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Database: UniProt
Entry: A0A2D0TAI4_ICTPU
LinkDB: A0A2D0TAI4_ICTPU
Original site: A0A2D0TAI4_ICTPU 
ID   A0A2D0TAI4_ICTPU        Unreviewed;      1934 AA.
AC   A0A2D0TAI4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Myosin-7 {ECO:0000256|ARBA:ARBA00039815};
DE   AltName: Full=Myosin heavy chain 7 {ECO:0000256|ARBA:ARBA00041438};
DE   AltName: Full=Myosin heavy chain slow isoform {ECO:0000256|ARBA:ARBA00043207};
DE   AltName: Full=Myosin heavy chain, cardiac muscle beta isoform {ECO:0000256|ARBA:ARBA00041905};
GN   Name=LOC108280896 {ECO:0000313|RefSeq:XP_017351886.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017351886.1};
RN   [1] {ECO:0000313|RefSeq:XP_017351886.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017351886.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC       essential for muscle contraction. Forms regular bipolar thick filaments
CC       that, together with actin thin filaments, constitute the fundamental
CC       contractile unit of skeletal and cardiac muscle.
CC       {ECO:0000256|ARBA:ARBA00037090}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000256|ARBA:ARBA00004204}.
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_017351886.1; XM_017496397.3.
DR   STRING; 7998.ENSIPUP00000013304; -.
DR   Ensembl; ENSIPUT00000013861; ENSIPUP00000013304; ENSIPUG00000009014.
DR   GeneID; 108280896; -.
DR   KEGG; ipu:108280896; -.
DR   OMA; CDEYQRT; -.
DR   OrthoDB; 2877572at2759; -.
DR   Proteomes; UP000221080; Chromosome 20.
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   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 5.
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:SF1; MYOSIN-7; 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}.
FT   DOMAIN          29..78
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          82..776
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          653..675
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1905..1934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1934 AA;  223419 MW;  A5D81C08A4A4B641 CRC64;
     MGDAEFGVAG PYLRKSEKER LEAQTRIFDM KKECFVPDPV EEFVKATITS REGDKVTVET
     ESGKTLTFKD SQILQQNPPK FDKIEDMAML TFLHEPAVLY NLKERYAAWM IYTYSGLFCV
     TVNPYKWLPV YNQEVVIAYR GKKRSEAPPH IFSISDNAYQ YMLSDRENQS LLITGESGAG
     KTVNTKRVIQ YFASIAASGT KKDLPGQNKG TLEDQIIQAN PALEAFGNAK TIRNDNSSRF
     GKFIRIHFDT RGKLASADIE TYLLEKSRVT FQLKAERDYH IFYQILSNKK PEILEMLLVT
     PNPYDYAFIS QGETTVPSID DAEELMATDN AFDVLGFTQE EKNSIYKLTG AIMHFGNMKY
     KQKQREEQAE ADGTEDADKA AYLMGLNSSD LIKGLCHPRV KVGNEWVTKG QNVQQVNYAI
     GALSKALYEK MFHWMVVRIN QSLETKQPRQ YFIGVLDIAG FEIFELNTFE QLCINFTNEK
     LQQFFNHHMF VLEQEEYKKE GIEWTFIDFG MDLQACIDLI EKPMGIMSIL EEECMFPKAT
     DATFKAKLYD NHLGKSSNFQ KPRIIKGKPE AHFALVHYAG TVDYNIINWL IKNKDPLNET
     VVGLYQKSSL KLLALLFANY AGVDTALADS GKKEKKKKGS SFQTVSALHR ENLNKLMTNL
     RSTHPHFVRC IIPNESKTPG AMENPLVMHQ LRCNGVLEGI RICRKGFPNR ILYGDFKQRY
     RILNPSAIPE GQFIDSKKGA EKLLASLDVD IQQYKFGHTK VFFKAGLLGQ LEEMRDERLS
     KILTGIQARS RGLLSRFEYQ KMVERRDALL VIQWNVRAFM SVKNWPWMKL YFKIKPLLRS
     AEAEKEMANM KEEFLKLKEA YAKSEARRKE LEEKMVSLLQ EKNDLQLQVQ AEQDNLCDAE
     ERCEGLIKNK IQMEAKVKDL NERLEDEEEM NAELTAKKRK LEDECSELKK DIDDLELTLA
     KVEKEKHATE NKVKNLTEEM AALDEIIAKL TKEKKALQEA HQQTLDDLQS EEDKVNTLTK
     IKVKLEQQVD DLEGSLEQEK KVRMDLERAK RKLEGDLKLA QESIMDLEND KQQLEERLKK
     KDFEISQLNS KIEDEQVIIA QLQKKIKELQ ARVEELEEEL EAERAARAKV EKQRADLARE
     LEEISERLEE AGGATVAQIE MNKKREAEFQ KLRRDLEEAT LHHEATAATL RKKQADSVAE
     LGEQIDNLQR IKQKLEKEKS ELKLELDDVV SSMEQIVKSK TNLEKMSRTL EDQLNEFRNK
     CEESQRSLND FVTQKAKLQS ENDELSRQVE EKDSLIFQLT RGKQSYSQQL DDLKRQLEEE
     VKAKNALAHA VQSARHDSDL LREQYEEEQE AKTELQRSLT KANAEVAQWR TKYETDAIQR
     TEELEEAKKK LAQRLQDAEE AVEAVNAKCS SLEKTKHRLQ NEIEDLMVDM ERSNAAAAAL
     DKKQRNFDKV LAEWKQKYEE SQCELESSQK EARSLSTELF KLKNSYEESL DHLETLKREN
     KILQEEISDL TEQLGEGGKT IHELEKARKQ LEQEKTDIQS ALEEAEGSLE HEEGKILRSQ
     LELNQIKSEN ERKLAEKDEE MEQTKRNLQR TIDTLQSSLE AETRSRNEAF RVKKKMEGDL
     NEMEIQLSQA NRQAAEAQKQ LKIIQSNLKD CQIQLDDFIH ANDDLKENTA IVERRNVLLQ
     AEIEELRSLL EQTERGRKLA EQELLDVSER VQLLHSQNTS LLNQKKKQEA DISQLQCEVE
     DSIQECRNAE EKAKKAITDA AMMAEELKKE QDTSAHLERM KKNMEQTIKD LQQRLNEAEQ
     IAMKGGKKQV QKLEARVREL ESELEAEQKR SSETVKGIRK YERRIKELSY QSEEDRKNIG
     RLQDLVDKLQ LKVKAYKRAA EDAEEQANVH LGKFRKLQHE LDEAEERADV AESQVNKLRA
     KSREPGSKKG FDEE
//
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