ID A0A286ZXE3_PIG Unreviewed; 1965 AA.
AC A0A286ZXE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Myosin-6 {ECO:0000256|ARBA:ARBA00039814};
DE AltName: Full=Myosin heavy chain 6 {ECO:0000256|ARBA:ARBA00041439};
DE AltName: Full=Myosin heavy chain, cardiac muscle alpha isoform {ECO:0000256|ARBA:ARBA00041383};
GN Name=MYH6 {ECO:0000313|Ensembl:ENSSSCP00000036306.2};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000036306.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000036306.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000036306.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000036306.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC {ECO:0000256|ARBA:ARBA00038612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000256|ARBA:ARBA00004657}.
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 Ensembl; ENSSSCT00000035069.3; ENSSSCP00000036306.2; ENSSSCG00000002029.6.
DR GeneTree; ENSGT00940000154805; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000002029; Expressed in heart left ventricle and 33 other cell types or tissues.
DR ExpressionAtlas; A0A286ZXE3; baseline and differential.
DR GO; GO:0030016; C:myofibril; 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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF11; MYOSIN-6; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 4.
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 1: Evidence at protein level;
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};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZXE3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..780
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1909..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1928
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 1965 AA; 226154 MW; DA95965456B348DF CRC64;
MTDAQMADFG AAAQYLRKSE KERLEAQTRP FDIRTECFVP DDKEEFVRAK ILSREGGKVT
AETENGKTVT VKEDQVLQQN PPKFDKIEDM AMLTFLHEPA VLFNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYNAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFASIAA IGDRGKKDNV NANKGTLEDQ IIQANPALEA FGNAKTVRND
NSSRFGKFIR IHFGATGKLA SADIETYLLE KSRVIFQLKA ERNYHIFYQI LSNKKPELLD
MLLVTNNPYD YAFVSQGEVS VASIDDSEEL VATDSAFDVL GFTSEEKAGV YKLTGAIMHY
GNMKFKQKQR EEQAEPDGTE DADKSAYLMG LNSADLLKGL CHPRVKVGNE YVTKGQNVQQ
VYYSIGALAK AVYEKMFNWM VTRINATLET KQPRQYFIGV LDIAGFEIFD FNSFEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLQA CIDLIEKPMG IMSILEEECM
FPKATDMTFK AKLYDNHLGK SNNFQKPRNI KGKPEAHFSL IHYAGTVDYN IIGWLEKNKD
PLNETVVGLY QKSSLKLMAT LFSSYASADV GDSSKGKGGK KKGSSFQTVS ALHRENLNKL
MTNLRTTHPH FVRCIIPNER KAPGVMDNPL VMHQLRCNGV LEGIRICRKG FPNRILYGDF
RQRYRILNPA AIPEGQFIDS RKGTEKLLGS LDIDHNQYKF GHTKVFFKAG LLGLLEEMRD
ERLSRILTRI QAQARGQLMR IEFKKILERR DALLVIQWNI RAFMGVKNWP WMKLYFKIKP
LLKSAETEKE MATMKEEFGR LKETLEKSEA RRKELEEKMV SLLQEKNDLQ LQVQAEQDNL
NDAEERCDQL IKNKIQLEAK VKEMTERLED EEEMNAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMAGLDEI IAKLTKEKKA LQEAHQQALD DLQAEEDKVN
TLTKSKVKLE QQVDDLEGSL EQEKKVRMDL ERAKRKLEGD LKLTQESIMD LENDKLQLEE
KLKKKEFEIN QQNSKIEDEQ ALALQLQKKL KENQARIEEL EEELEAERTA RAKVEKLRSD
LSRELEEISE RLEEAGGATS VQIEMNKKRE AEFQKMRRDL EEATLQHEAT AAALRKKHAD
SVAELGEQID NLQRVKQKLE KEKSEFKLEL DDVTSNMEQI IKAKANLEKM SRTLEDQANE
YRAKLEEAQR SLNDFSTQRA KLQTENGELS RQLEEKEALI SQLTRGKLSY TQQLEDLKRQ
LEEEGKAKNA LAHALQSARH DCDLLREQYE EETEAKAELQ RVLSKANSEV AQWRTKYETD
AIQRTEELEE AKKKLAQRLQ DAEEAVEAVN AKCSSLEKTK HRLQNEIEDL MVDVERSNAA
AAALDKKQRN FDKILAEWKQ KYEESQSELE SSQKEARSLS TELFKLKNAY EESLEHLETF
KRENKNLQEE ISDLTEQLGS SGKTIHELEK VRKQLEVEKL ELQSALEEAE ASLEHEEGKI
LRAQLEFNQI KAEIERKLVE KDEEMEQAKR NHLRVVDSLQ TSLDAETRSR NEALRVKKKM
EGDLNEMEIQ LSHANRMAAE AQKQVKSLQS LLKDTQIQLD DAVRANDDLK ENIAIVERRN
NLLQAELEEL RAVVEQTERS RKLAEQELIE TSERVQLLHS QNTSLINQKK KMESDLTQLQ
SEVEEAVQEC RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNMEQ TIKDLQHRLD
EAEQIALKGG KKQLQKLEAR VRELENELEA EQKRNAESVK GMRKSERRIK ELTYQTEEDR
KNLLRLQDLV DKLQLKVKAY KRQAEEAEEQ ANTNLSKFRK VQHELDEAEE RADIAESQVN
KLRAKSRDIG AKVGPSPDSA THPHSSACPR TSAPLRMGTP RPVFG
//
