UniProt: A0A1S3SMS6

Database: UniProt
Entry: A0A1S3SMS6_SALSA

LinkDB:  A0A1S3SMS6_SALSA 
Original site:  A0A1S3SMS6_SALSA

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Ontology (12)   
   GO (12)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
   SMART (1)   
All databases (30)   

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ID   A0A1S3SMS6_SALSA        Unreviewed;      1271 AA.
AC   A0A1S3SMS6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Unconventional myosin-VI {ECO:0000256|ARBA:ARBA00015382};
DE   AltName: Full=Unconventional myosin-6 {ECO:0000256|ARBA:ARBA00030027};
GN   Name=LOC106610693 {ECO:0000313|RefSeq:XP_014065649.1};
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_014065649.1};
RN   [1] {ECO:0000313|RefSeq:XP_014065649.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014065649.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC       {ECO:0000256|ARBA:ARBA00004486}. Cell projection, microvillus
CC       {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane
CC       {ECO:0000256|ARBA:ARBA00004632}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle {ECO:0000256|ARBA:ARBA00004132}. Golgi apparatus, trans-Golgi
CC       network membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane
CC       protein {ECO:0000256|ARBA:ARBA00004150}. Membrane, clathrin-coated pit
CC       {ECO:0000256|ARBA:ARBA00004600}.
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_014065649.1; XM_014210174.1.
DR   AlphaFoldDB; A0A1S3SMS6; -.
DR   GeneID; 106610693; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
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:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd21759; CBD_MYO6-like; 1.
DR   CDD; cd22294; MYO6_MIU_linker; 1.
DR   CDD; cd01382; MYSc_Myo6; 1.
DR   CDD; cd21958; MyUb_Myo6; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; IPR049016; MYO6_lever.
DR   InterPro; IPR032412; Myosin-VI_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR036114; MYSc_Myo6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF745; UNCONVENTIONAL MYOSIN-VI; 1.
DR   Pfam; PF21521; MYO6_lever; 1.
DR   Pfam; PF16521; Myosin-VI_CBD; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
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.
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}; Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hearing {ECO:0000256|ARBA:ARBA00022740};
KW   Membrane {ECO:0000256|ARBA:ARBA00023176};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          2..53
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          57..770
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          650..672
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          933..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1271 AA;  147000 MW;  1CAAC1A8FC182C63 CRC64;
     MEDGKPVWAP HPTDGFQLGM IVDIGAGVLT IEPFNRKGKT FLASMNQVFP AEEDVNKHME
     DNCSLMYLNE GTLLNNVRVR YSKDKIYTYV ANILIAVNPY NDIPKLYAPE TIKSYQGRSL
     GTLPPHVYAI ADKAYRDMRV LKMSQSIIVS GESGAGKTEN TKFVLRYLTT SYGTGQDIDE
     RIVQANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKNKV VGGFVSHYLL EKSRICMQSK
     EERNYHIFYR LCAGASEDIR QRLHLDSPDS FRYLNRGCTR YFASKDTDKQ IMQNRKSPEH
     VKLGALKDPL LDDQGDFNRM CGAMKKIGLD DTEKLDLFRV VAGVLHLGNI DFEETGSTSG
     GCILMNQSSQ KLAYCADLLG LDQEDLRVSL TTRVMLTTAG GAKGTVIKVP LRVEQANNAR
     DALAKAVYSC LFDHVVRRVN QCFPFKTSSN FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL
     QQFFNERILK EEQELYQREG LGVNEVHYVD NQDCIDLVEA KLVGILDILD EENRLPQPSD
     HHFANTIHSQ HKDHFRLTVP RKSKLAVHRN VRDDEGFIVR HFAGAVCYET IQFVEKNNDA
     LHMSLESLVC ESKDKFVREL FENSNNSKDS KQKAGKLSFI SVGNKFKTQL NLLLEKLRST
     GSSFIRCVKP NLKMVSHQFE GAQILSQLQC SGMVSVLDLM QGGFPSRAPF HELYNMYKQY
     MPDKLTRLDP RLFCKALFKA LGLNENDYKF GLTRVFFRPG KFAEFDQIMK SDPDHLAELV
     KKVNQWLVIS RWKKVQWCAL SVIKLKEKMK YRASALIKIQ KTVRMWLCKR KHKPRIDGMV
     KVRNLKTRME RFNEVVGALK EGKQEMAKQI QELGASIDTL MAKIKATVMT RKEIDQEYQG
     LVKRSEQLLS SMQKKKQEEE EMERLRRIEE EMAQERRRRE EEDQRRQKEE DDRRMKLEME
     HKRKQEEEER KRREEEERIM QAEMDIQIAL EREEDAQRSA MLEQEKRDRE LAMRIAQSEA
     ELITDEALMD LSLRSAGGLQ NLKAITMEEM AQLLAWGPQV QALKAAGVRK YDLSKWKYAE
     LRDVINTSCD IELLAACREE FHRRLKVYHA WKSKNKKRDT ATEQRAPKSI TDYAQQNPAP
     AVAAQQQEIA MNRQQRYFRI PFIRPGDQYK DPQNKKKGWW YAHFDGPWIA RQMELHPDKQ
     PILLVAGKDD MEMCELSLEE TGLTTKRGAE ILPRQFEEIW ERCNGIMYLR SAIESRQARP
     TYATAMLQNL L
//

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