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CONA2_LUPAN
ID   CONA2_LUPAN             Reviewed;         643 AA.
AC   F5B8V7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Conglutin alpha 2 {ECO:0000303|PubMed:21457583};
DE   AltName: Allergen=Lup an alpha-conglutin {ECO:0000305};
DE   Contains:
DE     RecName: Full=Conglutin alpha 2A subunit {ECO:0000250|UniProtKB:P04347};
DE   Contains:
DE     RecName: Full=Conglutin alpha 2B subunit {ECO:0000250|UniProtKB:P04347};
DE   Flags: Precursor;
GN   ORFNames=TanjilG_32393 {ECO:0000312|EMBL:OIV90516.1};
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   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}.
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DR   EMBL; HQ670407; AEB33710.1; -; mRNA.
DR   EMBL; KV862168; OIV90516.1; -; Genomic_DNA.
DR   EMBL; CM007380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_019429051.1; XM_019573506.1.
DR   AlphaFoldDB; F5B8V7; -.
DR   SMR; F5B8V7; -.
DR   STRING; 3871.F5B8V7; -.
DR   EnsemblPlants; OIV90516; OIV90516; TanjilG_32393.
DR   GeneID; 109336727; -.
DR   Gramene; OIV90516; OIV90516; TanjilG_32393.
DR   KEGG; lang:109336727; -.
DR   OMA; PDNRVES; -.
DR   OrthoDB; 603461at2759; -.
DR   Proteomes; UP000188354; Chromosome LG20.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 3.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..643
FT                   /note="Conglutin alpha 2"
FT                   /id="PRO_5010895118"
FT   CHAIN           23..457
FT                   /note="Conglutin alpha 2A subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT                   /id="PRO_0000446135"
FT   CHAIN           458..630
FT                   /note="Conglutin alpha 2B subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT                   /id="PRO_0000446136"
FT   DOMAIN          36..261
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          470..616
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          110..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        31..64
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
FT   DISULFID        107..464
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04347"
SQ   SEQUENCE   643 AA;  74194 MW;  8A18C45A9A727165 CRC64;
     MAKPCLFSFS LCLLLLSSLC LAERPERYKE CQLDRLNALE PDNRVESEGG VTETWNSNRP
     ELRCAGVAFE KHTIQPQGLH LPSYTNYPQL IFIVEGEGAL GISVPGCTET YEEAQQSQSS
     QDPRRRSSRS QSQEQEQQDS HQKIQYFREG DIIAIPPGIP YWTYNYGEQR LVAINLLDTT
     SLLNQLDPSP RRFYIAGNPE EEHPETQEQQ GQQREQQQGA GGRRRGKHQQ EQEEEGKNNV
     LSGFDPQFLT QAFNVDEEII NRLQNPDERL KQIVRVKRGL SIISPKSQEE EEEEEEEPRQ
     RGQPERREER REEEKEEEEE EDEPRSRERY ERQSRRRPGR QQGRQGEEQE EESESEQEGR
     GQQREWERTT RHRRAQGEEG EEEEEETSTR VRRQQGRGRG QEQGQEQGQE QEQEEEQQEG
     RRGRHGGRGR RSGQQREEEE EEQQQQQGRR KRQESRNGLE ETICTARLLE NIAKPSRADL
     YNPNAGRISS VNSLTLPILR WFQLSADYVN LYRNGIYAPH WNINANSVIF VTRGRGRVQV
     VNCQGNSVFN DDLRRGQLLV VPQNFVVAHQ AGDEGFEFIA FKTNDLAATS PVKQVFRGIP
     AEVLANAFGL RLNQVSQLKY SGNQGPLVSP QSESEDHTLP KVA
 
 
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