2SS8_HELAN
ID 2SS8_HELAN Reviewed; 141 AA.
AC P23110;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Albumin-8;
DE AltName: Full=Methionine-rich 2S protein;
DE AltName: Full=SFA8;
DE Flags: Precursor;
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 39-141.
RC TISSUE=Seed;
RX PubMed=1997318; DOI=10.1111/j.1432-1033.1991.tb15710.x;
RA Kortt A.A., Caldwell J.B., Lilley G.G., Higgins T.J.V.;
RT "Amino acid and cDNA sequences of a methionine-rich 2S protein from
RT sunflower seed (Helianthus annuus L.).";
RL Eur. J. Biochem. 195:329-334(1991).
RN [2]
RP PROTEIN SEQUENCE OF 39-141.
RC STRAIN=cv. Hybrid 246; TISSUE=Seed;
RX PubMed=8915004; DOI=10.1016/0014-5793(96)01117-9;
RA Egorov T.A., Odintsova T.I., Musolyamov A.K., Fido R., Tatham A.S.,
RA Shewry P.R.;
RT "Disulphide structure of a sunflower seed albumin: conserved and variant
RT disulphide bonds in the cereal prolamin superfamily.";
RL FEBS Lett. 396:285-288(1996).
RN [3]
RP STRUCTURE BY NMR OF 39-141, AND DISULFIDE BONDS.
RX PubMed=15170335; DOI=10.1021/bi0496900;
RA Pantoja-Uceda D., Shewry P.R., Bruix M., Tatham A.S., Santoro J., Rico M.;
RT "Solution structure of a methionine-rich 2S albumin from sunflower seeds:
RT relationship to its allergenic and emulsifying properties.";
RL Biochemistry 43:6976-6986(2004).
CC -!- FUNCTION: This is a 2S seed storage protein.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000269|PubMed:15170335}.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000305}.
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DR EMBL; X56686; CAA40015.1; -; mRNA.
DR PIR; S14259; S14259.
DR PDB; 1S6D; NMR; -; A=39-141.
DR PDBsum; 1S6D; -.
DR AlphaFoldDB; P23110; -.
DR SMR; P23110; -.
DR Allergome; 772; Hel a 2S Albumin.
DR EvolutionaryTrace; P23110; -.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000617; Napin/2SS/CON.
DR PANTHER; PTHR35496; PTHR35496; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..25
FT PROPEP 26..38
FT /evidence="ECO:0000269|PubMed:1997318,
FT ECO:0000269|PubMed:8915004"
FT /id="PRO_0000032153"
FT CHAIN 39..141
FT /note="Albumin-8"
FT /id="PRO_0000032154"
FT DISULFID 49..100
FT /evidence="ECO:0000269|PubMed:15170335"
FT DISULFID 62..89
FT /evidence="ECO:0000269|PubMed:15170335"
FT DISULFID 90..132
FT /evidence="ECO:0000269|PubMed:15170335"
FT DISULFID 102..139
FT /evidence="ECO:0000269|PubMed:15170335"
FT CONFLICT 67
FT /note="M -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:1S6D"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1S6D"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1S6D"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:1S6D"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1S6D"
SQ SEQUENCE 141 AA; 16090 MW; 1E5723B9122C9BD4 CRC64;
MARFSIVFAA AGVLLLVAMA PVSEASTTTI ITTIIEENPY GRGRTESGCY QQMEEAEMLN
HCGMYLMKNL GERSQVSPRM REEDHKQLCC MQLKNLDEKC MCPAIMMMLN EPMWIRMRDQ
VMSMAHNLPI ECNLMSQPCQ M