ID A0A3Q7U0W5_VULVU Unreviewed; 1939 AA.
AC A0A3Q7U0W5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Myosin-2 {ECO:0000256|ARBA:ARBA00039812};
DE AltName: Full=Myosin heavy chain 2 {ECO:0000256|ARBA:ARBA00041436};
DE AltName: Full=Myosin heavy chain 2a {ECO:0000256|ARBA:ARBA00042414};
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2 {ECO:0000256|ARBA:ARBA00041387};
GN Name=LOC112924899 {ECO:0000313|RefSeq:XP_025861300.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025861300.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025861300.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025861300.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025861300.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization.
CC {ECO:0000256|ARBA:ARBA00037212}.
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). Interacts with GCSAM.
CC {ECO:0000256|ARBA:ARBA00038665}.
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 RefSeq; XP_025861300.1; XM_026005515.1.
DR Proteomes; UP000286640; Unplaced.
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 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:SF39; MYOSIN-2; 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; 2.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000286640}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1127..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1901..1919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1939 AA; 223153 MW; 76C824FD634B01B7 CRC64;
MSSDQEMAIF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TVQSREGGKV
TVKTEAGATL TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEP TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELIATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
EQVTNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSANFQKPK VVKGKAEAHF SLIHYAGVVD YNITGWLDKN
KDPLNETVVG LYQKSSMKTL AYLFSGAQTA EAGNSGAKKG GKKKGSSFQT VSALFRENLN
KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQFI DSKKASEKLL ASIDIDHTQY KFGHTKVFFK AGLLGLLEEM
RDDKLAQLIT RTQARCRGFL ARVEYQKMVE RRESIFCIQY NIRAFMNVKH WPWMKLFFKI
KPLLKSAETE KEMATMKEEF QKTKDELAKS EAKRKELEEK MVTLLKEKND LQLQVQAEAE
GLADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK
VNTLTKAKIK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKLAQESI MDIENEKQQL
DEKLKKKEFE MSNLQSKIED EQALGIQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSEMKM EIDDLASNVE TVSKAKGNLE KMCRTLEDQV
SELKSKEEEQ QRLINDLTTQ RGRLQTESGE FSRQLDEKEA LVSQLSRGKQ AFTQQIEELK
RQLEEEIKAK NALAHALQSS RHDCDLLREQ YEEEQESKAE LQRALSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQAAEEHVEA VNAKCASLEK TKQRLQNEVE DLMLDVERTN
AACAALDKKQ RNFDKILAEW KQKYEETHAE LEASQKEARS LGTELFKMKN AYEESLDQLE
TLKRENKNLQ QEISDLTEQI AEGGKRIHEL EKIKKQVEQE KSEIQAALEE AEASLEHEEG
KILRIQLELN QVKSEIDRKI AEKDEEIDQL KRNHIRVVES MQTMLDAEIR SRNDAIRLKK
KMEGDLNEME IQLNHANRMA AEALRNYRNT QGILKDTQIH LDDALRGQED LKEQLAMVER
RANLLQAEIE ELRATLEQTE RSRKIAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
IQGEMEDIVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQHR
LDEAEQLALK GGKKQIQKLE ARVRELEGEV ESEQKRNAEA VKGLRKHERR VKELTYQTEE
DRKNILRLQD LVDKLQAKVK SYKRQAEEAE EQSNTNLSKF RKLQHELEEA EERADIAESQ
VNKLRVKSRE VHTKVISEE
//
