MYO1A_CHICK
ID MYO1A_CHICK Reviewed; 1045 AA.
AC P47807; Q90573;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Unconventional myosin-Ia;
DE AltName: Full=Brush border myosin I;
DE Short=BBM-I;
DE Short=BBMI;
DE AltName: Full=Myosin I heavy chain;
DE Short=MIHC;
GN Name=MYO1A; Synonyms=MYHL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8681398; DOI=10.1002/cm.970320216;
RA Collins K., Matsudaira P.T.;
RT "Recombinant expression of the brush border myosin I heavy chain.";
RL Cell Motil. Cytoskeleton 32:151-161(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-1045, AND PROTEIN SEQUENCE OF 332-343 AND
RP 490-503.
RC TISSUE=Intestine;
RX PubMed=2687288; DOI=10.1083/jcb.109.6.2895;
RA Garcia A., Coudrier E., Carboni J., Anderson J., Vandekerckhove J.,
RA Mooseker M., Louvard D., Arpin M.;
RT "Partial deduced sequence of the 110-kD-calmodulin complex of the avian
RT intestinal microvillus shows that this mechanoenzyme is a member of the
RT myosin I family.";
RL J. Cell Biol. 109:2895-2903(1989).
RN [3]
RP 3D-STRUCTURE MODELING OF 699-731.
RX PubMed=8994973; DOI=10.1016/s0969-2126(96)00154-2;
RA Houdusse A., Silver M., Cohen C.;
RT "A model of Ca(2+)-free calmodulin binding to unconventional myosins
RT reveals how calmodulin acts as a regulatory switch.";
RL Structure 4:1475-1490(1996).
CC -!- FUNCTION: Could play an important role in morphogenesis and function of
CC intestinal microvilli.
CC -!- TISSUE SPECIFICITY: Intestine.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; U04049; AAB38373.1; -; mRNA.
DR EMBL; X58479; CAA41388.1; -; mRNA.
DR PIR; A33620; A33620.
DR RefSeq; NP_990494.1; NM_205163.1.
DR AlphaFoldDB; P47807; -.
DR SMR; P47807; -.
DR STRING; 9031.ENSGALP00000007526; -.
DR PRIDE; P47807; -.
DR GeneID; 396072; -.
DR KEGG; gga:396072; -.
DR CTD; 4640; -.
DR VEuPathDB; HostDB:geneid_396072; -.
DR eggNOG; KOG0164; Eukaryota.
DR InParanoid; P47807; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; P47807; -.
DR PRO; PR:P47807; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR GO; GO:0045056; P:transcytosis; IMP:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 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; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Direct protein sequencing;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1045
FT /note="Unconventional myosin-Ia"
FT /id="PRO_0000123441"
FT DOMAIN 11..697
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 701..727
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 723..750
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 746..774
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 861..1044
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 574..596
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 46
FT /note="E -> Q (in Ref. 2; CAA41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="C -> S (in Ref. 2; CAA41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="T -> A (in Ref. 2; CAA41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="G -> A (in Ref. 2; CAA41388)"
FT /evidence="ECO:0000305"
FT CONFLICT 852..855
FT /note="CASE -> WPRQ (in Ref. 2; CAA41388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 119277 MW; 4C6888CA3FD669D0 CRC64;
MEATTSLLDA AAVGDLVMLD PLSEESLLRT LQERFSRGEI YTYIGEVVIS VNPYKPLPIY
TPEKVEEYHN CNFFAVKPHI YAIADDAYRS LRDRDRDQCI LITGESGAGK TEASKLVMSY
VAAVSSKGEE VDKVKEQLLQ SNPVLEAFGN AKTIRNDNSS RFGKYMDVEF DFKGDPLGGV
ISNYLLEKSR IVRHVKGERN FHIFYQLLAG GSAQLLQQLK LRPDCSHYGY LNHEKSVLPG
MDDAANFRAM QDAMAIIGFA PAEVTALLEV TAVVLKLGNV KLSSCFQASG MEASSITEPR
ELQEISQLIG LDPSTLEQAL CSRTVKVRDE SVLTALSVSQ GYYGRDALAK NIYSRLFDWL
VNRINTSIQV KPGKQRKVMG VLDIYGFEIF QDNGFEQFII NYCNEKLQQI FILMTLKEEQ
EEYVREGIQW TPVEFFDNSI ICDLIENSKV GILAMLDEEC LRPGTVNEDT FITKLNQIFA
SHKRYESKET LNAKHVTDVS LPLRCFRIHH YAGKVTYNVT GFIEKNNDLL FRDLSQAMWA
ARHTLLRSLF PEGDPQRPSL KLPPTTGSQF KASVATLMKN LYSKNPNYIR CIKPNDTKTA
MLFTPDLVLA QVRYLGLMEN VRVRRAGYAF RQLYQPFLER YKMLSRKTWP RWTGGDREGA
EVLLAELKFP PEELAYGHTK IFIRSPRTLF DLEKRRQQRV AELATLIQKM FRGWCCRKRY
QLMRKSQILI SAWFRGHMQR NRYKQMKRSV LLLQAYARGW KTRRMYRRYF RSDACTRLSN
FIYRRMVQKY LMGLQKNLPP MAVLDRTWPP APYKFLSDAN QELKSIFYRW KCKKYREQLT
PQQRAMLQAK LCASELFKDK KALYAQSLQQ PFRGEYLGLT QNRKYQKLQA VAKDKLVMAE
AVQKVNRANG KTVPRLLLLT TEHLVLADPK AAQPKMVLSL CDIQGASVSR FSDGLLALHL
KETSTAGGKG DLLLVSPHLI ELVTRLHQTL MDATAQALPL SIADQFSTRF PKGDVAVTVV
ESAKGGGDVP VCKKRGSHKM EILVH
