11SB_CUCMA
ID 11SB_CUCMA Reviewed; 480 AA.
AC P13744;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=11S globulin subunit beta;
DE Contains:
DE RecName: Full=11S globulin gamma chain;
DE AltName: Full=11S globulin acidic chain;
DE Contains:
DE RecName: Full=11S globulin delta chain;
DE AltName: Full=11S globulin basic 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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kurokawa Amakuri Nankin;
RX PubMed=2450746; DOI=10.1111/j.1432-1033.1988.tb13935.x;
RA Hayashi M., Mori H., Nishimura M., Akazawa T., Hara-Nishimura I.;
RT "Nucleotide sequence of cloned cDNA coding for pumpkin 11-S globulin beta
RT subunit.";
RL Eur. J. Biochem. 172:627-632(1988).
RN [2]
RP PROTEIN SEQUENCE OF 22-30 AND 297-302, AND PYROGLUTAMATE FORMATION AT
RP GLN-22.
RA Ohmiya M., Hara I., Mastubara H.;
RT "Pumpkin (Cucurbita sp.) seed globulin IV. Terminal sequences of the acidic
RT and basic peptide chains and identification of a pyroglutamyl peptide
RT chain.";
RL Plant Cell Physiol. 21:157-167(1980).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 22-480, AND DISULFIDE BONDS.
RA Itoh T., Fukuda T., Mikami B., Utsumi S.;
RT "Crystal structure of pumpkin seed globulin.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: This is a seed storage protein.
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 -!- 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; M36407; AAA33110.1; -; mRNA.
DR PDB; 2E9Q; X-ray; 2.20 A; A=22-480.
DR PDB; 2EVX; X-ray; 2.60 A; A=22-480.
DR PDBsum; 2E9Q; -.
DR PDBsum; 2EVX; -.
DR AlphaFoldDB; P13744; -.
DR SMR; P13744; -.
DR Allergome; 12222; Cuc ma 4.
DR Allergome; 12223; Cuc ma 4.0101.
DR EvolutionaryTrace; P13744; -.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3D-structure; Direct protein sequencing; Disulfide bond; Magnesium;
KW Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 22..480
FT /note="11S globulin subunit beta"
FT /id="PRO_0000032027"
FT CHAIN 22..296
FT /note="11S globulin gamma chain"
FT /id="PRO_0000032028"
FT CHAIN 297..480
FT /note="11S globulin delta chain"
FT /id="PRO_0000032029"
FT DOMAIN 51..251
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 309..458
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT BINDING 408
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 48..81
FT /evidence="ECO:0000269|Ref.3"
FT DISULFID 124..303
FT /note="Interchain (between gamma and delta chains)"
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 27
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="E -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2E9Q"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:2E9Q"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2E9Q"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:2E9Q"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2E9Q"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 366..380
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 405..425
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 443..450
FT /evidence="ECO:0007829|PDB:2E9Q"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:2E9Q"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:2E9Q"
SQ SEQUENCE 480 AA; 54626 MW; BCD8A83DD1AED93C CRC64;
MARSSLFTFL CLAVFINGCL SQIEQQSPWE FQGSEVWQQH RYQSPRACRL ENLRAQDPVR
RAEAEAIFTE VWDQDNDEFQ CAGVNMIRHT IRPKGLLLPG FSNAPKLIFV AQGFGIRGIA
IPGCAETYQT DLRRSQSAGS AFKDQHQKIR PFREGDLLVV PAGVSHWMYN RGQSDLVLIV
FADTRNVANQ IDPYLRKFYL AGRPEQVERG VEEWERSSRK GSSGEKSGNI FSGFADEFLE
EAFQIDGGLV RKLKGEDDER DRIVQVDEDF EVLLPEKDEE ERSRGRYIES ESESENGLEE
TICTLRLKQN IGRSVRADVF NPRGGRISTA NYHTLPILRQ VRLSAERGVL YSNAMVAPHY
TVNSHSVMYA TRGNARVQVV DNFGQSVFDG EVREGQVLMI PQNFVVIKRA SDRGFEWIAF
KTNDNAITNL LAGRVSQMRM LPLGVLSNMY RISREEAQRL KYGQQEMRVL SPGRSQGRRE