MYS_PODCA
ID MYS_PODCA Reviewed; 692 AA.
AC Q05000;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Myosin heavy chain;
DE Flags: Fragment;
OS Podocoryna carnea (Hydrozoan).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Filifera; Hydractiniidae; Podocoryna.
OX NCBI_TaxID=6096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8104835; DOI=10.1111/j.1432-0436.1993.tb00654.x;
RA Schuchert P., Reber-Mueller S., Schmid V.;
RT "Life stage specific expression of a myosin heavy chain in the hydrozoan
RT Podocoryne carnea.";
RL Differentiation 54:11-18(1993).
CC -!- FUNCTION: Myosin is a protein that binds to F-actin and has ATPase
CC activity that is activated by F-actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- DEVELOPMENTAL STAGE: Only present in the striated muscle cells of the
CC medusa stage.
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DR EMBL; X69057; CAA48795.1; -; mRNA.
DR AlphaFoldDB; Q05000; -.
DR SMR; Q05000; -.
DR PRIDE; Q05000; -.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.370; -; 5.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF01576; Myosin_tail_1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Thick filament.
FT CHAIN <1..692
FT /note="Myosin heavy chain"
FT /id="PRO_0000123386"
FT REGION <1..692
FT /note="Rodlike tail"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..670
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 692 AA; 77884 MW; A1BD21EC921F33C3 CRC64;
KVSQLEDDLT TSEAKNTKAA SRSGGLAKQL ADAEHKLGLA TKNIKSLEGA LSDAKSAAED
ESKGKHDNHQ KLQNALSEIE ALTEQLDEEQ ASRQDLQNKF SRANADAQQW KNKYDTDGAS
RVEELEDAKR KLANRVQEME EALAAAESKA ASMEKVKNRM NEEVEDLLLD LEKAQAQASN
LEKKQKKVDQ QINEWKLKCD EIQADLDKAQ RDARGYSTEL LKVRTASEDT IEKYDALKKE
NRALSAELQS VTEQLSDGGK NSAEVEKLRR KLGMENEELQ IALEEAEAAL EQEEGKLLKV
QLEYTQLRQS SDRKLSEKDE ELEGLRKNHQ RQMESLQNTI DSESRSKAEQ QKLRKKYDAD
MMELESQLES SNRVAAESQK QMKKLQAQIK ELQSMIDDES RGRDDMRDSA SRSERRANDL
AVQLDEARVA LEQAERARKL AENEKSENSD RVAELQALYN NVANAKAEGD YHSLQEEIED
LENEAKASED KAQRAMAEVA RLMSELNSAQ EATSTAEKSR QLVSKQVADL QSRLEDAEAQ
GGKGLKNQLR KLEQRIMELE SDVDTEARKG ADAIKAARKS EKKVKELAFT IEDEHKRREP
AQDTADKLNQ KLKKMRMQLE EAEQQKSTWQ SKYKKAAVEL EDAEERCEAA EAALQKARQR
ARGASGSATR GASRAPSQPR TPRSKTARAG ED