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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
 
 
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