ID H2TZM5_TAKRU Unreviewed; 2111 AA.
AC H2TZM5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSTRUP00000030134.3};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSTRUP00000030134.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000030134.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000030134.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000030134.3}
RP IDENTIFICATION.
RG Ensembl;
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 Ensembl; ENSTRUT00000030251.3; ENSTRUP00000030134.3; ENSTRUG00000011915.3.
DR GeneTree; ENSGT00940000156845; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR Proteomes; UP000005226; Chromosome 20.
DR GO; GO:0016020; C:membrane; 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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd20884; C1_Myosin-IXb; 1.
DR CDD; cd01385; MYSc_Myo9; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 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; 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 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000005226};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..130
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 162..997
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1740..1789
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1808..1996
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..900
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1081..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2064..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2111 AA; 240678 MW; 3349AC283A1382A8 CRC64;
MSVRDGAATV VTSVAGGGGG GRPASPNNHD GRSYLLQIYP RLAAQPTSCC SLRVHKDATA
ASVISDAAAV LGLDPGRMYV LAEVKESGGE EWVLEPGDLP AQRFLLWPRK AQEQHPQSLG
FYFLLQERNH DGTIHYVHLP SVAKEQEAQQ LTARGFLPPP QDDFADLCNL PVLNEDSILN
NLRTRFCKKK IYTYAGSILI AINPFMFLPI YNPKYVKMYE NHQLGKLEPH IFAIADVAYY
AMLRKKVNQC IVISGESGSG KTQSTNFLIH CLTALSQKGY ASGVERTILG AGPVLEAFGN
AKTAHNNNSS RFGKFIQVNY LESGVVRGAV VEKYLLEKSR LVSREKNERN YHVFYYLLFG
ASEEERKEFK LLPLEEYSYL KQQNFRIEDE EDLCHDFERL QQAMEMVGFL SATKKQIFSV
LSAILYLGNV TYKTKSNGRE EGLEVGPPEV LARLSELLKV KEELLVEALT KRKTVTVNDK
LILPYSHPEA ITARDSMAKS LYSALFDWIV LRINHALLNK KDMEESIPCL SIGVLDIFGF
EDFETNSFEQ FCINYANEQL QYYFNHHIFN LEQEEYQAEG ITWHNIDYTD NVGCIHLISK
KPTGLLYLLD EESNFPHATD ETLLAKIKQQ HQGNKYFVPT PVMEPAFVIQ HFAGRVKYQV
KDFREKNTDH MRSDIVALLR SSDSAYVRQL IGMDPVAMFR WGILRATIRG LAAFNEAGRA
RAAKTSGVVR PASRTPLGEL KQSNAPVDRM YKRVSMLDFY FDHSEERPLE AFEDIFASYE
NKKHMHAEII SSIKNLQLDG EDPRKLLQSW GRLRFPRHVL QKQKNAKHRQ AIPKSLLDSR
SLKFIVGLTL HDRTTKSLLH LHKKKKPPSI SAQFQTSLTK LLETLNRAEP FFIRCIRSNA
QKKEMYLDEV LVIQQLRYTG MLETVRIRRS GYGAKYTFQE FVNQFRVLLP KDTKSFKEDI
SELLEKKMGL DPATYQIGKT KVFLKELERQ KLQDTLHKDV MRKIIFLQRW FRAHLQRKEF
LDMRQAAILI QSSWRRYLKE EQKRRAATLI QAVWRGHWQR SENHRKKQVA TKIQALYRGH
SARKRCQSLR GEKRRKEEEE KEARKRAEEE EKRRREEEEE ARRQAEEEEE RRRIEDEKAR
IKAEEEEAKR QAEREEIARM AEEAENKLVK EPQTREDPDI ELITEEMLDD NLTAPETEEE
VNTSSHREDE GVKGEKLDDM EMDLELNGTL AEAGPQLEER DGEDDLENHT PAESDSTSVL
SSDGIFTLQP STTGEEMDKK SLDDTSVCSD ADQNRAKPSA VNKGQLSRSQ EKREQRRRRG
LEHNQRETER ASSSAGSKDD TSSLKSKTQA TRLKERAESK ELDQYTFVAW KMKEDKAAKK
ETKTSPAAGP VRPSTLPLQP VSDRNGVSES TGAVSLQRRP GAIKEKPEKW RGGRRSDGEL
SERTSPQQPH SKEERRRKTP LSETASSSID SLSPGSEGAG ALQLNSPSDS LSESSKGGSF
RRKHQEGSAH QDSTQSIPST PDRSGGVFSK IFKKRPHKEA QTPDNGELTL AQILNERPAG
GEAPTSGHPS RPPSQSQGDR AGKALGRNPT IKISRATRVS EQWNASLDRE ITNANELRHL
DEFLGNQVND FRTRGKSLSA TEAIFVTSTM QFRETIKAMY SLPKPTIGYK GLMTGYQNKV
IHLAGDKQKG EVKLVVNLFQ SVLDGFIRGE MKKEEAEPAK PAKTRKKRRS KDKSMESPLD
HSFTNYQVSI MQSCDQCNSY IWAMEKAYMC TYCKMVCHKK CLCKITADCS TFSAKKCDEE
STGQHFGVRV CHLVNDKSPV PMVLEMMLEH VEMQGLYTEG IYRKSGSANR MKELHQRLET
EPHAVCLEDY PIHTVTGLVK QWLRELPDPL MTFMHYNDFL HAVELPEKQE QLHAVYKVLE
ELPPANFNTL ERLIFHLVRV CKVEDHNRMS PNSLAIVFAP CVLRCPDSAD PLLSMKDVAK
TTICVEMIIN EQIRRYNEKM EEIEQLEYAE ALAVNQLKLK RQNTMHEKAS SDLSVVPENE
PLNPDTEKNL VERIKSIKQE KEDLACRLPE MEQPGSDQEN LDSETSQSSE SLLDELQRSS
VHMSEPDGLD Q
//
