ID A0A2K6TT85_SAIBB Unreviewed; 1923 AA.
AC A0A2K6TT85;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Myosin heavy chain 14 {ECO:0000313|Ensembl:ENSSBOP00000022876.1};
GN Name=MYH14 {ECO:0000313|Ensembl:ENSSBOP00000022876.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000022876.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000022876.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 39432.ENSSBOP00000022876; -.
DR Ensembl; ENSSBOT00000039728.1; ENSSBOP00000022876.1; ENSSBOG00000027842.1.
DR GeneTree; ENSGT00940000158808; -.
DR OMA; QXELAAS; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016460; C:myosin II complex; IEA:Ensembl.
DR GO; GO:0097513; C:myosin II filament; IEA:Ensembl.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 3.
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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF31; MYOSIN-14; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 7.
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};
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:UP000233220}.
FT DOMAIN 51..101
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 105..819
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..720
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1066..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1835..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 859..942
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1385..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1923 AA; 217933 MW; 69D8FB321DEEC6DD CRC64;
MAAVTMSLPG RKATPRPGPV PEAAQPFLFT PRGPSAGVGP GSGTSPQVEW TARRLVWVPS
ELHGFEAAAL RDEGEEEAEV ELAESGRRLR LPRDQIQRMN PPKFSKAEDM AELTCLNEAS
VLHNLRERYY SGLIYTYSGL FCVVINPYKQ LPIYTEAIVE MYRGKKRHEV PPHVYAVTEG
AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAA SPKGRKEPGV PASASTVSYG
ELERQLLQAN PILEAFGNAK TVKNDNSSRF GKFIRINFDV AGYIVGANIE TYLLEKSRAI
RQAKDECSFH IFYQLLGGAG EQLKADLLLE PCSHYRFLTN GPSSSPGQER ELFQETLESL
RVLGFTHEEI ILLMGSWCLS PSAAQKLCHL LGLGVTDFSR ALLTPRIKVG RDYVQKAQTK
EQADFALEAL AKATYERLFR WLVLRLNRAL DRSPRQGASF LGILDIAGFE IFQLNSFEQL
CINYTNEKLQ QLFNHTMFVL EQEEYQREGI PWTFLDFGLD LQPCIDLIER PANPPGLLAL
LDEECWFPKA TDKSFVEKVA QEQGGHPKFQ RPRHLRDQAD FSVLHYAGKV DYKANEWLMK
NMDPLNDSVA ALLHQSTDRL TAEIWKDEHG GFQQFAFLGS FPPSPPGSAG KCSSAVSPPG
VEGIVGLEQV SSLGDGPPGG RPRRGMFRTV GQLYKESLSR LMATLSNTNP SFVRCIVPNH
EKRAGKLEPR LVLDQLRCNG VLEGIRICRQ GFPNRILFQE FRQRKIFFRA GVLAQLEEER
DLKVTDIIVS FQAAARGYLA RRAFQKRQQQ QSALRVMQRN CAAYLKLRHW QWWRLFTKVK
PLLQVTRQDD VLQARAQELQ KAQELQQQSL REVGELRSRM AELEEERTRL AEQLRAEAEL
CAEAEETRGR LAARKQELEL VVSELEARVG EEEECSRQLQ TEKRRLQQHI QVWPPACPAD
PSVHPHLCFS KPCGARQKLQ LEKVTTEAKM KKFEEDLLLL EDQNSKLSKE RKLLEDRLAE
FSSQAAEEEE KVKSLNKLRL KYEATIADME DRLRKEEKSR QELEKLKRRL DGESSELQEQ
MAEQQQRAED LRSQLGRKEE ELQAALARAE DEGGARAQLL KSLREVQAAL AEAQEDVEAE
RVARAKAEKQ RRDLGEELEA LRGELEDTLG STNAQQELRS KREQEVTELK KALEEETRIH
EAAVQELRQR HGQALGELAE QLEQARRGKG AWEKTRLALE AEVSELRVEL SSLQTARQEG
EQRRRRLESQ LQEVQGRAGD GERARAETAE KLQRAQAELE NVSGALNEAE SKAIRLSKEL
SSMDAQLHDA QELLQEETRA KLALGSRVRA MEAEAAGLRE QLEEEAAARE RAGRELQTAQ
AQLSEWRRRQ EEEAGALEAG EEARRRAARE AEALTQRLAE KTETVDRLER GRRRLQQELD
DATVDLEQQR QLVSTLEKKQ RKFDQVGTSV HPAAEPASPS VLPVHELERA CRVAEQAAND
LRAQVTELED ELTAAEDAKL RLEVTVQALK TQHERDLQGR DEAGEERRRQ LAKQLRDAEV
ERDEERKQRA LAVAARKKLE GELEELKAQL VSAGQGKEEA VKQLRKMQAQ MKELWREVEE
SRSSREEIFA QNRESDKRLK GLEAEVLRLQ EELAASDRAR RQAQQDRDEM ADEVANGNLS
KAAILEEKRQ LEGRLGQLEE ELEEEQSNSE LLNDRYRKLL LQVESLTSEL SAERSFSAKA
ESGRQQLERQ IQELRGRLGE EDAGARARQK MTIAALESKL AQAEEQLEQE SSSGLSRREE
VMAVPGDVTW APALAKLEKG NLRVKQLKRQ LEEAEEEASR AQAGRRRLQR ELEDVTESAE
SMNREVTTLR NRLRRGPLTF TTRTVRQVFR LEEGVASDEE AEDAEPGSGP SPEPEGSPSA
HPQ
//
