ID A0A2K5E9I9_AOTNA Unreviewed; 1940 AA.
AC A0A2K5E9I9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000029898.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000029898.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- 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_012308494.1; XM_012453071.1.
DR RefSeq; XP_012308495.1; XM_012453072.1.
DR RefSeq; XP_012308496.1; XM_012453073.1.
DR STRING; 37293.ENSANAP00000029898; -.
DR Ensembl; ENSANAT00000047928.1; ENSANAP00000029898.1; ENSANAG00000032437.1.
DR GeneID; 105717719; -.
DR GeneTree; ENSGT00940000154760; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0031672; C:A band; IEA:Ensembl.
DR GO; GO:0005826; C:actomyosin contractile ring; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; 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:0070252; P:actin-mediated cell contraction; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
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 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}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000233020};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1154..1173
FT /note="Disordered"
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 1940 AA; 223109 MW; 495E5E7BB94BE635 CRC64;
MSSDSEMAVF GEAAPYLRKS EKERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSREAGKV
TVKTEAGATL TVKDDQVYPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV GAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEES ASGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELMATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
EQVTNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSANFQKPK VVKGKAEAHF SLIHYAGTVD YNITGWLDKN
KDPLNETVVG LYQKSAMKTL ANLFSGAQTA EAEASGGAKK GGKKKGSSFQ TVSALFRENL
NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDIDHTQ YKFGHTKVFF KAGLLGLLEE
MRDDKLAQLM TRTQARCRGF LARVEYQKMV ERREAIFCIQ YNIRAFMNVK HWPWMKLFFK
IKPLLKSAET EKEMATMKEE FQKTKDELAK SEAKRKELEE KMVTLLKEKN DLQLQVQAEA
EGLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
KVNTLTKAKI KLEQQVDDLE GSLEQEKKLR MDLERAKRKL EGDLKLAQES IMDIENEKQQ
LDEKLKKKEF EISNLQSKIE DEQALGIQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNV ETISKAKGNL EKMCRTLEDQ
VSELKSKEEE QQRLINDLTT QRGRLQTESG EFSRQLDEKE ALVSQLSRGK QAFTQQIEEL
KRQLEEEMKA KNALAHALQS SRHDCDLLRE QYEEEQESKA ELQRALSKAN TEVAQWRTKY
ETDAIQRTEE LEEAKKKLAQ RLQAAEEHVE AVNAKCASLE KTKQRLQNEV EDLMLDVERT
NAACAALDKK QRNFDKVLAE WKQKYEETHA ELEASQKEAR SLGTELFKMK NAYEESLDQL
ETLKRENKNL QQEISDLTEQ IAEGGKRIHE LEKIKKQVEQ EKCELQAALE EAEASLEHEE
GKILRIQLEL NQVKSEVDRK IAEKDEEIDQ LKRNHIRVVE SMQSTLDAEI RSRNDAIRLK
KKMEGDLNEM EIQLNHANRM AAEALRNYRN TQGILKDTQI HLDDALRSQE DLKEQLAMVE
RRANLLQAEI EELRATLEQT ERSRKIAEQE LLDASERVQL LHTQNTSLIN TKKKLETDIS
QMQGEMEDIL QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN MEQTVKDLQL
RLDEAEQLAL KGGKKQIQKL EARVRELEGE VESEQKRNVE AVKGLRKHER RVKELTYQTE
EDRKNILRLQ DLVDKLQAKV KSYKRQAEEA EEQSNTNLAK FRKLQHELEE AEERADIAES
QVNKLRVKSR EVHTKVISEE
//
