ID A0A1S3T1M3_SALSA Unreviewed; 2829 AA.
AC A0A1S3T1M3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Unconventional myosin-XVIIIa-like isoform X5 {ECO:0000313|RefSeq:XP_014070495.1};
GN Name=LOC106613097 {ECO:0000313|RefSeq:XP_014070495.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014070495.1};
RN [1] {ECO:0000313|RefSeq:XP_014070495.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014070495.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_014070495.1; XM_014215020.1.
DR OrthoDB; 3687088at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; cd01386; MYSc_Myo18; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {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:UP000087266}.
FT DOMAIN 721..1487
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 13..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2157..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2539..2599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2616..2829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1839..1980
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2260..2285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2345..2365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2376..2404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2411..2425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2463..2484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2496..2524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2548..2566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2616..2672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2673..2695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2709..2728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2743..2781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2802..2829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 814..821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2829 AA; 314037 MW; B92F5CEC8A9214F0 CRC64;
MAFSSRFSFW EQKVKEEVRP PGSKISNQGS DSDSGSMSSR SQSVPSLEPG RGLLRTKSPE
PAKTHPGIRV RSPSPPRVRG AVKVPERFKS LVPPIQTPAQ HFRSPDPRRA SIISPEPVLN
GNSKPNGSVN VSAVNGNSAN GSARQPDLDN DDPSLTLKKV VKVVRQVVRK ALPAEEEDAP
APEPTKPAPE PPKLLPSQAP TSVPKVPKVP LFSFKHDTIK TEEKDDISAG LASLMVRGRT
RNRPRTRMDE PPEKEQEEAV KREEKEGPKL VEIKSISNFG PVSKQEDQTP VSAAPAKVHP
MASNLISVPS RSSPAGFIPA SKPSLLSPPA GFTPPPKSAS LSPPAGFVPA PKSSPLCQPN
GYVPAPKSAT LSPPAGFVPA PKSTAVSRSV STAAPKSSPA IPPSCFIPPP KCPPLSPPAG
FVPSPKYNAF TPSVSTAAPK SSPAIPTSCF IPPLKSAPIS PPAGFISASK YTPLSPPAGF
IPSCKYSPVT PPSASFPTSK SSPSTPPAGF IPVSKVSPLS PTPPKASPLS PPPAFIIPKA
SALSPPPALI PPPKLPAVKK PEVAASPLSS VPIEKASPQN NSSTVSSKTT PTITQKEAPL
SPTEEAQRRL DRIFSAPATS LLQHTIQLEP AVCASAPTLS PAPAPNPPQV KTEEQIAAEQ
TWYGSEKVWL VHKDGFSLAT LLKTEAGSLP EGKVKIKLEH DGTVLDVDDD DVEKANPPSF
DRSEDLASLQ YLNESSVMHS LRQRYGGNLI HTHAGPNMII INPLSAPSMY SEKVMHMFKG
CRREDTAPHI YAVAQSAYRN LLTTRQDQSI VLLGKSGSGK TTNCQHLVQY LVSIAGSTGK
IFSGEKWQAV YTILEAFGNS STSMNTNASR FSQIVSLDFD QAGQVASASV QTMLLEKLRV
TKRPETESTF NIFYYMMSGA DSTLRTELHF NHFAENSAFG IVPQSKLEDK QKSSQQFTKL
QAAMKVLGIS VEEQRALWLI LGAIYHLGAA GATKEAEEAG RKQFARHEWA QKAAYLLGCT
LEELSSSIFK HQVKGALQRS TSFRGGPDEA GAGDSSVSKI TALDCLEAMA SGLYSELFTL
VISLVNRALK SSQHSLCSLL IVDTPGFQNP RMAKRQRGAT FEELCHNYAQ ERLQTLFHER
TFVQELERYK EENIELALDD IGSSTSMSVA AIDQASTQAL VRTHLRTDEA RGLLWLMEEE
AVQPGGSEDT LLERLFSYYG PDQGDNKGHA LLLKSDKPHH FLLGHSHGTA WVEYDAQGWL
SHAKQNPASQ NAATLLQDSQ KKNISSLFSS RSGGPTVLSG SIAGLEGGSQ LALRRATSMR
KTFTTGMAAV KKKSLCIQIK LQVDALLDTV RRSRVHFVHC LLPKADALGV GMEPRVAHGE
SCDSGLMQLD VGLLRAQLRG SKLIDALRIY RQGYPDHMVF SEFRRRFDVL APHLTKKHGC
HYMVTDEKRA VEELLESLDL ENSSYHMGLS RVFFRAGTLA KLEEQRDVQT RRNITMFQAA
CRGYLARQAF KKRKIQDLAI RCIQKNIKKN KGVKGWPWWK VFTTVRPLIE VQLTEEQIRG
KDEEIQQLKG RLEKVDKERN ELRLNSDRLE SRITELSSEL ADERNTGESA SQLLESETSE
RLRLEKDMKD LQTKFDSMKK SMDSMEMEVM ETRLLRASEL NGEMDDDDTG GEWRLKYERA
IRETEFTKKR LQQEFIDKLE VEQQNKRQLE RRLSDLQADS EEGQRTAQQL KKKCQRLTAE
LQDTKLHLEG QQSRNHDLEK KQRKFDSEQN LSQDEVQREK NLREKLSREK DMLTGEVFSL
RQQLEDKDLE MCAQNVKLEQ LEAELLDLSS QETKDEASLS KVKKTMRDLE AKVKDQEEEL
DEQAGTIQML EQAKLRLEME TERLRQTHSK EIESKDEEVE EIRQSCSKKL KQIEVQLEEE
YDDKQKVLRE RRELETKLLS AQDQVKPRDV ETEKRLKKDL KRTKALLADA QIMLDHMKNN
APSKREIAQL KNQLEESEFT CAAAVKARKS MEVEIEDLHV QMDDISKAKQ ALEEQLSRLL
REKNDLQSRM EEDQEDMNEL MKKHKSAVVQ STQNLAQISD LQAQLEEALK QKQDVQEKLS
ALQSQLEFQE TSMVEKSLVS RHEAKIREME TKMEFEKTQV KRLESLVARL KENLEKLTEE
RDHRSTSETR EKEQNKRLQR QIRDIKEEMG ELAKKEGEAS RKKHELEMDI ESLEAANQSL
QADLKLAFKR IGDLQAAIED DMESDGNEDL ISSLQDMVTK YQKRRNKTEG DSSDSEIEDC
VDGVKSWLSK NKGSTKNLSD DGSLKSSRFA VNVDAKEGKE WKEGKEWKEF NKEGKEKEVD
SRRPVSVMSS LSYRKHSNIN DSIGGKGDDS SLKKGQDSQE SITTFRKAKP KCSSPQGDSS
SWRKSQTGND DDRGSVISQA YTEATSRARK GMDSRWGDFD KESTVSSMAP SRACVATTRF
GLSPEDDTKS TISLGMSSPL SRRSTSAHRT DESYGRSGRC PSSPSVSRRS GGRSPGSVSR
ADSRISDFRS CRLSEFDDME DGHSVAFTER SSAYSPHSST GRSLSMPPPP ARSYRDDDEL
PDTSDVKPAT VSHRNYLDPD LEKAINEVLN FKPIKFKRTS LEDSEAEAGR KEDDTEDDRK
SVVSVRGRGD RKSVLSVRGR DDREDDSRRS TSSLRRSASA VDCRRSSSSM SSRSHSHSGK
KNKGKKKKRS HSSESDSSDE DRSSKKDSSK NKGKKSKKTS KKESSSSSSS LDSESDSESG
SSSGASTISY QSTNSVKRAP GHQASSPEGE REVGTPAEGQ PPPNKKEEKN RKKKVDNLMM
KYLYRPDSD
//
