ID A0A2Y9PYL0_DELLE Unreviewed; 1976 AA.
AC A0A2Y9PYL0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Myosin-10 isoform X11 {ECO:0000313|RefSeq:XP_022451879.1};
GN Name=MYH10 {ECO:0000313|RefSeq:XP_022451879.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022451879.1};
RN [1] {ECO:0000313|RefSeq:XP_022451879.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022451879.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022451879.1; XM_022596171.2.
DR Ensembl; ENSDLET00000033661; ENSDLEP00000030653; ENSDLEG00000021805.
DR Proteomes; UP000248483; Unplaced.
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:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0097513; C:myosin II filament; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR CDD; cd14920; MYSc_Myh10; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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:SF24; MYOSIN-10; 1.
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; SSF90257; Myosin rod fragments; 7.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000248483}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1126..1172
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 COMPBIAS 1126..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1976 AA; 228948 MW; A531DF1A6A4E873D CRC64;
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV
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 MFVLEQEEYQ REGIEWSFID 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 KVARELQAQL AELQEDFESE KASRNKAEKQ
KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEEETKNH EAQIQDMRQR
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ
VQELHAKVSE GDRLRVELAE KANKLQNELD NVSTLLEEAE KKGIKFAKDA AGLESQLQDT
QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLALQ AQLTDTKKKV
DDDLGTIESL EEAKKKLLKD VEALSQRLEE KALAYDKLEK TKNRLQQELD DLLVDLDHQR
QIVSNLEKKQ KKFDQLLAEE KNISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE
ESERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED
AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLMKQVRE LEAELEDERK QRALAVASKK
KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK
KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEIANS ASGKSALLDE KRRLEARIAQ
LEEELEEEQS NMELLNDRFR KTTLQVDTLN AELAAERSAA QKSDNARQQL ERQNKELKAK
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED
ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE
VSTLKNRLRR GGPISFSASR SGRRQLHIEG ASLELSDDDT ESKTSDVNET QPPQSE
//
