ID L8J4S1_9CETA Unreviewed; 1947 AA.
AC L8J4S1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
DE Flags: Fragment;
GN ORFNames=M91_10500 {ECO:0000313|EMBL:ELR62442.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR62442.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR62442.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
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 EMBL; JH880342; ELR62442.1; -; Genomic_DNA.
DR STRING; 72004.ENSBMUP00000033304; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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; 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; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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, ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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:UP000011080}.
FT DOMAIN 29..79
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 83..760
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 638..660
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1316..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 824..1244
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1861..1892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..183
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:ELR62442.1"
FT NON_TER 1947
FT /evidence="ECO:0000313|EMBL:ELR62442.1"
SQ SEQUENCE 1947 AA; 224812 MW; A8DE7BDA7F88A27B CRC64;
VTMAQQAADK YLYVDKNFIN NPLAQADWAA KKLVWVPSDK SGFEPASLKE EMGEEAIVEL
VENGKKVKVN KDDIQKMNPP KFSKVEDMAE LTCLNEASVL HNLKERYYSG LIYTYSGLFC
VVINPYKNLP IYSEEIVEMY KGKKRHEMPP HIYAITDTAY RSMMQDREDQ SILCTGESGA
GKTENTKKVI QYLAHVASSH KSKKDQGELE RQLLQANPIL EAFGNAKTVK NDNSSRFGKF
IRINFDVNGY IVGANIETCI LVVNCKECSG VGRTDLLLES YNKYRFLSNG HVTIPGQQDK
DMFQETMEAF RIMGIPEEEQ MGLLRVISGV LQLGNIVFKK ERNSDQASMP DNTAAQKVSH
LLGINVTDFT RGILTPRIKV GRDYVQKAQT KEQADFAIEA LAKATYERMF RWLVLRINKA
LDKTKRQGAS FIGILDIAGF EIFDLNSFEQ LCINYTNEKL QQLFNHTMFI LEQEEYQREG
IEWNFIDFGL DLQPCIDLIE KPAGPPGILA LLDEECWFPK ATDKSFVEKV MQEQGTHPKF
QKPKQLKDKA DFCIIHYAGK VDYKADEWLM KNMDPLNDNI ATLLHQSSDK FVSELWKDVD
RIIGLDQVAG MSETAMPGAF KTRKGMFRTV GQLYKEQLAK LMATLRNTNP NFVRCIIPNH
EKKAGKLDPH LVLDQLRCNG VLEGIRICRQ GFPNRVVFQE FRQRYEILTP NSIPKGFMDG
KQACVLMIKA LELDSNLYRI GQSKVFFRAG VLAHLEEERD LKITDVIIGF QACCRGYLAR
KAFAKRQQQL TAMKVLQRNC AAYLKLRNWQ WWRLFTKVKP LLQVSRQEEE MMAKEEELVK
VREKQLAAEN RLSEMETLQS QLLAEKLQLQ EQLQAETELC AEAEELRARL TAKKQELEEI
CHDLEARVEE EEERCQHLQA EKKKMQQNIQ ELEEQLEEEE SARQKLQLEK VTTEAKLKKL
EEDQIIMEDQ NCKLAKEKKL LEDRIAEFTT NLMEEEEKSK SLAKLKNKHE AMITDLEERL
RREEKQRQEL EKTRRKLEGD STDLNDQIAE LQAQIAELKM QLAKKEEELQ AALARVEEET
TQKNMALKKI RELESQISEL QEDLESERAA RNKAEKQKRD LGEELEALKT ELEDTLDSTA
AQQELRSKRE QEVNILKKTL EDEARTHEAQ IQDMRQKHSQ AVEELAEQLE QTKRVKANLE
KAKQTLENER GELANEVKVL QQGKADTEHK RKKVEAQLQE LQVKFTEGER VRTELADKVS
KLQVELDNVT GLLTQSDSKS SKLTKDFSAL ESQLQDTQEL LQEENRQKLS LSTKLKQVED
EKNSLKEQLE EEEEAKRNLE KQISTLHAQV TDMRKKMDDS VGCLETAEEA KRKLQKDLEG
LSQRYEEKVA AYDKLEKTKT RLQQELDDLL VDLDHQRQSV SNLEKKQKKF DQLLAEEKTI
SAKYAEERDR AEAEAREKET KALSLARALE EAMEQKAELE RLNKQFRTEM EDLMSSKDDV
GKSVHELEKS KRALEQQVEE MKTQLEELED ELQATEDAKL RLEVNLQAMK AQFERDLQGR
DEQSEEKKKQ LVKQVREMEA ELEDERKQRS IAVAARKKLE MDLKDLEAHI DSANKNRDEA
IKQLRKVQAQ MKDYMRELDD TRASREEILA QSKENEKKLK SMEAEMIQLQ EELAAAERAK
RQAQQERDEL ADEIANSSGK GALALEEKRR LEARIAQLEE ELEEEQGNTE LVNDRLKKAN
LQIDQLNTDL NLERSHTQKN ENARQQLERQ NKELKVKLQE MEGTVKSKFK ASIAALEAKI
AQLEEQLDNE TKERQAACKQ VRRAEKKLKD VLLQVDDERR NAEQYKDQAD KASTRLKQLK
RQLEEAEEEA QRANASRRKL QRELEDATET ADAMNREVSS LKNKLRRGDL PFVVPRRMAR
KGASDCSDDE MDGKADGAEA KAAEARA
//
