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Database: UniProt
Entry: A0A452SLH9_URSAM
LinkDB: A0A452SLH9_URSAM
Original site: A0A452SLH9_URSAM 
ID   A0A452SLH9_URSAM        Unreviewed;      1566 AA.
AC   A0A452SLH9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Myosin-4 {ECO:0000256|ARBA:ARBA00044107};
DE   AltName: Full=Myosin heavy chain 2b {ECO:0000256|ARBA:ARBA00044300};
DE   AltName: Full=Myosin heavy chain 4 {ECO:0000256|ARBA:ARBA00044226};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033474.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000033474.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; ENSUAMT00000037284.1; ENSUAMP00000033474.1; ENSUAMG00000025308.1.
DR   GeneTree; ENSGT00940000163646; -.
DR   OMA; PGEVNQP; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
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; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; 2.
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:SF78; MYOSIN-4; 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; 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};
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:UP000291022}.
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..754
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          631..653
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1097..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1125..1144
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   1566 AA;  179542 MW;  99EEBA6EFE247D9D CRC64;
     MSSDTEMAIF GEAAPYLRKS EKERIEAQNR PFDAKNSVFV VDAKESYVKS TVQSREGGKV
     TVKTDAGATV TVKEDQVFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA ITGEKKKEEP TPGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
     IEMLLITTNP YDFAFVSQGE ITVPSIDDQE ELLATDSAVD ILGFSTDEKA AIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
     QQVYNAVGAL AKAIYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNHHMFLIE KPMGIFSILE EECMFPKATD TSFKNKLYEQ HLGKSANFQK
     PKPAKGKAEA HFSLVHYAGT VDYNIAGWLD KNKDPLNETV VGLYQKSGMK TLALLFAGGQ
     SAEAESGGGK KGAKKKGSSF QTVSALFREN LNKLMTNLRS THPHFVRCII PNETKTPGAM
     EHELVLHQLR CNGVLEGIRI CRKGFPSRIL YADFKQRYKV LNASAIPEGQ FIDSKKASEK
     LLGSIDIDHN QYKFGHTKVF FKAGLLGTLE EMRDEKLAQL ITRTQAVCRG YLMRVEFKKM
     MERRESIFCI QYNVRAFMNV KHWPWMKLYF KIKPLLKSAE TEKEMATMKE EFEKTKEELA
     KSEAKRKELE EKMVALMQEK NDLQLQVQSE ADGLADAEER CDQLIKTKIQ LEAKIKELTE
     RAEEEEEINA ELTAKKRKLE DECSELKKDI DDLELTLAKV EKEKHATENK VKNLTEEMAG
     LDETIAKLTK EKKALQEAHQ QTLDDLQAEE DKVNTLTKAK TKLEQQVDDL EGSLEQEKKI
     RMDLERAKRK LEGDLKLAQE STMDVENDKQ QLDEKFKKKE FEMSNLQSKI EDEQALAMQL
     QKKIKELQAR IEELEEEIEA ERASRAKAEK QRSDLSRELE EISERLEEAG GATSAQIEMN
     KKREAEFQKM RRDLEEATLQ HEATAATLRK KHADSVAELG EQIDNLQRVK QKLEKEKSEL
     KMEIDDLASN METVSKAKGN LEKTCRTLED QLSEVKMKEE EQQRLINELS AQKARLHTES
     GEFSRQLDEK EALVSQLSRG KQAFTQQIEE LKRQLEEESK AKNALAHALQ SARHDCDLLR
     EQYEEEQEAK AELQRSMSKA NSEVAQWRTK YETDAIQRTE ELEEAKKKLA QRLQDAEEHV
     EAVNSKCASL EKTKQRLQNE VEDLMLDVER SNAACATLDK KQRNFDKVLA EWKQKYEETQ
     AELEASQKEA RTLSTELFKV KNAYEESLDH LENLKRENKN LQQEISDLTE QIAEGGKHIH
     ELEKVKKQID QEKSELQAAL EEAEGSLEHE EGKILRIQLE LNQVKSEIDR KIPATQRRRP
     RRPSLT
//
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