GenomeNet

Database: UniProt
Entry: G3TF43_LOXAF
LinkDB: G3TF43_LOXAF
Original site: G3TF43_LOXAF 
ID   G3TF43_LOXAF            Unreviewed;      1940 AA.
AC   G3TF43;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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};
GN   Name=MYH1 {ECO:0000313|Ensembl:ENSLAFP00000012921.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012921.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000012921.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012921.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000012921.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012921.3};
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   -!- 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; ENSLAFT00000015421.3; ENSLAFP00000012921.3; ENSLAFG00000015427.3.
DR   GeneTree; ENSGT00940000154760; -.
DR   Proteomes; UP000007646; 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   CDD; cd14915; MYSc_Myh4; 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: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; 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   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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000007646}.
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   COILED          847..1928
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1940 AA;  222941 MW;  721EBCDBF607EEBE CRC64;
     MSADSEMAVF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV AEPKESFVKG TIQSREGGKV
     TVKTEGGATL TVKDDQIFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGDKKKEEV TSGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPEL
     IEMLLITTNP YDFAFVSQGE ITVPSIDDQE ELMATDSAVD ILGFTADEKV AIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEFVTKGQTV
     QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNRHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYEQHL GKSNNFQKPR PTKGKAEAHF SLVHYAGTVD YNIAGWLDKN
     KDPLNETVVG LYQKSALKTL AFLFAGGQSA EPEAGSGGKK GGKKKGSSFQ TVSALFRENL
     NKLMTNLRST HPHFVRCLIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
     ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDIDHTQ YKFGHTKVFF KAGLLGTLEE
     MRDDKLAQLI THTQALCRGY LMRVEFKKMM ERRESVFCIQ YNIRAFMNVK HWPWMKLYFK
     IKPLLKSAET EKEMATMKEE FEKTKEELAK SEAKRKELEE KMVALIQEKN DLQLQVQSEA
     DGLADAEERC DQLIKTKIQL EVKIKELTER ADDEEEINAE LTAKKRKLED ECSELKKDID
     DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
     KVNTLTKVKT KLEQQVDDLE GSLEQEKKLR MDLERAKRKL EGDLKLAQES TMDIENDKQQ
     LDEKLKKKEF EMNNLQGRIE DEQVLGMQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
     RSDLSRELEE ISERLEEAGG ATSTQIELNK KREAEFQKMR RDLEEATLQH ETTAATLRKK
     HADSVAELGE QIDNLQRVKQ KLEKEKSELK MEIDDLTSNM ETVSKAKGNL EKMCHTLEDQ
     LSEVKSKEEE HQRLINELST QKARLHTESG ELSRQLDEKD ALVSQLSRGK QAYIQQVEEL
     KRQLEEESKA KNALAHALQS AHHDCDLLRE QYEEEQEGKA ELQRAMSKAN SEVAQWRTKY
     ETDAIQRTEE LEDAKKKLAQ RLQDAEEHVE AAIAKCASLE KTKQRLQNEV EDLMLDVERS
     TAACAALEKK QRNFDKILSD WKQKYEETQA ELEASQKESR SLSTELFKVK NAYEESLDQL
     ETLKRENKNL EQEISDLTEQ IAEGGKHIHE LEKVKKQIDQ EKSELQAALE EAEGSLEHEE
     SKILRIQLEL NQVKSEIDQK IAEKDEEINQ LKRNHLRAVE SMQSTLDAEI RSRNDALRIK
     KKMEGDLNEM EIQLNHANRQ AAEAIRNLRS TQGILKDTQL HLDDAIRGQD DLKEQLAMAE
     RRANLMQAET EELRASLEQT ERSRKVAEQE LLDASERVQL LHTQNTGLLN TKKKLETDIS
     QIQGEMEDVV QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN LEQMAKDLQH
     RLDEAEQLAL KGGKKQIQKL EARVRELENE VENEQKRNVE AVKGLRKHER RVKELAYQAE
     EDRKNVLRLQ DLVDKLQTKV KVYKRQAEEA EEQSNVNLAK FRKLQHELEE AEERADIAES
     QVNKLRMKSR EVHTKVKSEE
//
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