ID G9KC60_MUSPF Unreviewed; 1031 AA.
AC G9KC60;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Myosin IC {ECO:0000313|EMBL:AES02485.1};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES02485.1};
RN [1] {ECO:0000313|EMBL:AES02485.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES02485.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
CC -!- SUBCELLULAR LOCATION: Cell projection, stereocilium membrane
CC {ECO:0000256|ARBA:ARBA00004289}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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 EMBL; JP013887; AES02485.1; -; mRNA.
DR AlphaFoldDB; G9KC60; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 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; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF255; UNCONVENTIONAL MYOSIN-IC; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
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};
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}.
FT DOMAIN 22..706
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 860..1031
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT REGION 583..605
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES02485.1"
FT NON_TER 1031
FT /evidence="ECO:0000313|EMBL:AES02485.1"
SQ SEQUENCE 1031 AA; 118290 MW; D1BA6A606490B91D CRC64;
ALGSDGVRVT MESALTARDR VGVQDFVLLE NFTSEAAFIE NLRRRFRENL IYTYIGPVLV
SVNPYRDLQI YSRQHMERYR GVSFYEVPPH LFAVADTVYR ALRTERRDQA VMISGESGAG
KTEATKRLLQ FYAETCPAPE RGGAVRDRLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDVQ
FDFKGAPVGG HILSYLLEKS RVVHQNHGER NFHVFYQLLE GGEEDMLRRL GLDRNPQSYL
YLVKGQCAKV SSINDKSDWK VVRKALTVID FTEEEVEDLL SIVASVLHLG NIHFAADEES
NAQVTTENQL KYLTRLLGVD GPTLREALTH RKIIAKGEEL LSPLNLEQAA YARDALAKAV
YSRTFTWLVR KINRSLASKD AESPSWRSTT VLGLLDIYGF EVFQHNSFEQ FCINYCNEKL
QQLFIELTLK SEQEEYEAEG IAWEPVQYFN NKIICDLVEE KFKGIISILD EECLRPGEAT
DLTFLEKLED TIKHHPHFLT HKLADQRTRK SLERGEFRLL HYAGEVTYSV TGFLDKNNDL
LFRNLKETMC SSENPIMSQC FDRSELSDKK RPETVATQFK MSLLQLVEIL KSKEPAYVRC
IKPNDAKQPG RFDEVLIRHQ VKYLGLMENL RVRRAGFAYR RKYEAFLQRY KSLCPETWPT
WAGRPQDGVA VLVRHLGYKP EEYKMGRTKI FIRFPKTLFA TEDALEVRRQ SLATKIQATW
RGFHWRQKFL RVKRSAICIQ SWWRGTLGRR KAAKRKWAAQ TIRRLIRGFI LRHAPRCPEN
AFFLDHVRTS FLLNLRRQLP RNVLDTSWPT PPAALREASE LLRELCMKNM VWKYCRSISP
EWKHQLQQKA VASEIFRGKK DNYPQSVPRL FISTRLGADE ISPKVLQALG SEPIQYAVPV
VKYDRKGYKA RSRQLLLTPS AVVIVEDAKV KQRIDYANLT GISVSSLSDS LFVLHVQRED
NKQKGDVVLQ SDHVIETLTK TAISADRVNN ININQGSITF AGGPGRDGTI DFTPGSELLI
TKAKNGHLAV V
//
