ID A0A384BUI1_URSMA Unreviewed; 1940 AA.
AC A0A384BUI1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Myosin-8 isoform X2 {ECO:0000313|RefSeq:XP_008686237.2};
GN Name=MYH8 {ECO:0000313|RefSeq:XP_008686237.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008686237.2};
RN [1] {ECO:0000313|RefSeq:XP_008686237.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008686237.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_008686237.2; XM_008688015.2.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000261680; Unplaced.
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; -; 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:SF35; MYOSIN-8; 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; 4.
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};
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:UP000261680}.
FT DOMAIN 35..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 88..784
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 848..1929
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1940 AA; 222744 MW; 6922FE6C5EE525B2 CRC64;
MSASSDAEMA VFGEAAPFLR KSEKERIEAQ NKPFDAKTSV FVAEPKASYV KSTIQSKEGG
KVTVKTEGGA TLTVREDQVF PMNPPKYDKI EDMAMMTHLH EPGVLYNLKE RYAAWMIYTY
SGLFCVTVNP YKWLPVYNAE VVAAYRGKKR QEAPPHIFSI SDNAYQFMLT DRENQSILIT
GESGAGKTVN TKRVIQYFAT IAVTGEKKKE EATSGKMRGT LEDQIISANP LLEAFGNAKT
VRNDNSSRFG KFIRIHFGTT GKLASADIET YLLEKSRVTF QLKAERSYHI FYQITSNKKP
DLIEMLLITT NPYDYAFVSQ GEITVPSIDD QEELMATDSA IDILGFTPEE KVSIYKLTGA
VMHYGNMKFK QKQREEQAEP DGTEVADKAA YLQNLNSADL LKALCYPRVK VGNEYVTKGQ
TVQQVYNAVG ALAKAVYEKM FLWMVARINQ QLDTKQPRQY FIGVLDIAGF EIFDFNSFEQ
LCINFTNEKL QQFFNHHMFV LEQEEYKKEG IEWTFIDFGM DLAACIELIE KPLGIFSILE
EECMFPKATD TSFKNKLYDQ HLGKSANFQK PKVVKGKAEA HFSLIHYAGT VDYNIGGWLD
KNKDPLNDTV VGLYQKSAMK TLASLFSTYA SADTSDSGAK KGAKKKGSSF QTVSALFREN
LNKLMTNLRS THPHFVRCII PNETKTPGAM EHELVLHQLR CNGVLEGIRI CRKGFPSRIL
YGDFKQRYKV LNASAIPEGQ FIDSKKASEK LLASIDIDHT QYKFGHTKVF FKAGLLGLLE
EMRDEKLAQI ITRTQAVCRG FLMRVEYQKM LQRREAVFCI QYNIRAFMNV KHWPWMKLFF
RIKPLLKSAE TEKEMATMKK EFQKTKDELA KSEAKRKELE EKMVTLLKEK NDLQLQVQSE
ADALADAEER CEQLIKNKIQ LEAKIKEVTE RAEDEEEINA ELTAKKRKLE DECSELKKDI
DDLELTLAKV EKEKHATENK VKNLTEEMAG LDETIAKLTK EKKALQEAHQ QTLDDLQAEE
DKVNTLTKAK IKLEQQVDDL EGSLEQEKKL RMDLERAKRK LEGDLKLAQE STMDVENDKQ
QLDEKLKKKE LEISNLLSKI EDEQAVEIQL QKKIKELQAR IEELEEEIEA ERASRAKAEK
QSSDLSRELE EISERLEEAG GATSAQIEMN KKREAEFQKM RRDLEEATLQ HEAMAATLRK
KHADSVAELG EQIDNLQRVK QKLEKEKSEL KMEIDDLASN AEAISKAKGN LEKMCRTLED
QVSELKTKEE EQQRLINDLT AQRARLQTEA GEYSQQLDEK DALVSQLSRS KQASTQQIEE
LKRQLEEETK AKNALAHALQ SSRHDCDLLR EQYEEEQEGK AELQRALSKA NSEVAQWRTK
YETDAIQRTE ELEEAKKKLA QRLQEAEEHI EAVNAKCASL EKTKQRLQNE VEDLMLDVER
TNAACAALDK KQRNFDKVLA EWKQKYEETQ AELEASQKEA RALSTELFKV KNAYEESLDQ
VETLRRENKN LQQEISDLTE QIAEGGKQIH ELEKIKKQVE QEKCDIQAAL EEAEASLEHE
EGKILRIQLE LNQVKSEVDR KLAEKDEEID QLKRNHIRVV ESMQSTLDAE IRSRNDAIRV
KKKMEGDLNE MEIQLNHANR QAAEALRNYR NTQGILKDTQ LHLDDALRGQ EDLKEQLAMV
ERRANLLQAE IEELRATLEQ TERSRKIAEQ ELLDASERVQ LLHTQNTSLI NTKKKLENDV
SQLQSEVEEV IQESRNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NMEQTVKDLQ
HRLDEAEQLA LKGGKKQIQK LEARVRELEG EVENEQKRNA EAVKGLRKHE RRVKELTYQT
EEDRKNVLRL QDLVDKLQAK VKSYKRQAEE AEEQSNANLA KFRKLQHELE EAEERADIAE
SQVNKLRVKS REVHTKISGE
//
