OP1_MAIZE
ID OP1_MAIZE Reviewed; 1521 AA.
AC K7U9N8; K7UKR6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein OPAQUE1 {ECO:0000303|PubMed:22892319};
DE AltName: Full=Myosin XI motor protein {ECO:0000305};
GN Name=O1 {ECO:0000303|PubMed:22892319};
GN ORFNames=ZEAMMB73_923224 {ECO:0000312|EMBL:AFW64277.1}, Zm.5032;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000312|EMBL:AFW64277.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP INTERACTION WITH HIP, LACK OF INTERACTION WITH ZEINS; FL1 AND PROTEIN
RP BODIES PROTEINS, AND DISRUPTION PHENOTYPE.
RX PubMed=22892319; DOI=10.1105/tpc.112.101360;
RA Wang G., Wang F., Wang G., Wang F., Zhang X., Zhong M., Zhang J., Lin D.,
RA Tang Y., Xu Z., Song R.;
RT "Opaque1 encodes a myosin XI motor protein that is required for endoplasmic
RT reticulum motility and protein body formation in maize endosperm.";
RL Plant Cell 24:3447-3462(2012).
CC -!- FUNCTION: Myosin XI motor protein required for endoplasmic reticulum
CC motility and protein body formation (PubMed:22892319). May function by
CC binding with its tail domain to receptor proteins on membranes and
CC exerting force with its N-terminal motor domain against actin
CC filaments, thereby transporting its cargo along polarized actin cables
CC (By similarity). {ECO:0000250|UniProtKB:Q0WPU1,
CC ECO:0000269|PubMed:22892319}.
CC -!- SUBUNIT: Interacts (via C-terminus) with HIP (via C-terminus), but not
CC with zeins, FL1 or intrinsic proteins of protein bodies.
CC {ECO:0000269|PubMed:22892319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22892319}.
CC Note=Associated with the endoplasmic reticulum membrane.
CC {ECO:0000269|PubMed:22892319}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=K7U9N8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=K7U9N8-2; Sequence=VSP_058625;
CC -!- TISSUE SPECIFICITY: High expression in kernels and stems, intermediate
CC in ears and leaves, and low in roots, silks and tassels.
CC {ECO:0000269|PubMed:22892319}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in early developing kernels.
CC {ECO:0000269|PubMed:22892319}.
CC -!- DOMAIN: IQ domain mediates interaction with calmodulin.
CC {ECO:0000305|PubMed:22892319}.
CC -!- DOMAIN: The tail domain is a globular cargo-binding domain.
CC {ECO:0000305|PubMed:22892319}.
CC -!- DISRUPTION PHENOTYPE: Dilated endoplasmic reticulum, small and
CC misshapen protein bodies, and opaque endosperm.
CC {ECO:0000269|PubMed:22892319}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000305}.
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DR EMBL; CM000780; AFW64277.1; -; Genomic_DNA.
DR EMBL; CM000780; AFW64278.1; -; Genomic_DNA.
DR EMBL; CM000780; AFW64276.1; -; Genomic_DNA.
DR AlphaFoldDB; K7U9N8; -.
DR SMR; K7U9N8; -.
DR STRING; 4577.GRMZM2G449909_P01; -.
DR PaxDb; K7U9N8; -.
DR PRIDE; K7U9N8; -.
DR EnsemblPlants; Zm00001eb193160_T001; Zm00001eb193160_P001; Zm00001eb193160. [K7U9N8-2]
DR Gramene; Zm00001eb193160_T001; Zm00001eb193160_P001; Zm00001eb193160. [K7U9N8-2]
DR eggNOG; KOG0160; Eukaryota.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; K7U9N8; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd15475; MyosinXI_CBD; 1.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
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; IPR037975; MyosinXI_CBD.
DR InterPro; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Motor protein; Myosin; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1521
FT /note="Protein OPAQUE1"
FT /id="PRO_0000438210"
FT DOMAIN 4..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 60..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 733..755
FT /note="IQ 1"
FT /evidence="ECO:0000255"
FT DOMAIN 756..778
FT /note="IQ 2"
FT /evidence="ECO:0000255"
FT DOMAIN 781..803
FT /note="IQ 3"
FT /evidence="ECO:0000255"
FT DOMAIN 804..826
FT /note="IQ 4"
FT /evidence="ECO:0000255"
FT DOMAIN 829..851
FT /note="IQ 5"
FT /evidence="ECO:0000255"
FT DOMAIN 852..874
FT /note="IQ 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1162..1459
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 493..527
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 529..552
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 587..612
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT COILED 870..910
FT /evidence="ECO:0000255"
FT COILED 974..1050
FT /evidence="ECO:0000255"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 208..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 139
FT /note="Missing (in isoform 2)"
FT /id="VSP_058625"
SQ SEQUENCE 1521 AA; 173369 MW; 7786A6EC6E1FE116 CRC64;
MSYRKGLKVW VEEKGEGWVE AEVVEAKERA VVVFSSQRKK ITVSPEKLLP RDTDEDLGGG
HVDDMTKLTY LNEPGVLYNL KKRYALNEIY TYTGSILIAV NPFTRLPHLY NEYMMEQYKG
IRLGELSPHV FAVADASYSR AMVNDSRSQS ILVSGESGAG KTETTKLIMQ YLTFVGGRAA
LDDRTVEQQV LESNPLLEAF GNAKTVRNDN SSRFGKFVEI QFDSSGRISG AAIRTYLLER
SRVVQITDPE RNFHCFYQLC ASGKDAELYK LGHISSFHYL NQSNTHDLEG TNNEDEYWKT
KRAMDIVGIS REDQDAIFRT LAAILHLGNI EFVPGKDADS SKIKDSTSNF HLQTAAKLFM
CDSDLLVSTL CSRSIHTREG IIVKALDCAA AAANRDALAK TVYARLFDWL VENINKSIGQ
DVDSKLQIGV LDIYGFESFK NNSFEQFCIN FANEKLQQHF NEHVFKMEQE EYKSEEINWS
YIEFIDNQDV LDLIEKKPIG IIALLDEACM FPKSTHETFA TKMFRNFSSH LRLERTKFSE
TDFTISHYAG KVTYQTDSFL EKNRDYIVAE HCNLLSSSRC PFVSGLFTSL PEESIRSSYK
FSSVASRFKL QLQALMETLN STEPHYVRCV KPNSANRPQL FENQSVLHQL RCGGVLEAVR
ISLAGYPTRR TYAEFVDRFA VLVPELMIGS YDEKMMTKGI LEKMKLENFQ LGKTKVFLRA
GQIAILDMRR AEILDNAARH IQGRFRTFIT RKEFVKTREA SISIQAYCRG CLARKMFANR
RETAAAVIVQ KYVRRWLLRR AHLQACLAAL LIQSYIRGFI ARRYFSVIRE HKAATVIQST
WRRRKFVILF QNYRQATVAI QCSWRQKLAR KELRKLKMAA NEAGALREAK NKLEKKMDDL
ALRLTLERRL RASSEESKSV EILKRDKIIE SLSAECAAAK SAAQNEHAKK LLLQKQLDDS
LREITMLQSK KIMSAEAAEE NSNLKNLVES LSTKNSILEN ELIVTRKSSD DTMEKLKEVE
GKCNHLQQNL DKLQEKLTNL ENENHVLRQK AFNMPTMNNL SVAPKTLSEK FSASIGLPNS
EPKHIYESPT PTKYLASLPQ TLSTSRRSRL PVERHEQNHE ILLRCIKENL GYKDGKPVAA
CIIYKCLLHW RAFESERTAI FDHVIEAIND VLKGNEADGR LPYWLSNTSA LLCLLQRNLR
SNGLFTTPSR RSGGALGKIA QTLRSPSKFI GRSDTLPHVD ARYPAILFKQ QLTACVEKIF
GQLRDNLKKE ISPLLNVCIQ APKSTRGQSG KASKSSGVGA HPASNSNWDN IVNFLDLLMD
TLRENYVPSF FIRKLITQLF SFINIQLFNS LLLRRECCTF SNGEYVKAGL SLLEKWITDV
TDEFAGTSWH ELNYIRQAVG FLVIHQKRKK TLEEIKQDLC PSLSVRQIYR ICSMYWDDKY
GTQGISTEVV AAMREMVNKD TQNLVSNSFL LDDDLSIPFS TEDLSMAIPS IDYADVDLPE
SLQHYTSVQF LLRQQDPQPA Q
