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CONA3_LUPAN
ID   CONA3_LUPAN             Reviewed;         585 AA.
AC   F5B8V8; C9WC98;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Conglutin alpha 3 {ECO:0000303|PubMed:21457583};
DE   AltName: Allergen=Lup an alpha-conglutin {ECO:0000305};
DE   Contains:
DE     RecName: Full=Conglutin alpha 3A subunit {ECO:0000250|UniProtKB:P04347};
DE   Contains:
DE     RecName: Full=Conglutin alpha 3B subunit {ECO:0000250|UniProtKB:P04347};
DE   Flags: Precursor;
GN   ORFNames=TanjilG_01206 {ECO:0000312|EMBL:OIW01699.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND ALLERGEN.
RC   STRAIN=cv. Tanjil; TISSUE=Seed;
RX   PubMed=21457583; DOI=10.1186/1471-2229-11-59;
RA   Foley R.C., Gao L.-L., Spriggs A., Soo L.Y.C., Goggin D.E., Smith P.M.C.,
RA   Atkins C.A., Singh K.B.;
RT   "Identification and characterisation of seed storage protein transcripts
RT   from Lupinus angustifolius.";
RL   BMC Plant Biol. 11:59-59(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil; TISSUE=Seedling;
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 57-585.
RC   STRAIN=cv. Merrit;
RA   Smith P.M., Goggin D.E., Cameron E.C.;
RT   "Cloning of Lupinus angustifolius seed storage protein genes.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBUNIT.
RC   STRAIN=cv. Zeus;
RX   PubMed=22264085; DOI=10.1021/jf2042592;
RA   Czubinski J., Dwiecki K., Siger A., Kachlicki P., Neunert G.,
RA   Lampart-Szczapa E., Nogala-Kalucka M.;
RT   "Release of flavonoids from lupin globulin proteins during digestion in a
RT   model system.";
RL   J. Agric. Food Chem. 60:1830-1836(2012).
CC   -!- FUNCTION: Sulfur-rich seed storage protein. This protein found in the
CC       seeds of many leguminous and non-leguminous plants is the source of
CC       sulfur-containing amino acids in seed meals.
CC       {ECO:0000269|PubMed:21457583}.
CC   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC       chain derived from a single precursor and linked by a disulfide bond
CC       (By similarity). Component of globulins complexes which accumulate in
CC       seeds (Probable). {ECO:0000250|UniProtKB:P04347,
CC       ECO:0000305|PubMed:22264085}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during seed development.
CC       {ECO:0000269|PubMed:21457583}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000305|PubMed:21457583}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACN39600.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; HQ670408; AEB33711.1; -; mRNA.
DR   EMBL; KV861864; OIW01699.1; -; Genomic_DNA.
DR   EMBL; CM007371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FJ263366; ACN39600.1; ALT_INIT; mRNA.
DR   RefSeq; XP_019462298.1; XM_019606753.1.
DR   RefSeq; XP_019462299.1; XM_019606754.1.
DR   RefSeq; XP_019462300.1; XM_019606755.1.
DR   AlphaFoldDB; F5B8V8; -.
DR   SMR; F5B8V8; -.
DR   STRING; 3871.F5B8V8; -.
DR   EnsemblPlants; OIW01699; OIW01699; TanjilG_01206.
DR   GeneID; 109361312; -.
DR   Gramene; OIW01699; OIW01699; TanjilG_01206.
DR   KEGG; lang:109361312; -.
DR   OMA; PHGKRVH; -.
DR   OrthoDB; 603461at2759; -.
DR   Proteomes; UP000188354; Chromosome LG11.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Reference proteome; Seed storage protein; Signal;
KW   Storage protein.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..585
FT                   /note="Conglutin alpha 3"
FT                   /id="PRO_5010895108"
FT   CHAIN           24..399
FT                   /note="Conglutin alpha 3A subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT                   /id="PRO_0000446137"
FT   CHAIN           400..572
FT                   /note="Conglutin alpha 3B subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT                   /id="PRO_0000446138"
FT   DOMAIN          37..258
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          412..558
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          113..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        32..65
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT   DISULFID        108..406
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT   CONFLICT        119
FT                   /note="Q -> R (in Ref. 3; ACN39600)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="Y -> C (in Ref. 3; ACN39600)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  67381 MW;  E12486240213BC4C CRC64;
     MANPFLLSLS LCLVLLYTSA CLGEGLDRFN ECQLDRLNAL EPDNRIESEG GVTETWNSNK
     PELRCAGVAF EKHTIEPKGL HLPSYTNYPQ IIMIVQGEGA LGISVPGCTE TFEEAQQSQS
     RQERRRGQRS QSQEQEDSHQ KIRHFREGDI LVIPPGTPYW TYNYGDEQLV AINLLDTTSL
     SNQLDPNPRR FYLAGNPEEE YPETQQQRQQ RQQHQRPSGR RHGQHQKEEE QEGKNNILSG
     FDPQFLSQAL NIDEDTVHKL QNPNERIKQI IRVEEGLGVI SPKWQEQEEE EEEKEEPRQR
     RRRERREERE EEEKEEEDEP RESRRHRGGH EEEEVEEERG RGRGGSEWKR TTRRRHTRGD
     EGQEEEETTT TTEERRRRRG GRGSRQEEEE EQSPPRSRNG LEETICTAIL RENIADPTRA
     DLYNPTAGRI STANSLTLPI LGWFQLSAEY VNLYRNGIYA PHWNINANSV IYVIRGRGRV
     QVVNSQGNSV FNDDLRRGQL LVVPQNFVVA HQAGDEGFEF IAFKTNDQAT TSPLKQVFRG
     IPAEVLANAF RLSLNQVSEL KYNGNHNPLV TPQSQSQDHN LVKVA
 
 
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