MLOH1_HORVU
ID MLOH1_HORVU Reviewed; 544 AA.
AC O49873;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=MLO protein homolog 1;
GN Name=MLO-H1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Igri;
RA Panstruga R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in modulation of pathogen defense and leaf
CC cell death. Activity seems to be regulated by Ca(2+)-dependent
CC calmodulin binding and seems not to require heterotrimeric G proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The C-terminus contains a calmodulin-binding domain, which
CC binds calmodulin in a calcium-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MLO family. {ECO:0000305}.
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DR EMBL; Z95496; CAB08860.1; -; Genomic_DNA.
DR PIR; T05952; T05952.
DR AlphaFoldDB; O49873; -.
DR ExpressionAtlas; O49873; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR InterPro; IPR004326; Mlo.
DR PANTHER; PTHR31942; PTHR31942; 1.
DR Pfam; PF03094; Mlo; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding; Membrane; Pathogenesis-related protein; Plant defense;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="MLO protein homolog 1"
FT /id="PRO_0000209929"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 437..458
FT /note="Calmodulin-binding"
FT REGION 485..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 60875 MW; D4FBCDD2A2A87796 CRC64;
MAGPAGGREL SDTPTWAVAV VCAVMILVSV AMEHALHKLG HWFHKWRKKA LGEALEKMKA
ELMLVGFISL LLIVTQDPVS RICISKEAGE KMLPCKPYDG AGGGKGKDNH RRLLWLQGES
ETHRRFLAAP AGVDVCAKQG KVALMSAGSM HQLHIFIFVL AVFHVLYSVV TMTLSRLKMK
QWKKWESETA SLEYQFANDP SRCRFTHQTT LVRRHLGLSS TPGVRWVVAF FRQFFTSVTK
VDYLTLRQGF INAHLSQGNR FDFHKYIKRS LEDDFKVVVR ISLKLWFVAV LILFLDFDGI
GTLLWMSVVP LVILLWVGTK LEMVIMEMAQ EIHDRESVVK GAPAVEPSNK YFWFNRPDWV
LFLMHLTLFQ NAFQMAHFVW TVATPGLKKC YHEKMAMSIA KVVLGVAAQI LCSYITFPLY
ALVTQMGSHM KRSIFDEQTA KALTNWRKMA KEKKKARDAA MLMAQMGGGA TPSVGSSPVH
LLHKAGARSD DPQSVPASPR AEKEGGGVQH PARKVPPCDG WRSASSPALD AHIPGADFGF
STQR