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Database: UniProt
Entry: MYO10_ARATH
LinkDB: MYO10_ARATH
Original site: MYO10_ARATH 
ID   MYO10_ARATH             Reviewed;        1770 AA.
AC   F4IVR7; Q8RYE8;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Myosin-10;
DE   AltName: Full=Myosin XI D;
DE            Short=AtXID;
GN   Name=XI-D; Synonyms=XID; OrderedLocusNames=At2g33240; ORFNames=F25I18.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=10984423; DOI=10.1242/jcs.113.19.3353;
RA   Hodge T., Cope M.J.;
RT   "A myosin family tree.";
RL   J. Cell Sci. 113:3353-3354(2000).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=11516337; DOI=10.1186/gb-2001-2-7-research0024;
RA   Reddy A.S., Day I.S.;
RT   "Analysis of the myosins encoded in the recently completed Arabidopsis
RT   thaliana genome sequence.";
RL   Genome Biol. 2:RESEARCH0024.1-RESEARCH0024.17(2001).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORM 2).
RX   PubMed=19369591; DOI=10.1104/pp.109.136853;
RA   Avisar D., Abu-Abied M., Belausov E., Sadot E., Hawes C., Sparkes I.A.;
RT   "A comparative study of the involvement of 17 Arabidopsis myosin family
RT   members on the motility of Golgi and other organelles.";
RL   Plant Physiol. 150:700-709(2009).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21233331; DOI=10.1104/pp.110.170720;
RA   Peremyslov V.V., Mockler T.C., Filichkin S.A., Fox S.E., Jaiswal P.,
RA   Makarova K.S., Koonin E.V., Dolja V.V.;
RT   "Expression, splicing, and evolution of the myosin gene family in plants.";
RL   Plant Physiol. 155:1191-1204(2011).
CC   -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC       regulated transport of various organelles and proteins for their
CC       segregation. Functions by binding with its tail domain to receptor
CC       proteins on organelles and exerting force with its N-terminal motor
CC       domain against actin filaments, thereby transporting its cargo along
CC       polarized actin cables (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4IVR7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4IVR7-2; Sequence=VSP_047340;
CC   -!- DOMAIN: IQ domain mediates interaction with calmodulin. {ECO:0000250}.
CC   -!- DOMAIN: The tail domain is a globular cargo-binding domain.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM14807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002334; AAM14807.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08804.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62028.1; -; Genomic_DNA.
DR   PIR; A84743; A84743.
DR   RefSeq; NP_001324211.1; NM_001336436.1. [F4IVR7-2]
DR   RefSeq; NP_180882.2; NM_128883.3. [F4IVR7-1]
DR   AlphaFoldDB; F4IVR7; -.
DR   SMR; F4IVR7; -.
DR   STRING; 3702.F4IVR7; -.
DR   iPTMnet; F4IVR7; -.
DR   PaxDb; 3702-AT2G33240-1; -.
DR   EnsemblPlants; AT2G33240.1; AT2G33240.1; AT2G33240. [F4IVR7-1]
DR   EnsemblPlants; AT2G33240.4; AT2G33240.4; AT2G33240. [F4IVR7-2]
DR   GeneID; 817886; -.
DR   Gramene; AT2G33240.1; AT2G33240.1; AT2G33240. [F4IVR7-1]
DR   Gramene; AT2G33240.4; AT2G33240.4; AT2G33240. [F4IVR7-2]
DR   KEGG; ath:AT2G33240; -.
DR   Araport; AT2G33240; -.
DR   TAIR; AT2G33240; XID.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_3_1_1; -.
DR   InParanoid; F4IVR7; -.
DR   OrthoDB; 664095at2759; -.
DR   PRO; PR:F4IVR7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IVR7; baseline and differential.
DR   Genevisible; F4IVR7; AT.
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-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; ISS:TAIR.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; TAS:TAIR.
DR   CDD; cd15475; MyosinXI_CBD; 1.
DR   CDD; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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; 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   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF797; MYOSIN-10; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Coiled coil; Motor protein; Myosin; Nucleotide-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1770
FT                   /note="Myosin-10"
FT                   /id="PRO_0000422865"
FT   DOMAIN          25..73
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          78..748
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          774..803
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          799..828
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          822..851
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          847..876
FT                   /note="IQ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          870..899
FT                   /note="IQ 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1347..1718
FT                   /note="Dilute"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT   REGION          511..545
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          547..570
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          605..629
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          629..651
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1388..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1477..1566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          900..1253
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1491..1510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1529..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         225..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1256..1268
FT                   /note="KSLDLFVFMYLFQ -> VSFTRPP (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047340"
SQ   SEQUENCE   1770 AA;  200639 MW;  56084D27F0EB6574 CRC64;
     MVWKHQLIGF SGIFSNVSPA SVKVTVGSQV WVEDPDEAWL DGEVVEANGQ EIKVNCQTKT
     VVAKVNAVHP KDPEFPELGV DDMTKLAYLH EPGVLLNLKA RYNANEIYTY TGNILIAVNP
     FKRLPHLYGN EIMEQYKGTD FGELSPHPFA VADSAYRKMI NEGVSQAILV SGESGAGKTE
     STKMLMQYLA YMGGKAESEG RSVEQQVLES NPVLEAFGNA KTVRNNNSSR FGKFVEIQFN
     HMGRISGAAI RTYLLERSRV CQVSDPERNY HCFYMLCAAP EQETERYQLG KPSTFHYLNQ
     SNCHALDAID DSKEYLATRK AMDVVGISPE EQDAIFRVVA AILHLGNIEF AKSEESDGAE
     PKDDKSRFHL KVAAKLFMCD EKALENSLCN RVMVTRGESI TKPLDPGSAA LSRDALAKIV
     YSKLFDWLVT KINNSIGQDS SSKYIIGVLD IYGFESFKTN SFEQFCINLT NEKLQQHFNQ
     HVFKMEQEEY TKEEIDWSYI EFIDNQDVLD LIEKKPGGII ALLDEACMFP RSTHDTLAEK
     LYQTFGSHKR FTKPKLARTD FTICHYAGDV TYQTELFLDK NKDYVVGEHQ SLMNSSDCSF
     VSSLFPKSRE ESSKSSKFSS IGSQFKQQLQ SLLETLNTTE PHYIRCVKPN NVLKPEIFEN
     VNVLHQLRCG GVMEAIRISC AGYPTRKPFN EFLTRFRILA PEATERSFDE VDACKKLLAR
     VDLKGFQIGK TKVFLRAGQM AELDAHRAEV LGHSARIIQR KVITYLSRKK YLLLQSASTE
     IQAFCRGHIA RVQFKATRRE AASVRIQKQA RTYICQTAFK KLCASAISIQ SGLRAMAARV
     EFQYRTKRKA AIIIQSQIRR CLCRRRYLRT KKAAITTQCG WRVKVAHREL RKLKMAAKET
     GALQDAKTKL EKEVEELTSC LELEKQMRME LEQVKTQEVE DLRSALNDMK LQLGETQVTK
     SEEILKLQSA LQDMQLEFEE LAKELEMTND LAAENEQLKD LVSSLQRKID ESDSKYEETS
     KLSEERVKQE VPVIDQGVII KLEAENQKLK ALVSTLEKKI DSLDRKHDVT SSNISDQLKE
     SASSDYEMLS NLAAENERLK ALVSSLENEN YENDGNDSPN EQKEGPQMLK EEILAEDFSI
     DDEMTNKLAA ENKDLYDLVD LLERKIDETE KKYEEASKLC EERLKQVVDT EKKYEEASRL
     CEERLKQVVD TETKLIELKT SMQRLEEKVS DMEAEDKILR QQALRNSASR KMSPQKSLDL
     FVFMYLFQPV ENGHHESFAP IPSRRFGAMS FRRSQIEQQP HEFVDVLLKC VSKNVGFSHG
     KPVAAFTIYK CLIHWKLFEA EKTSVFDRIV PIFGSAIENP EDDSNLAYWL TNTSTLLFLL
     QRSLKSHSTT GASPKKPPQP TSFFGRMTQG FRSPSSASLS GDVVQQVDAR YPALLFKQQL
     TAYIETIYGI FQENVKRKLA PVLSSCIQGL KDSSHEFSAE TLSAESSEQN SPEKPSEENP
     PEKLSEDNSS GKLSEDYLAA KPSEDNSPAK PSEENSQAKL SEVNPQAKPS AENSLAKPSE
     ENSPTETWQD VIGLLNQLLG TLKKNYVPLF LAQKIFCQTF QDINVQLFNS LLQRECCTFI
     MGKKVNVWLN ELESWCSQAT EDFVGSSWDE LKNTRQALVL LVTEQKSTIT YDDLTTNLCP
     ALSTQQLYRI CTLCKIDDHE DQNVSPDVIS NLKLLVTDED EDSRSFLLDN NSSIPFAADE
     ISNSMQEKDF TNVKPAVELA DNPNFHFLKE
//
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