ID A0A3Q7RI97_VULVU Unreviewed; 2166 AA.
AC A0A3Q7RI97;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Unconventional myosin-IXb isoform X1 {ECO:0000313|RefSeq:XP_025845472.1};
GN Name=MYO9B {ECO:0000313|RefSeq:XP_025845472.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025845472.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025845472.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025845472.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025845472.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_025845472.1; XM_025989687.1.
DR STRING; 9627.ENSVVUP00000022193; -.
DR KEGG; vvp:112913119; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR GO; GO:0030048; P:actin filament-based movement; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd20884; C1_Myosin-IXb; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd04407; RhoGAP_myosin_IXB; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
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; IPR028557; RhoGAP_myosin_IXB.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 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; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 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 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 146..959
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1638..1687
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1709..1894
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 714..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..863
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1052..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1943..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2146
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:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2166 AA; 244637 MW; 14F51DE098CB8E0E CRC64;
MSVNEAGSSG RGGQAAYHLH IYPQLATSQS RASCRVTATK DSTTSDVIQD AIASLQLDGT
KCYVLVEVKE TGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY
VHMQLVSQAT ATRRLVERGL LPRQEADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG
SILVAVNPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYAMLRKR VNQCIVISGE
SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPED
YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ IFSVLSAILY LGNVTYKKRA
TGRDEGLEVG PPEVLDTLSQ LLKVKREILV EVLTKRKTVT ANDKLILPYS LSEAITARDS
MAKSLYSALF DWIVLRINHA LLNKKDMEES VSCLSIGVLD IFGFEDFERN SFEQFCINYA
NEQLQYYFNQ HIFKLEQEEY QSEGISWHNI DYTDNVGCIH LISKKPTGLF YLLDEESNFP
HATSQTLLAK FKQQHEDNRY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV
ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE AGQLRAERAE KAAAGMGSPG
THGHLGDLQR GASTPSEKLY RAREQRDLHD QIIKTIKGLP WQGEDPRRLL QSLSRLQKPR
TFILKSKGIK QKQLIPKNLL DSKSLKLIIS MTLHDRTTKS LLHLHKKKKP PSISAQFQTS
LNKLLEALGK AEPFFIRCIR SNAEKKELCF DEELVLQQLR YTGMLETVRI RRSGYSAKYT
FQDFTEQFQV LLPKNAQPCR EVISALLEKM DVDKRNYQIG KTKVFLKETE RQALQETLHR
EVVRKILLLQ SWFRMVLERR HFLQMRQAAI TIQACWRSYR VRRALERTQA AVYIQAAWRG
YKQRMAYRRR RQSIIRLQSL CRGHLQRKSF SQMVAEKQKA GEEKEAQQAL REETAEGGPG
QAAKQEQVPR QDPEPSEDGE HLALEPEVWP NDEPLAESSQ PEKEVPSPEK ALLPQKNAAE
SHEKVPSSRE KRESRRQRGL EHVKLQNKHI QSCKEESALR EPSERTLPEQ EESLLEDKKE
NREDETPSDL GTETENASKK QPEEPLQAMP ASQLSGETLK MPQGGDPTPG HVERPTSLAL
DSTVSVPTPS TTPETPKDKS KLGGDLRAQD RPESPGSSTQ IQRYRDPDSE RLASAVELWR
GKKLMTAASS TMLSQSLDLS ERHRAVGAAL TPTEDRRISL STSDVSKLLP SPSQTKIQPS
TETVDGEPSS KKLAVQKKKS GDTSAGTDSG LSPGAQADSK STFKRLFLHK NKDKKSSLEG
VEETENTVPG HTMLEAATTK KNLEASSHQH RHPAGEKHAK EPGGKGKKNR NLKIGKITVS
EKWRESVFRK ITNANELKYL DEFLLNKIND LRSQKTPTES LFIEATEKFR SNLKTMYSVP
NGKIHVGYKD LMENYQIVVN NLAAERGEKD TNLVLNLFQS LLDEFTRGHT KNDFEPPKQS
KAQKKKRKQD RAAQHHNGHV FVSYQVSIPQ SCEQCLSYIW LMDKALLCSV CKMTCHKKCV
HKIQTYCSYT CGRKSEPGAE PGHFGVCVDS LTSDKASVPI VLEKLLEHVE MHGLYTEGLY
RKSGAANRTR ELRQALQTDP AAVKLENFPI HAITGVLKQW LRELPEPLMT FAQYGDFLRA
VELPEKQEQL AAIYAVLEHL PEANHNSLER LIFHLVKVAL LEDVNRMSPS ALAIIFAPCL
LRCPDNSDPL TSMKDVLKVT TCVEMLIKEQ MRKYKVKMEE INQLEAAESI AFRRLSLLRQ
NAPWPLKLGF SSPYEGVLIK SPKARGSSAG SLEELGVLPE EEVPSGDEDR EKEILIERIQ
SIKEEKEDIT YRLPELDPRG SDEENLDSET SASTESLLEE RAGRGASEGP PAPALPSPGA
PALSPLPVAA APPRRRPSSF VTVRVKTPRR TPIMPTTNIK LPPGLPSHLP GRAPGAQEAA
APVRRREPPA RRPDQVHSVY ITPSTHLPVQ GIREPLDEDS RLPGAKRRYS DPPTYCLPPT
SGQANG
//
