CONA1_LUPAN
ID CONA1_LUPAN Reviewed; 506 AA.
AC F5B8V6; Q96475;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Conglutin alpha 1 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an alpha-conglutin {ECO:0000305};
DE Contains:
DE RecName: Full=Conglutin alpha 1A subunit {ECO:0000250|UniProtKB:P04347};
DE Contains:
DE RecName: Full=Conglutin alpha 1B subunit {ECO:0000250|UniProtKB:P04347};
DE Flags: Precursor;
GN Name=CONALPHA {ECO:0000303|PubMed:9247543};
GN ORFNames=TanjilG_28353 {ECO:0000312|EMBL:OIW11262.1};
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 267-397, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Unicrop;
RX PubMed=9247543; DOI=10.1023/a:1005868105651;
RA Ilgoutz S.C., Knittel N., Lin J.M., Sterle S., Gayler K.R.;
RT "Transcription of genes for conglutin gamma and a leginsulin-like protein
RT in narrow-leafed lupin.";
RL Plant Mol. Biol. 34:613-627(1997).
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 -!- TISSUE SPECIFICITY: Expressed in developing cotyledons and in the
CC embryonic axis of germinating seeds. {ECO:0000269|PubMed:9247543}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during seed development.
CC {ECO:0000269|PubMed:21457583, ECO:0000269|PubMed:9247543}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ670406; AEB33709.1; -; mRNA.
DR EMBL; CM007365; OIW11262.1; -; Genomic_DNA.
DR EMBL; U74384; AAC49787.1; -; mRNA.
DR AlphaFoldDB; F5B8V6; -.
DR SMR; F5B8V6; -.
DR STRING; 3871.F5B8V6; -.
DR Allergome; 7697; Lup an alpha_Conglutin.
DR EnsemblPlants; OIW11262; OIW11262; TanjilG_28353.
DR Gramene; OIW11262; OIW11262; TanjilG_28353.
DR Proteomes; UP000188354; Chromosome LG05.
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; Glycoprotein; Reference proteome;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..506
FT /note="Conglutin alpha 1"
FT /id="PRO_5011015128"
FT CHAIN 20..321
FT /note="Conglutin alpha 1A subunit"
FT /evidence="ECO:0000250|UniProtKB:P04347"
FT /id="PRO_0000446133"
FT CHAIN 322..506
FT /note="Conglutin alpha 1B subunit"
FT /evidence="ECO:0000250|UniProtKB:P04347"
FT /id="PRO_0000446134"
FT DOMAIN 36..235
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 334..483
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..64
FT /evidence="ECO:0000250|UniProtKB:P04347"
FT DISULFID 107..328
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P04347"
FT CONFLICT 273
FT /note="Missing (in Ref. 3; AAC49787)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="RE -> LS (in Ref. 3; AAC49787)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..390
FT /note="VNAN -> GNAK (in Ref. 3; AAC49787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57793 MW; 0C785F3695C12F8B CRC64;
MANKLLALSL FLLFSGCFAS TFRQQPQQNE CQFQRLNALE PDNSVKSEAG TIETWNPNND
QLRCAGVALS RCTIQRNGLR RPFYTNAPQE IYIQQGRGIF GLIFPGCRET YEEPQEQEQG
QGPRPQDRHQ KVEHFREGDI IAVPTGVPFW MYNNEQTPVI AITLIDTTNL DNQLDQIPRR
FYLSGNQEQE FLQYQQKEGG QGQQQEGGNE GGNVLSGFND EFLEEAFSVD REIVRNIKGK
NDDREGSIVE VKEGLKVISP PTLRPRQGRE EEEEEEEEEE ERRGDRRRHR PHHHEEEEEE
EEWSHQVRRV RRPHHHREDR NGLEETLCTL KLRHNIGQST SPDAYNPQAG RLKTLTSLDF
PILRWLGLAA EHGSIYKNAM FVPYYNVNAN SILYVLNGSA WFQVVDCSGN AVFNGELNEG
QVLTIPQNYA VAIKSLDDNF SYVAFKTNDI PQIAALAGLT SSIRALPLDV VAHAFNLDRD
QARQLKNNNP YKFLVPPPQS QLRAVA
