ID A0A3Q7TIW7_VULVU Unreviewed; 2006 AA.
AC A0A3Q7TIW7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Myosin-10 isoform X7 {ECO:0000313|RefSeq:XP_025861272.1};
GN Name=MYH10 {ECO:0000313|RefSeq:XP_025861272.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025861272.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025861272.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025861272.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025861272.1};
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 ---------------------------------------------------------------------------
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 RefSeq; XP_025861272.1; XM_026005487.1.
DR STRING; 9627.ENSVVUP00000040446; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd14920; MYSc_Myh10; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 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:SF24; MYOSIN-10; 1.
DR Pfam; PF00612; IQ; 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; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 5.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 61..111
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 115..813
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 691..713
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1157..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1980..1995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2006 AA; 232420 MW; E0BFCC9910BFC8B6 CRC64;
MRRAPRRPGP GAGANERPSR GNCPWILLFT MAQRTGLEDP ERYLFVDRAV IYNPATQADW
TAKKLVWIPS ERHGFEAASI KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVEDM
AELTCLNEAS VLHNLKDRYY SGLIYTYSGL FCVVINPYKN LPIYSENIIE MYRGKKRHEM
PPHIYAISES AYRCMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS SHKGRKDHNI
PGELERQLLQ ANPILESFGN AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR
AVRQAKDERT FHIFYQLLSG AGEHLKSDLL LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM
EAMHIMGFSH EEILSMLKVV SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM
EFTRAILTPR IKVGRDYVQK AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ
GASFIGILDI AGFEIFELNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWSFID
FGLDLQPCID LIERPANPPG VLALLDEECW FPKATDKTFV EKLVQEQGSH SKFQKPRQLK
DRADFCIIHY AGKVDYKADE WLMKNMDPLN DNVATLLHQS SDRFVAELWK DVDRIVGLDQ
VTGMTETAFG SAYKTKKGMF RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL
DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM
IRALELDPNL YRIGQSKIFF RAGVLAHLEE ERDLKITDII IFFQAVCRGY LARKAFAKKQ
QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK VKPLLQVTRQ EEELQAKDEE LLKVKERQTK
VEGELEEMER KHQQLLEEKN ILTEQLQAET ELFAEAEEMR ARLAAKKQEL EEILHDLESR
VEEEEERNQI LQNEKKKMQA HIQDLEEQLD EEEGARQKLQ LEKVTAEAKI KKMEEEILLL
EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE KAKNLAKIRN KQEVMISDLE ERLKKEEKTR
QELEKAKRKL DGETTDLQDQ IAELQAQIDE LKVQLAKKEE ELQGALARGD DETLHKNNAL
KVVRELQAQI AELQEDFESE KASRNKAEKQ KRDLSEELEA LKTELEDTLD TTAAQQELRT
KREQEVAELK KALEEETRSH EAQIQDMRQR HATALEELSE QLEQAKRFKA NLEKNKQGLE
TDNKELACEV KVLQQVKAES EHKRKKLDAQ VQELHAKVSE GDRLRVELAE KANKLQNELD
NVSSLLEEAE KKGIKFAKDA ASLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE
QQEEEEEARK NLEKQVLVLQ SQLADTKKKV DDDLGTIESL EEARKKLLKD VEALGQRLEE
KALAYDKLEK TKNRLQQELD DLTVDLDHQR QIASNLEKKQ KKFDQLLAEE KNISARYAEE
RDRAEAEARE KETKALSLAR ALEEALETKE EFERQNKQLR ADMEDLISSK DDVGKNVHEL
EKSKRALEQQ VEEMRTQLEE LEDELQATED AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK
KRLLVKQVRE LEAELEDERK QRALAVASKK KLEIDLKDLE AQIEAANKAR DEVIKQLRKL
QAQMKDYQRE LEEARASRDE IFAQSKESEK KLKSLEAEIL QLQEELASSE RARRHAEQER
DELADEIANS ASGKSALLDE KRRLEARIAQ LEEELEEEQS NMELLNDRFR KTTLQVDTLN
AELAAERSAA QKSDNARQQL ERQNKELKAK LQELEGAVKS KFKATISALE AKIGQLEEQL
EQEAKERAAA NKLVRRTEKK LKEIFMQVED ERRHADQYKE QMEKANARMK QLKRQLEEAE
EEATRANASR RKLQRELDDA TEANEGLSRE VSTLKNRLRR GGPISFSSSR SGRRQLHIEG
ASLELSDDDT ESKTSDVNET QPPQSE
//
