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Database: UniProt
Entry: F7FKN4_CALJA
LinkDB: F7FKN4_CALJA
Original site: F7FKN4_CALJA 
ID   F7FKN4_CALJA            Unreviewed;      1940 AA.
AC   F7FKN4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Myosin heavy chain 3 {ECO:0000313|Ensembl:ENSCJAP00000023953.2};
GN   Name=MYH3 {ECO:0000313|Ensembl:ENSCJAP00000023953.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000023953.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000023953.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000023953.2}
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   -!- 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_002747955.2; XM_002747909.4.
DR   RefSeq; XP_017827769.1; XM_017972280.1.
DR   STRING; 9483.ENSCJAP00000023953; -.
DR   Ensembl; ENSCJAT00000025338.4; ENSCJAP00000023953.2; ENSCJAG00000012860.4.
DR   GeneID; 100394006; -.
DR   KEGG; cjc:100394006; -.
DR   CTD; 4619; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000161575; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; F7FKN4; -.
DR   OMA; CERMAKQ; -.
DR   OrthoDB; 2877572at2759; -.
DR   TreeFam; TF314375; -.
DR   Proteomes; UP000008225; Chromosome 5.
DR   Bgee; ENSCJAG00000032980; Expressed in testis.
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   CDD; cd14910; MYSc_Myh1_mammals; 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:SF2; MYOSIN-1; 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}; 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:UP000008225};
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          1126..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  223202 MW;  96ABCA908E6459DD CRC64;
     MSSDSEMAIF GEAAPYLRKS EKERIEAQNK PFDAKTSVFV ADPKESFVKA TVQSREGGKV
     TAKTEGGTTV TVKDDQVYPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGEKKKEET TSGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
     IEMLLITTNP YDYAYVSQGE ITVPSIDDQE ELMATDSAID ILGFSSDERV SIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
     QQVYNAVGAL AKAVYDKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDYNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKVEAHF SLVHYAGTVD YNIAGWLDKN
     KDPLNETVVG LYQKSAMKTL AYLFSGAAAA EAEAGGGGKK GGKKKGSSFQ TVSALFRENL
     NKLMTNLRST HPHFVRCIIP NETKTPGAME HELVLHQLRC NGVLEGIRIC RKGFPSRILY
     ADFKQRYKVL NASAIPEGQF IDSKKASEKL LGSIDIDHTQ YKFGHTKVFF KAGLLGLLEE
     MRDEKLAQLI TRTQARCRGF LARVEYQKMV ERRESIFCIQ YNIRAFMNVK HWPWMKLYFK
     IKPLLKSAET EKEMANMKEE FEKTKESLAK AEAKRKELEE KMVALMQEKN DLQLQVQAEA
     ESLADAEERC DQLIKTKIQL EAKIKEVTER AEDEEEINAE LTAKKRKLED ECSELKKDID
     DLELTLAKVE KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQEAHQQ TLDDLQAEED
     KVNTLTKAKI KLEQQVDDLE GSLEQEKKIR MDLERAKRKL EGDLKLAQES TMDIENDKQQ
     LDEKLKKKEF EMSNLQSKIE DEQALGMQLQ KKIKELQARI EELEEEIEAE RASRAKAEKQ
     RSDLSRELEE ISERLEEAGG ATSAQIEMNK KREAEFQKMR RDLEEATLQH EATAATLRKK
     HADSVAELGE QIDNLQRVKQ KLEKEKSEMK MEIDDLASNM ETVSKSKGNL EKMCRTLEDQ
     LSELKSKEEE QQRLINDLTA QRARLQTESG EYSRQLDEKD SLVSQLSRGK QAFTQQIEEL
     KRQLEEEIKA KSALAHALQS SRHDCDLLRE QYEEEQEAKA ELQRAMSKAN SEVAQWRTKY
     ETDAIQRTEE LEEAKKKLAQ RLQDAEEHVE AVNAKCASLE KTKQRLQNEV EDLMIDVERT
     NAACAALDKK QRNFDKILAE WKQKYEETHA ELEASQKESR SLSTELFKIK NAYEESLDQL
     ETLKRENKNL QQEISDLTEQ IAEGGKRIHE LEKIKKQVEQ EKSEIQAALE EAEASLEHEE
     GKILRIQLEL NQVKSEIDRK IAEKDEEIDQ LKRNHIRVVE SMQSTLDAEI RSRNDAIRLK
     KKMEGDLNEM EIQLNHANRM AAEALRNYRN TQGILKDTQI HLDDALRGQE DLKEQLAMVE
     RRANLLQAEI EELRATLEQT ERSRKIAEQE LLDASERVQL LHTQNTSLIN TKKKLETDIS
     QIQGEMEDIV QEARNAEEKA KKAITDAAMM AEELKKEQDT SAHLERMKKN LEQTVKDLQH
     RLDEAEQLAL KGGKKQIQKL EARVRELEGE VENEQKRNVE AVKGLRKHER RVKELTYQTE
     EDRKNILRLQ DLVDKLQAKV KAYKRQAEEA EEQSNVNLSK FRKIQHELEE AEERADIAES
     QVNKLRVKSR EVHTKIISEE
//
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