2SS_CUCMA
ID 2SS_CUCMA Reviewed; 141 AA.
AC Q39649;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=2S seed storage albumin protein {ECO:0000305};
DE AltName: Full=2S albumin {ECO:0000305};
DE Contains:
DE RecName: Full=2S albumin small chain;
DE Contains:
DE RecName: Full=2S albumin large chain;
DE Flags: Precursor;
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA03993.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-56 AND 75-94, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Kurokawa Amakuri Nankin {ECO:0000269|PubMed:8275099};
RC TISSUE=Cotyledon {ECO:0000312|EMBL:BAA03993.1};
RX PubMed=8275099; DOI=10.1046/j.1365-313x.1993.04050793.x;
RA Hara-Nishimura I., Takeuchi Y., Inoue K., Nishimura M.;
RT "Vesicle transport and processing of the precursor to 2S albumin in
RT pumpkin.";
RL Plant J. 4:793-800(1993).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 36-45 AND 75-84.
RC TISSUE=Cotyledon {ECO:0000269|PubMed:8275099};
RX PubMed=1743299; DOI=10.1016/0014-5793(91)81349-d;
RA Hara-Nishimura I., Inoue K., Nishimura M.;
RT "A unique vacuolar processing enzyme responsible for conversion of several
RT proprotein precursors into the mature forms.";
RL FEBS Lett. 294:89-93(1991).
CC -!- FUNCTION: This is a 2S seed storage protein. {ECO:0000305}.
CC -!- SUBUNIT: The mature protein consists of a small and a large chain
CC linked by 2 disulfide bonds. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain
CC {ECO:0000269|PubMed:8275099}. Vacuole {ECO:0000269|PubMed:8275099}.
CC Note=Cotyledonary membrane-bound vacuolar protein bodies.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000255}.
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DR EMBL; D16560; BAA03993.1; -; mRNA.
DR AlphaFoldDB; Q39649; -.
DR Allergome; 12224; Cuc ma 5.
DR Allergome; 12225; Cuc ma 5.0101.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0000322; C:storage vacuole; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; TAS:UniProtKB.
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 PRINTS; PR00496; NAPIN.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Reference proteome;
KW Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8275099"
FT PROPEP 23..35
FT /evidence="ECO:0000269|PubMed:1743299,
FT ECO:0000269|PubMed:8275099"
FT /id="PRO_0000032146"
FT CHAIN 36..?
FT /note="2S albumin small chain"
FT /evidence="ECO:0000269|PubMed:8275099"
FT /id="PRO_0000032147"
FT CHAIN 75..141
FT /note="2S albumin large chain"
FT /evidence="ECO:0000269|PubMed:8275099"
FT /id="PRO_0000032148"
FT DISULFID 43..97
FT /note="Interchain (between small and large chains)"
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 55..86
FT /note="Interchain (between small and large chains)"
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 87..132
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 99..139
FT /evidence="ECO:0000250|UniProtKB:P04403"
SQ SEQUENCE 141 AA; 16597 MW; 3E812A81C5E67EB5 CRC64;
MARLTSIIAL FAVALLVADA YAYRTTITTV EVEENRQGRE ERCRQMSARE ELRSCEQYLR
QQSRDVLQMR GIENPWRREG GSFDECCREL KNVDEECRCD MLEEIAREEQ RQARGQEGRQ
MLQKARNLPS MCGIRPQRCD F
