AHY3_ARAHY
ID AHY3_ARAHY Reviewed; 484 AA.
AC Q647H2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Arachin Ahy-3;
DE Contains:
DE RecName: Full=Arachin Ahy-3 chain alpha;
DE Contains:
DE RecName: Full=Arachin Ahy-3 chain beta;
DE Flags: Precursor;
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818;
RN [1] {ECO:0000312|EMBL:AAU21492.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Shanyou 523 {ECO:0000269|Ref.1};
RC TISSUE=Cotyledon {ECO:0000269|Ref.1};
RX AGRICOLA=IND43739496; DOI=10.1016/j.plantsci.2005.04.010;
RA Yan Y.-S., Lin X.-D., Zhang Y.-S., Wang L., Wu K., Huang S.-Z.;
RT "Isolation of peanut genes encoding arachins and conglutins by expressed
RT sequence tags.";
RL Plant Sci. 169:439-445(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 316-354; 412-423 AND 428-436, AND REPRESSION BY WATER
RP STRESS.
RC STRAIN=cv. M13 {ECO:0000269|Ref.2}; TISSUE=Seed {ECO:0000269|Ref.2};
RA Katam R., Vasanthaiah H.K.N., Basha S.M., McClung S.;
RT "Suppression of seed storage proteins upon water stress in Arachis hypogea
RT var. M-13 seeds.";
RL Submitted (MAR-2007) to UniProtKB.
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 {ECO:0000305}.
CC -!- INDUCTION: Repressed by water stress. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000255}.
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DR EMBL; AY722687; AAU21492.1; -; mRNA.
DR AlphaFoldDB; Q647H2; -.
DR SMR; Q647H2; -.
DR Allergome; 52; Ara h 3.
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 Direct protein sequencing; Disulfide bond; Seed storage protein; Signal;
KW Storage protein.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..294
FT /note="Arachin Ahy-3 chain alpha"
FT /evidence="ECO:0000250|UniProtKB:P04405, ECO:0000255"
FT /id="PRO_0000287419"
FT PROPEP 295..298
FT /evidence="ECO:0000250|UniProtKB:P04405"
FT /id="PRO_0000287420"
FT CHAIN 299..478
FT /note="Arachin Ahy-3 chain beta"
FT /evidence="ECO:0000250|UniProtKB:P04405"
FT /id="PRO_0000287421"
FT PROPEP 479..484
FT /evidence="ECO:0000250|UniProtKB:P04405"
FT /id="PRO_0000287422"
FT DOMAIN 35..253
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 311..460
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 208..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 32..65
FT /evidence="ECO:0000250"
FT DISULFID 108..305
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000250|UniProtKB:P04405"
SQ SEQUENCE 484 AA; 54569 MW; 5A3E950752E89D2D CRC64;
MAKLLALSVC FCFLVLGASS VTFRQQGEEN ECQFQRLNAQ RPDNCIESEG GYIETWNPNN
QEFQCAGVAL SRFVLRRNAL RRPFYSNAPQ EIFIYQGSGY FGLIFPGCPG TFEEPIQGSE
QFQRPSRHFQ GQDQSQRPLD THQKVHGFRE GDLIAVPHGV AFWIYNDQDT DVVAISVLHT
NSLHNQLDQF PRRFNLAGKQ EQEFLRYQQR SGRQSPKGEE QEQEQENEGG NVFSGFSTEF
LSHGFQVNED IVRNLRGENE REEQGAIVTV KGGLSILVPP EWRQSYQQPG RGDKDFNNGI
EETICTATVK MNIGKSTSAD IYNPQAGSVR TVNELDLPIL NRLGLSAEYG SIHRDAMFVP
HYNMNANSMI YALHGGAHVQ VVDCNGNRVF DEELQEGQSL VVPQNFAVAA KSQSEHFLYV
AFKTNSRASI SNLAGKNSYM WNLPEDVVAN SYGLQYEQAR QLKNNNPFTF LVPPQDSQMI
RTVA