regulation of cell migration via its role as RHOA GTPase
CC activator. This is regulated by its interaction with the SLIT2 receptor
CC ROBO1; interaction with ROBO1 impairs interaction with RHOA and
CC subsequent activation of RHOA GTPase activity, and thereby leads to
CC increased levels of active, GTP-bound RHOA (By similarity).
CC {ECO:0000250|UniProtKB:Q13459, ECO:0000269|PubMed:7882973}.
CC -!- SUBUNIT: Interacts (via IQ domains) with CALM. Interacts with RHOA.
CC Interacts (via Rho-GAP domain) with ROBO1; this inhibits the
CC interaction with RHOA and the stimulation of RHOA GTPase activity, and
CC thereby increases the levels of active RHOA.
CC {ECO:0000250|UniProtKB:Q13459}.
CC -!- INTERACTION:
CC Q63358; D4A631: Arfgef1; NbExp=4; IntAct=EBI-6251137, EBI-6251168;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q13459}. Note=In undifferentiated cells
CC colocalizes with F-actin in the cell periphery while in differentiated
CC cells its localization is cytoplasmic with the highest levels in the
CC perinuclear region. {ECO:0000250|UniProtKB:Q13459}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, lung, thymus, brain, liver,
CC spleen and heart muscle. Detected in lung, testis, spleen and liver,
CC and at reduced level in different brain regions (at protein level).
CC {ECO:0000269|PubMed:9819351}.
CC -!- DEVELOPMENTAL STAGE: During forebrein development, it is expressed at
CC higher levels in embryonic and early postnatal stages than in the adult
CC forebrain. {ECO:0000269|PubMed:9819351}.
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; X77609; CAA54700.1; -; mRNA.
DR PIR; S54307; S54307.
DR AlphaFoldDB; Q63358; -.
DR SMR; Q63358; -.
DR IntAct; Q63358; 16.
DR STRING; 10116.ENSRNOP00000048368; -.
DR iPTMnet; Q63358; -.
DR PhosphoSitePlus; Q63358; -.
DR jPOST; Q63358; -.
DR PaxDb; Q63358; -.
DR PRIDE; Q63358; -.
DR UCSC; RGD:3146; rat.
DR RGD; 3146; Myo9b.
DR VEuPathDB; HostDB:ENSRNOG00000016256; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_2_2_1; -.
DR InParanoid; Q63358; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q63358; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000016256; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; Q63358; baseline and differential.
DR Genevisible; Q63358; RN.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032433; C:filopodium tip; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0043008; F:ATP-dependent protein binding; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IDA:RGD.
DR GO; GO:0048495; F:Roundabout binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISO:RGD.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
DR GO; GO:0002548; P:monocyte chemotaxis; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:RGD.
DR GO; GO:0035385; P:Roundabout signaling pathway; 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; IPR028557; MYO9B.
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:SF2; PTHR46184:SF2; 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; 4.
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; 3.
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 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Cytoskeleton; GTPase activation; Metal-binding; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT CHAIN 2..1980
FT /note="Unconventional myosin-IXb"
FT /id="PRO_0000123471"
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..954
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 958..978
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 981..1001
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1002..1024
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1025..1054
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1663..1848
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1592..1641
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 715..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..856
FT /note="Actin-binding"
FT REGION 941..1045
FT /note="Neck or regulatory domain"
FT REGION 1046..1980
FT /note="Tail"
FT REGION 1049..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1704
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT REGION 1891..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1841..1861
FT /evidence="ECO:0000255"
FT COILED 1918..1948
FT /evidence="ECO:0000255"
FT COMPBIAS 1094..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1957
FT /note="Basic and acidic 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 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
FT MOD_RES 1649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
FT MOD_RES 1886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1965
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
SQ SEQUENCE 1980 AA; 225037 MW; D79FEC4D0FAE0C05 CRC64;
MSAHEAGSSG RRRPATFHLH IYPQLPSAGS QTSCRVTATK DSTTSDVIRD VVASLHLDGS
KHYVLVEVKE SGGEEWVLDA SDSPVHRVLL WPRRAQKEHP REDGYYFLLQ ERNADGSIQY
LHVQLLAQPT AACRLVERGL LPRPQADFDD LCNLPELNEA NLLQSLKLRF VQQKIYTYAG
SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKH VNQCIVISGE
SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPQD
YFYLNQHNLN IEDGEDLKHD FERLQQAMEM VGFLPATKKQ IFSVLSAILY LGNVTYKKRA
TGRDEGLEVG PPEVLDTLSQ LLKVKRETLV EVLTKRKTIT VNDKLILPYS LSEAITARDS
MAKSLYSALF DWIVLRINHA LLNKKDMEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA
NEQLQYYFTQ HIFKLEQEEY QGEGISWHNI DYTDNVGCIH LISKKPTGLF YLLDEESNFP
HATSHTLLAK FKQQHEDNKY FLGTPVLEPA FIIQHFAGRV KYQIKDFREK NMDYMRPDIV
ALLRGSDSSY VRQLIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAEAGVSSPV
TRSHVEELPR GANTPSEKLY RDLHNQIIKS LKGLPWQGED PRRLLQSLSR LQKPRTFFLK
SKGIKQKQII PKNLLDSKSL RLIISMTLHD RTTKSLLHLH KKKKPPSISA QFQTSLNKLL
EALGKAEPFF IRCIRSNAEK KELCFDDELV LQQLRYTGML ETVRIRRSGY SAKYTFQDFT
EQFQVLLPKD VQPCREAIAA LLEKLQVDRQ NYQIGKTKVF LKETERQALQ ERLHGEVLRR
ILLLQSWFRM VLERRHFVQM KHAALTIQAC WRSYRVRRTL ERTRAAVYLQ AAWRGYLQRQ
AYHHQRHSII RLQSLCRGHL QRRSFSQMML EKQKAEQARE TAGAEMSEGE PSPVAAGEQP
SEHPVEDPES LGVETETWMN SKSPNGLSPK KEIPSPEMET PAQKTVPAES HEKVPSSREK
RESRRQRGLE HVERQNKHIQ SCREENSTLR EPSRKASLET GESFPEDTKE PREDGLETWT
ETAAPSCPKQ VPIVGDPPRS PSPLQRPASL DLDSRVSPVL PSSSLESPQD EDKGENSTKV
QDKPESPSGS TQIQRYQHPD TERLATAVEI WRGKKLASAM LSQSLDLSEK PRTAGAALTP
TEERRISFST SDVSKLSPVK TSTEVDGDLS AKKPAGHKKK SEDPSAGPDA GLPTGSQGDS
KSAFKRLFLH KAKDKKPSLE GVEETEGSGG QAAQEAPARK TLDVPSSQQH RHTTGEKPLK
GKKNRNRKVG QITVSEKWRE SVFRKITNAN ELKFLDEFLL NKVNDLRSQK TPIESLFIEA
TERFRSNIKT MYSVPNGKIH VGYKDLMENY QIVVSNLAAE RGEKDTNLVL NVFQSLLDEF
TRSYNKTDFE PVKGKAQKKK RKQERAVQEH NGHVFASYQV NIPQSCEQCL SYIWLMDKAL
LCSVCKMTCH KKCVHKIQSY CSYTGRRKSE LGAEPGHFGV CVDSLTSDKA SVPIVLEKLL
EHVEMHGLYT EGLYRKSGAA NRTRELRQAL QTDPATVKLE DFPIHAITGV LKQWLRELPE
PLMTFAQYGD FLRAVELPEK QEQLAAIYAV LDHLPEANHT SLERLIFHLV KVALLEDVNR
MSPGALAIIF APCLLRCPDN SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEINHLEA
AESIAFRRLS LLRQNAPWPL KLGFSSPYEG VRTKSPRTPV VQDLEELGAL PEEAAGGDED
REKEILMERI QSIKEEKEDI TYRLPELDPR GSDEENLDSE TSASTESLLE ERAVRGAAEE
