ERID_HERER
ID ERID_HERER Reviewed; 1456 AA.
AC A0A1V0QSE4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=ABC-type transporter eriD {ECO:0000303|PubMed:28371074};
DE AltName: Full=Erinacine biosynthesis cluster protein D {ECO:0000303|PubMed:28371074};
GN Name=eriD {ECO:0000303|PubMed:28371074};
OS Hericium erinaceus (Lion's mane mushroom) (Hydnum erinaceus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Hericium.
OX NCBI_TaxID=91752;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=28371074; DOI=10.1002/anie.201700565;
RA Yang Y.L., Zhang S., Ma K., Xu Y., Tao Q., Chen Y., Chen J., Guo S.,
RA Ren J., Wang W., Tao Y., Yin W.B., Liu H.;
RT "Discovery and characterization of a new family of diterpene cyclases in
RT bacteria and fungi.";
RL Angew. Chem. Int. Ed. 56:4749-4752(2017).
RN [2]
RP FUNCTION.
RX PubMed=31535864; DOI=10.1021/jacs.9b08935;
RA Liu C., Minami A., Ozaki T., Wu J., Kawagishi H., Maruyama J.I., Oikawa H.;
RT "Efficient reconstitution of basidiomycota diterpene erinacine gene cluster
RT in ascomycota host Aspergillus oryzae based on genomic DNA sequences.";
RL J. Am. Chem. Soc. 141:15519-15523(2019).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of erinacines, cyathane-xylosides that show unique
CC biological activities, including leishmanicidal activity, stimulating
CC activity for nerve growth-factor synthesis, and agonistic activity
CC toward the kappa opioid receptor. {ECO:0000269|PubMed:28371074,
CC ECO:0000269|PubMed:31535864}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; KY683779; ARE72241.1; -; mRNA.
DR AlphaFoldDB; A0A1V0QSE4; -.
DR SMR; A0A1V0QSE4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1456
FT /note="ABC-type transporter eriD"
FT /id="PRO_0000452923"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1148..1168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1184..1204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1233..1253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1269..1289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1301..1321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1337..1357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1423..1443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 118..372
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 813..1056
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 849..856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1456 AA; 162910 MW; D36C04C111F5B31A CRC64;
MAENEKVTYG GALPPSPSTA DTEVAALARS MTNASRSSVY SPEKPDGTNP FLGTDDPRMD
PLSGKFEPER WTKAILQLQS SDPEGYPHHT AAVSFSDLSV YGYGRPTDHQ KTVGNYFLDI
PGLARDILGR KGQRIDILRN FEGVIRESEM LVVLGRPGSG CTTLLKTIAG ETHGFWITDN
SHINYQGISF KRMHKQFRGE VIYNAENDVH FPNMTVGQTL RFAAEARTPR TRLPGVSRSQ
WAEHMKDVVM SIFGLTHTVN TKVGNDFVRG VSGGERKRVS IAEVALSGSP LQCWDNSTRG
LDSATALEFV KSLRLSSKYA GATAVVAIYQ ASQAIYDLFD KVVVLYEGQQ IYFGRADRAK
QFFIDMGFEC PPRQTTADFL TSLTNPGECL PRPGFEGRVP RTADEFAAAW RNSRDRQELL
QEIERFNDEF PEDGEHLEKF KKARKLIQAK GSQSPYTLST PMQIRLCLKR AWQRFMADTS
NFLTSVIGNF ILALIISSIF YNLPQNTLSF YSRGALLFFA ILMNAFASSL EILQIYEQRP
IVEKHKRMAL YHPYADAIAS VLCDLPGKVI ASFAFNLVLY FMTNLRRTPG AFFTFYLFSL
MCILVMSMIF RTIGATSKTI SQAMAPSSVI LLALVIFTGF TIPTRDMLGW SRWINYINPI
GYAFESIMVN EFDGREYACG DFIPTGPGYT DVPATSRVCA SAGAVFGSDV VEGAAYIATA
YEYFPQHKWR NLGILFGFIA FFACTYLFAT EFIAASKSKG EVLVFRRGHV PLKKEGASED
EEAGTGSTGT RTQEEPVDKD ANIAGIQRQV ATFHWEDVIY DIKIKGQPRR ILDHVDGWVR
PGTLTALMGA SGAGKTTLLD TLANRVTMGV VEGKMQVDGH DRDSSFQRNT GYVQQQDLHL
QTSTVREAML FSARLRQPHT VPDAEKAAYV EEVIHLLEMQ KYADAIVGVP GEGLNVEQRK
RLTIGVELVA KPQLLLFLDE PTSGLDSQTA WSICTLLRKL ANNGQAILCT IHQPSAMLFQ
SFDRLLLLQR GGQTVYFGDI GENSRTIIDY FEGQGADPCP HSANPAEWML SVIGAAPGAV
AKRDYYEAWR GSEAYRAVKE ELRQMRENPK PISQESTDAL RVYAAPFHVQ LFHVTFRFYQ
QLYRTPSYIY SKIFLVAGSN LLIGFSFFNA HNTIQGLQNQ MYSVFMGLTV FGNLVNQIMP
HFVTQRSLYE VRERPSRAYS WVVFMLSNVL GELPWNTLAG VVLFFCWYYP VGMYRNAEVT
HAVTERGGLM FLLIWQFMLF TSTFAHMLIA GVDSDVTGGN IASLLFSLTF LFCGVLAGPS
GPNAFPRFWI FMYRLSPFTY LVEAMVSVGV ANAPAFCSDI EVRHFEPPSG ETCGQYLQQY
MSVNDGSLAN PNATADCQFC QQTTTNSFLT GIHSSYAHRW RNFGFLWVFI LFNIGMAVFF
YWLARVPKGS RVKKQK