ID H2SH47_TAKRU Unreviewed; 1953 AA.
AC H2SH47;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Myosin-9 {ECO:0000256|ARBA:ARBA00039816};
DE AltName: Full=Myosin heavy chain 9 {ECO:0000256|ARBA:ARBA00041440};
DE AltName: Full=Myosin heavy chain, non-muscle IIa {ECO:0000256|ARBA:ARBA00042289};
DE AltName: Full=Non-muscle myosin heavy chain IIa {ECO:0000256|ARBA:ARBA00043098};
GN Name=LOC777991 {ECO:0000313|Ensembl:ENSTRUP00000011729.3};
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:ENSTRUP00000011729.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000011729.3, 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:ENSTRUP00000011729.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC granule {ECO:0000256|ARBA:ARBA00037865}.
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; ENSTRUT00000011789.3; ENSTRUP00000011729.3; ENSTRUG00000004910.3.
DR GeneTree; ENSGT00940000155632; -.
DR HOGENOM; CLU_000192_4_2_1; -.
DR Proteomes; UP000005226; Chromosome 17.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd14932; MYSc_Myh18; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 2.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF16; MYOSIN-9; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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}.
FT DOMAIN 25..75
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 79..775
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1508..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..1953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1953 AA; 227249 MW; 297FC5E7C74CEFAC CRC64;
MTDADKFLYG DRSGVNNPLA QADWASKKLV WIPSEKLGFE PGSVKEELGD ECMVELTDSG
RKVKVNKDDI QKMNPPKFSK VEDMAELTCL NEASVLHNLK ERYYSGLIYT YSGLFCVVVN
PYKHLPIYSE DIVNMYKGKK RHEMPPHIYA ITDTAYRSMM QDREDQSILC TGESGAGKTE
NTKKVIQYLA YIASSFKSKK DQVSGELEKQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERSFHIFYYL LTGAGDKLRS ELCLEDYSKY
RFLSNGNMTI PGLQDKELFA ETMEAFHIMS IPEEERIGFL KVVSAVLQLG NMTFKKERHS
DQASMPDDTA AQKVCHLLSV NVTDFTRAIL SPRIKVGRDY VQKAQTQEQA EFAVEALAKA
SYERMFRWLV FRINKALDKT KRQGASFIGI LDIAGFEIFE LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQREGIEWS FIDFGLDLQP CIELIDKPAG PPGILALLDE ECWFPKATDK
SFVEKVVQEQ GTHPKFQKPK KLKDDVDFCI IHYAGKVDYK ADEWLMKNMD PLNESVATLL
NQSTDKFTAE LWRDMDHIVG LDKVAGMSDS TYGAFKTRKG MFRTVGQLYK EQLGNLMTTL
RNTNPNFVRC IIPNHEKKAG KLEPHLVLDQ LRCNGVLEGI RICRQGFPNR VVFQEFRQRY
EILTPNAIPK GFMDGKQACV LMIKALELDP NLYRIGQSKV FFRAGVLAHL EEERDMKITD
VIITFQAWCR GYVARKAFTK RQQQLTAMKV IQRNCAAYLK LRNWQWWRLF TKVKPLLQVT
RQEEEMLAKE DELSKVKEKQ LQAEEMIKEF ESKQQQLNAE KMALQEQLQA ETELCAEAEE
MRARLVNRKQ ELEEILHDME SRLEEEEERV NQMLNERKKM QQNIADLEQQ LDEEEADRQK
LQMEKVTTDS KMKALEGNIM VLDDQNNKLN KEKKLLEDRI AEFSSNLSEE EEKSRSLQKL
KNKHEAIITD LEDRLRKEEK QRQELEKNRR KLEGDSTDLH DQIADLQAQI ADLRAQLANK
EEELQNALIR IEEEAAANMA SQKKIKELEA QILELDEDLE REKFYRSKNG QRCKELEKEL
EAIKNKLDDT LDTTAAQQEL RAKRETEVAQ LRKAQEEENK MHESQIAELS KKHLQAFNEM
NEQLEQAKRN KLSVEKAKQA LESEFNELQI ELKTLGQSKS DSEHRRKKAE SQVQELQVKY
GDCERQRQEA VEKIAKLQSE LENVNSLLNE SEGKNTKSSK DMLSLESHLQ DTQELLQEET
RQKLAISTRF RQMEEEQNSL REMLEEEEEA KKNVEKQISV LQGQLGDMKK KMDQEVSSLE
SAEESRKRLQ REFDTVKLQL EEKEAAYEKL ERTKTRLQQE LDDLLVNQDG LRQLVNNMER
KQRKFDQMLA EEKTISTQYA EERDKAEAEA REKETRALTL ARELETITDL KNELERTNKQ
LKAEMEDLVS SKDDAGKNVH ELERSKRATE QQLEEIKTQL EELEDELQAT EDAKLRLEVN
MQAMKAQFDR DLQARDEQGE ERRKQLVKQV HELEAELEDE RRQRSQAVSA KKKLELDLGE
LEVHIDAANK GRDEALKQLK KLQVQFKDMM RESEDLRLSR DEAINSAKET EKKVKTMEAD
AAQFQEDLAT AERLKRQMQA ERDELQDEIN GNNTKKYVAR HEKRRLEARI TQLEEELEEE
QLNSEMANDR NKRTTLQVDQ LTAELSAERS AAQRLEGARS QAERKNKELS LKLQELESTI
KSKYKSSLTA LEAKVAQLEE QLDTEIKERQ QATRMVRRTE KKMKELVLQV EDERRNTEQY
KDQADKLNSR TRQLKRQLEE AEEEVTRANA YRRKLQRELE DANETQDTMN REVNILKSKL
RRDLPFTIRT VNRSGLESDD DVAVPADTEP ATE
//
