MYH10_BOVIN
ID MYH10_BOVIN Reviewed; 1976 AA.
AC Q27991;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Myosin-10;
DE AltName: Full=Cellular myosin heavy chain, type B;
DE AltName: Full=Myosin heavy chain 10;
DE AltName: Full=Myosin heavy chain, non-muscle IIb;
DE AltName: Full=Non-muscle myosin heavy chain B;
DE Short=NMMHC-B;
DE AltName: Full=Non-muscle myosin heavy chain IIb;
DE Short=NMMHC II-b;
DE Short=NMMHC-IIB;
GN Name=MYH10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ohara M., Ishiguro N., Shinagawa M.;
RT "Bos taurus nonmuscle myosin heavy chain B mRNA, complete cds.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 204-302.
RC TISSUE=Brain cortex;
RX PubMed=7782316; DOI=10.1074/jbc.270.24.14533;
RA Itoh K., Adelstein R.S.;
RT "Neuronal cell expression of inserted isoforms of vertebrate nonmuscle
RT myosin heavy chain II-B.";
RL J. Biol. Chem. 270:14533-14540(1995).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC Involved with LARP6 in the stabilization of type I collagen mRNAs for
CC CO1A1 and CO1A2. During cell spreading, plays an important role in
CC cytoskeleton reorganization, focal contacts formation (in the central
CC part but not the margins of spreading cells), and lamellipodial
CC extension; this function is mechanically antagonized by MYH9 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). Interacts with PLEKHG6. Interacts with
CC ECPAS (By similarity). Interacts with KIF26B (By similarity). Interacts
CC with LARP6. Interacts with MCC. Interacts with CFAP95 (By similarity).
CC {ECO:0000250|UniProtKB:P35580, ECO:0000250|UniProtKB:Q61879}.
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}.
CC Note=Colocalizes with MCC at the leading edge of migrating cells.
CC {ECO:0000250}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: Phosphorylated by ABL2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional non-muscle myosin. This protein
CC should not be confused with the unconventional myosin-10 (MYO10).
CC {ECO:0000305}.
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DR EMBL; AB022023; BAA36494.1; -; mRNA.
DR EMBL; U15716; AAA87715.1; -; mRNA.
DR RefSeq; NP_777259.1; NM_174834.1.
DR AlphaFoldDB; Q27991; -.
DR SMR; Q27991; -.
DR STRING; 9913.ENSBTAP00000028188; -.
DR PaxDb; Q27991; -.
DR PeptideAtlas; Q27991; -.
DR PRIDE; Q27991; -.
DR Ensembl; ENSBTAT00000075528; ENSBTAP00000065840; ENSBTAG00000021151.
DR GeneID; 317655; -.
DR KEGG; bta:317655; -.
DR CTD; 4628; -.
DR VEuPathDB; HostDB:ENSBTAG00000021151; -.
DR VGNC; VGNC:31794; MYH10.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155159; -.
DR HOGENOM; CLU_000192_4_4_1; -.
DR InParanoid; Q27991; -.
DR OMA; XERAAAN; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF333601; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021151; Expressed in trachea and 108 other tissues.
DR ExpressionAtlas; Q27991; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0097513; C:myosin II filament; IEA:Ensembl.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
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:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 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 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; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell adhesion;
KW Cell projection; Cell shape; Coiled coil; Methylation; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1976
FT /note="Myosin-10"
FT /id="PRO_0000123420"
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1126..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 845..1976
FT /evidence="ECO:0000255"
FT COMPBIAS 1697..1717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1645
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1930
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1940
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1952
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1960
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT0"
SQ SEQUENCE 1976 AA; 229099 MW; 6144354451C0F790 CRC64;
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVLV
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV SSVLQFGNIS
FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA
VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW
FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF RTVGQLYKES
LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF RAGVLAHLEE
ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK
VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA HIQDLEEQLD
EEEGARQKLQ LEKVTAEAKI KKMEEEILLL EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE
KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ IAELQAQIDE
LKIQVAKKEE ELQGALARGD DETLHKNNAL KVVRELQAQI AELQEDFESE KASRNKAEKQ
KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKSH EAQIQDMRQR
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ
VQELHAKVSE GDRLRVELAE KANKLQNELD NVSTLLEEAE KKGIKFAKDA AGLESQLQDT
QELLQEETRQ KLNLSSRIRQ LEEERSSLQE QQEEEEEARR SLEKQLQALQ AQLTDTKKKV
DDDLGTIENL EEAKKKLLKD VEVLSQRLEE KALAYDKLEK TKTRLQQELD DLLVDLDHQR
QIVSNLEKKQ KKFDQLLAEE KNISARYAEE RDRAEAEARE KETKALSLAR ALEEALEARE
EAERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED
AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLIKQVRE LEAELEDERK QRALAVASKK
KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK
KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEIANS ASGKSALLDE KRRLEARIAQ
LEEELEEEQS NMELLNDRFR KTTLQVDTLN TELAAERSAA QKSDNARQQL ERQNKELKAK
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED
ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE
VSTLKNRLRR GGPISFSSSR SGRRQLHIEG ASLELSDDDT ESKTSDINET QPPQSE
