MYO1G_CHICK
ID MYO1G_CHICK Reviewed; 1007 AA.
AC Q5ZMC2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Unconventional myosin-Ig;
GN Name=MYO1G; ORFNames=RCJMB04_2i22;
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 [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Unconventional myosin required during immune response for
CC detection of rare antigen-presenting cells by regulating T-cell
CC migration. Unconventional myosins are actin-based motor molecules with
CC ATPase activity and serve in intracellular movements. Acts as a
CC regulator of T-cell migration by generating membrane tension, enforcing
CC cell-intrinsic meandering search, thereby enhancing detection of rare
CC antigens during lymph-node surveillance, enabling pathogen eradication.
CC {ECO:0000250|UniProtKB:Q5SUA5}.
CC -!- SUBUNIT: Interacts with calmodulin; via its IQ motifs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5SUA5};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q5SUA5}. Cell
CC projection, phagocytic cup {ECO:0000250|UniProtKB:Q5SUA5}.
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; AJ719462; CAG31121.1; -; mRNA.
DR RefSeq; NP_001026132.1; NM_001030961.1.
DR AlphaFoldDB; Q5ZMC2; -.
DR SMR; Q5ZMC2; -.
DR STRING; 9031.ENSGALP00000009037; -.
DR GeneID; 420412; -.
DR KEGG; gga:420412; -.
DR CTD; 64005; -.
DR VEuPathDB; HostDB:geneid_420412; -.
DR eggNOG; KOG0164; Eukaryota.
DR InParanoid; Q5ZMC2; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q5ZMC2; -.
DR PRO; PR:Q5ZMC2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; ISS:UniProtKB.
DR GO; GO:0002456; P:T cell mediated immunity; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; ISS: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; 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; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Adaptive immunity; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Immunity; Lipid-binding; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1007
FT /note="Unconventional myosin-Ig"
FT /id="PRO_0000340319"
FT DOMAIN 9..696
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 699..728
FT /note="IQ"
FT DOMAIN 813..1006
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 573..595
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1007 AA; 114970 MW; 9AE171C2E5F88FE3 CRC64;
MTELEGPEFG KADFVLLDEV TMEHFMENLR LRFSKGRIYT YIGEVVVAMN PYQPLELYGP
SVVEQYRGRE LYERPPHLFA LADAAYKAMK RRAKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPTQRAE VERVKNGLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPTGGH
IYNYLLEKSR VLQQQPGERN FHSFYQLLLG APDALLASLH LQRDPTAYCY TQQGTQGSAG
GDDARGYRAV EEAMAVIGFT PEEVGAVQRI LAAILHLGNV QFVAEGEVAA LEAVEQLAVL
AQLTGTTPEQ LRQALLARTV ATGGGELIEK GHSPTEAAYG RDACAKAIYE RLFGWIVGRI
NASITARGYD VRQHGKSTVI GVLDIYGFEI FDTNSFEQFC INYCNEKLQQ LFIELILRQE
QAEYQREGIT WQNIEYFSNE PIVELVEQPH RGILALLDEA CLAVGTVTDA LFLANMDARL
GHHPHYSSRK LCPTDKTMEF DRDFRIKHYA GDVTYSVEGF LDKNKDTLFQ DFKRLLYNSM
DPVLRAMWPD GEQSITEVTK RPLTAATLFK NSIVALVENL ASKEPYYVRC IKPNDQKSPV
LFDEERCRHQ VAYLGLLENV RVLRAGFAYR QPYDRFLQRY KMTCEYTWPN HLMATDREAT
QTLLEQHGFQ DDVAYGHTKV FIRTPRTLFC LEQERAQLIP IIVLLLQKAW RGALARRWCR
YLRAAYAIMG YYKRHKVKAY LLELIRRFQG VRSMPDFGKS LAWPEPPAVL SRFQENSQQL
FRRWRARQIV KNIPPSDMAQ IRAKVAAMGA LHGLRKDWGC QRGWVRDYLS SASENPGLAL
PFAHRVQALR DKVHFGAVLF SSHVRKINRF NKSRDRAILI TDQHLYKLEP RKQYRVMREL
PLSMVTGLSV TSCRAQLVVF HTQNHDDLAV CLHKTQPRGD ERVGELVGVL LEHCRTTKRE
LQVHVSDRIQ LSLRGRKRLL TVETQPDVAA PDFRKSRDGF VLYWPGS
