11S1_CARIL
ID 11S1_CARIL Reviewed; 505 AA.
AC B5KVH4;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=11S globulin seed storage protein 1 {ECO:0000305};
DE AltName: Full=11S legumin {ECO:0000303|PubMed:21718052};
DE AltName: Full=Allergen Car i 4 {ECO:0000303|PubMed:21718052, ECO:0000303|PubMed:28121438};
DE AltName: Full=Pec11S-1 {ECO:0000303|PubMed:21718052};
DE AltName: Allergen=Car i 4.0101 {ECO:0000305};
DE Contains:
DE RecName: Full=11S globulin seed storage protein 1 acidic chain {ECO:0000305};
DE Contains:
DE RecName: Full=11S globulin seed storage protein 1 basic chain {ECO:0000305};
DE Flags: Precursor;
OS Carya illinoinensis (Pecan).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Carya.
OX NCBI_TaxID=32201 {ECO:0000312|EMBL:ABW86978.1};
RN [1] {ECO:0000312|EMBL:ABW86978.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-41; 79-101; 102-122;
RP 104-122; 188-212; 257-269; 274-281; 368-392 AND 460-474, 3D-STRUCTURE
RP MODELING, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, IDENTIFICATION
RP BY MASS SPECTROMETRY, ALLERGEN, AND REGIONS.
RX PubMed=21718052; DOI=10.1021/jf2017447;
RA Sharma G.M., Irsigler A., Dhanarajan P., Ayuso R., Bardina L.,
RA Sampson H.A., Roux K.H., Sathe S.K.;
RT "Cloning and characterization of an 11S legumin, Car i 4, a major allergen
RT in pecan.";
RL J. Agric. Food Chem. 59:9542-9552(2011).
RN [2]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=28121438; DOI=10.1021/acs.jafc.6b04199;
RA Mattison C.P., Rai R., Settlage R.E., Hinchliffe D.J., Madison C.,
RA Bland J.M., Brashear S., Graham C.J., Tarver M.R., Florane C.,
RA Bechtel P.J.;
RT "RNA-Seq Analysis of Developing Pecan (Carya illinoinensis) Embryos Reveals
RT Parallel Expression Patterns among Allergen and Lipid Metabolism Genes.";
RL J. Agric. Food Chem. 65:1443-1455(2017).
CC -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC ECO:0000305|PubMed:21718052, ECO:0000305|PubMed:28121438}.
CC -!- SUBUNIT: Homohexamer (By similarity). Each subunit is composed of an
CC acidic and a basic chain derived from a single precursor and linked by
CC a disulfide bond (PubMed:21718052). {ECO:0000250|UniProtKB:A0A1L6K371,
CC ECO:0000269|PubMed:21718052}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level)
CC (PubMed:21718052). Expressed in seeds (PubMed:28121438).
CC {ECO:0000269|PubMed:21718052, ECO:0000269|PubMed:28121438}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation
CC (PubMed:21718052). Expressed during embryonic development including the
CC water, gel, dough and mature nut stages in the nut cavity tissues
CC including the contents of the central vacuole, endosperm, embryo,
CC placenta, seed coat, ovary packing tissue, developing fruit and
CC cotyledon lobes. Expression increases during the transition from water
CC to gel stage, levels off or decreases slightly from the gel to dough
CC stage and increases again from the dough to mature stage
CC (PubMed:28121438). {ECO:0000269|PubMed:21718052,
CC ECO:0000269|PubMed:28121438}.
CC -!- INDUCTION: Up-regulated during nut development.
CC {ECO:0000269|PubMed:28121438}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC binds to IgE in 57% of the 28 patients tested allergic to pecan nuts.
CC Acidic chain is more immunoreactive than the basic chain.
CC {ECO:0000269|PubMed:21718052}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR EMBL; EU113051; ABW86978.1; -; mRNA.
DR AlphaFoldDB; B5KVH4; -.
DR SMR; B5KVH4; -.
DR Allergome; 8299; Car i 4.
DR Allergome; 8300; Car i 4.0101.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0048316; P:seed development; IEP:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
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; Direct protein sequencing; Disulfide bond; IgE-binding protein;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..316
FT /note="11S globulin seed storage protein 1 acidic chain"
FT /evidence="ECO:0000250|UniProtKB:Q2TPW5, ECO:0000255"
FT /id="PRO_0000448540"
FT CHAIN 317..505
FT /note="11S globulin seed storage protein 1 basic chain"
FT /evidence="ECO:0000250|UniProtKB:Q2TPW5"
FT /id="PRO_0000448541"
FT DOMAIN 42..255
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 329..478
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 118..132
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21718052"
FT REGION 193..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..219
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21718052"
FT REGION 238..249
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21718052"
FT REGION 282..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 316..321
FT /note="NGXEET; peptidase recognition motif"
FT /evidence="ECO:0000250|UniProtKB:Q2TPW5"
FT COMPBIAS 201..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 37..70
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT DISULFID 113..323
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000250|UniProtKB:P04776"
SQ SEQUENCE 505 AA; 58016 MW; 4B4A57816D3D6D7E CRC64;
MAKPILLSIY LCLIIVALFN GCLAQSGGRQ QHKFGQCQLN RLDALEPTNR IEAEAGVIES
WDPNHQQLQC AGVAVVRRTI EPNGLLLPHY SNAPQLVYIA RGRGITGVLF PGCPETFEES
QRQSQQGQRR EFQQDRHQKI RHFREGDIIA FPAGVAHWCY NDGSSPVVAI FLLDTHNNAN
QLDQNPRNFY LAGNPDDEFR PQGQQEYEQH RRQQQHQQRR GEHGEQQRDL GNNVFSGFDA
EFLADAFNVD TETARRLQSE NDHRGSIVRV EGRQLQVIRP RWSREEQEHE ERKERERERE
SESERRQSRR GGRDDNGLEE TICTLSLREN IGDPSRADIY TEEAGRISTV NSHNLPILRW
LQLSAERGAL YSDALYVPHW NLNAHSVVYA LRGRAEVQVV DNFGQTVFDD ELREGQLLTI
PQNFAVVKRA RDEGFEWVSF KTNENAMVSP LAGRTSAIRA LPEEVLVNAF QIPREDARRL
KFNRQESTLV RSRSRSSRSE RRAEV
