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Database: UniProt
Entry: A0A6P6UY12_COFAR
LinkDB: A0A6P6UY12_COFAR
Original site: A0A6P6UY12_COFAR 
ID   A0A6P6UY12_COFAR        Unreviewed;       889 AA.
AC   A0A6P6UY12;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   SubName: Full=Uncharacterized protein LOC113715437 {ECO:0000313|RefSeq:XP_027095436.1, ECO:0000313|RefSeq:XP_027095448.1};
GN   Name=LOC113715437 {ECO:0000313|RefSeq:XP_027095436.1,
GN   ECO:0000313|RefSeq:XP_027095448.1};
OS   Coffea arabica (Arabian coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=13443 {ECO:0000313|Proteomes:UP001652660, ECO:0000313|RefSeq:XP_027095448.1};
RN   [1] {ECO:0000313|Proteomes:UP001652660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=40002058; DOI=10.3390/foods14040614;
RG   RefSeq;
RA   Tenea G.N., Cifuentes V., Reyes P., Cevallos-Vallejos M.;
RT   "Unveiling the Microbial Signatures of Arabica Coffee Cherries: Insights
RT   into Ripeness Specific Diversity, Functional Traits, and Implications for
RT   Quality and Safety.";
RL   Foods 14:614-614(2025).
RN   [2] {ECO:0000313|RefSeq:XP_027095436.1, ECO:0000313|RefSeq:XP_027095448.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaves {ECO:0000313|RefSeq:XP_027095436.1,
RC   ECO:0000313|RefSeq:XP_027095448.1};
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   RefSeq; XP_027095436.1; XM_027239635.1.
DR   RefSeq; XP_027095448.1; XM_027239647.1.
DR   AlphaFoldDB; A0A6P6UY12; -.
DR   GeneID; 113715437; -.
DR   OrthoDB; 1047602at2759; -.
DR   Proteomes; UP001652660; Chromosome 1c.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080115; F:myosin XI tail binding; IEA:UniProtKB-ARBA.
DR   InterPro; IPR007656; GTD-bd.
DR   InterPro; IPR039306; MYOB.
DR   PANTHER; PTHR31448; MYOSIN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR31448:SF55; MYOSIN-BINDING PROTEIN 3-LIKE ISOFORM X1; 1.
DR   Pfam; PF04576; Zein-binding; 1.
DR   PROSITE; PS51775; GTD_BINDING; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP001652660};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          544..642
FT                   /note="GTD-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51775"
FT   REGION          244..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          578..644
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        247..259
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  98481 MW;  265A3B9C1961D783 CRC64;
     MAAMGNSSVR LRNHRRFMTL LTSAACEWFL IFMLFVDATL SYLLTKFAHY CNLQTPCLLC
     SRIEHVFGIN KHGYYRSLLC CNHREEISSL VYCHNHCKLA DVDTTCEDCL MSLARRNKSN
     SESCRFLVAK LGVDTDESGL KSLLLNKSVI SDSSGPRTCS CCNKILRVKS NAQRLLEVAP
     VGYGASKANV KPPLPRVPGR SRFSRRDSLK RLRDKFSGPS APCPGGSTCV DSLSHVGYTE
     LKITSDSESE VPFSDDDDAT STSHGNNNFG AESNIQLVTR KVPKALAGDS IPVNQNCQTP
     EPLPSLLDQP VQLESSEANH VGHLESGAFM KHGLEELNWI QSNPKPTTSA ALPELVSLDD
     IPQSVETDKP IAAFPQPSDL SILSELLSLN SVLSSSNVVK ISEKSAEATG CSVNGNSSLA
     KHKIGAGFTD DCNPTMSRNV NSANKSASTN KQKPEPDVLA EPHKTNDSGR VEEALRSPSQ
     ISSSNVDLSP KDRSPRAHCD ALLKSDALGS DAIDTVQMAA ALERHDSDHE SLDGISVKEI
     EGETLLERLK RQVDYDRRCM KAMFKELEEE RNAAAIAANQ AMAMITRLQE EKAALHMEAL
     QYLRMMEEQA EYDMEALEKA NDLLAEREKE VQDLEAEVEI YRNNILEGPE IDYHCNETSN
     AKAESKTGEK YHLLPVENGD IATDDSKSDN ALKGSDKPRQ LSNSELDFED EKLYISLCLE
     KLEKKFHHIS SNWVHINLAN GEFAEHATKR VEDDEKLPYD TQTQISHQKG ECALSLHNDL
     CAPNGISGGD VSAKLVQENQ LLCEESDYLD VSQENLSTNG GVRKLDTFES EFIDLKSRLE
     ALEMDRDIIK HALNSLRNGN DGLQFIQEIA YQLQELRKIE FKKRCLSIP
//
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