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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}.
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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
 
 
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