COS1_COCNU
ID COS1_COCNU Reviewed; 466 AA.
AC A0A222NNM9; A0A0R7UCU5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Cocosin 1 {ECO:0000305};
DE AltName: Full=11S globulin 1 {ECO:0000303|Ref.1, ECO:0000312|EMBL:AKS26848.1};
DE AltName: Full=CnCOS-1 {ECO:0000303|Ref.1};
DE Contains:
DE RecName: Full=Cocosin 1 acidic chain {ECO:0000305};
DE Contains:
DE RecName: Full=Cocosin 1 basic chain {ECO:0000305};
DE Flags: Precursor;
GN Name=COS-1 {ECO:0000303|Ref.1, ECO:0000312|EMBL:AKS26848.1,
GN ECO:0000312|PDB:5WPW};
OS Cocos nucifera (Coconut palm).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC Attaleinae; Cocos.
OX NCBI_TaxID=13894 {ECO:0000312|EMBL:ASQ40963.1};
RN [1] {ECO:0000312|EMBL:AKS26848.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Laguna Tall {ECO:0000303|Ref.1};
RC TISSUE=Endosperm {ECO:0000303|Ref.1};
RX DOI=10.18191/2015-08-1-011;
RA Caldo K.M.P., Garcia R.N., Tecson-Mendoza E.M.;
RT "Biochemical and molecular characterization of two 11S globulin isoforms
RT from coconut and their expression analysis during seed development.";
RL Int. J. Philipp. Sci. Technol. 8:46-51(2015).
RN [2] {ECO:0000312|EMBL:ASQ40963.1, ECO:0007744|PDB:5WPW}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS)
RP OF 43-466, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISULFIDE
RP BONDS.
RC TISSUE=Endosperm {ECO:0000303|PubMed:28712292};
RX PubMed=28712292; DOI=10.1021/acs.jafc.7b02252;
RA Jin T., Wang C., Zhang C., Wang Y., Chen Y.W., Guo F., Howard A., Cao M.J.,
RA Fu T.J., McHugh T.H., Zhang Y.;
RT "Crystal Structure of Cocosin, A Potential Food Allergen from Coconut
RT (Cocos nucifera).";
RL J. Agric. Food Chem. 65:7560-7568(2017).
RN [3] {ECO:0007744|PDB:5XTY}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ALA-2; ALA-398 AND
RP VAL-416, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISULFIDE
RP BONDS.
RX PubMed=29096167; DOI=10.1016/j.molimm.2017.10.018;
RA Vajravijayan S., Nandhagopal N., Gunasekaran K.;
RT "Crystal structure determination and analysis of 11S coconut allergen:
RT Cocosin.";
RL Mol. Immunol. 92:132-135(2017).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:28712292,
CC ECO:0000305|PubMed:29096167, ECO:0000305|Ref.1}.
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:0000269|PubMed:28712292, ECO:0000269|PubMed:29096167}.
CC -!- TISSUE SPECIFICITY: Endosperm of the seeds.
CC {ECO:0000269|PubMed:28712292, ECO:0000269|PubMed:29096167,
CC ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: During seed development. Not expressed at 5-6
CC months after pollination (MAP), weakly expressed at 6-7 MAP and highly
CC at 7-9 MAP. Weak expression level at 6-7 MAP after which expression
CC gradually increases, with the highest expression at 11-12 MAP (at
CC protein level). {ECO:0000269|PubMed:28712292,
CC ECO:0000269|PubMed:29096167, ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; KP902412; AKS26848.1; -; mRNA.
DR EMBL; KY242371; ASQ40963.1; -; Genomic_DNA.
DR PDB; 5WPW; X-ray; 1.85 A; A/B=43-466.
DR PDB; 5XTY; X-ray; 2.20 A; A/B=1-466.
DR PDBsum; 5WPW; -.
DR PDBsum; 5XTY; -.
DR AlphaFoldDB; A0A222NNM9; -.
DR SMR; A0A222NNM9; -.
DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB.
DR GO; GO:0048316; P:seed development; IEP:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Seed storage protein; Signal;
KW Storage protein.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..281
FT /note="Cocosin 1 acidic chain"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_0000445713"
FT CHAIN 282..466
FT /note="Cocosin 1 basic chain"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_0000445714"
FT DOMAIN 50..242
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 294..443
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT DISULFID 45..78
FT /evidence="ECO:0000269|PubMed:28712292,
FT ECO:0000269|PubMed:29096167, ECO:0007744|PDB:5WPW,
FT ECO:0007744|PDB:5XTY"
FT DISULFID 121..288
FT /note="Interchain (between acidic and basic chains)"
FT /evidence="ECO:0000269|PubMed:28712292,
FT ECO:0000269|PubMed:29096167, ECO:0007744|PDB:5WPW,
FT ECO:0007744|PDB:5XTY"
FT CONFLICT 2
FT /note="G -> A (in Ref. 1; AKS26848)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> A (in Ref. 1; AKS26848)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="I -> V (in Ref. 1; AKS26848)"
FT /evidence="ECO:0000305"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5XTY"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:5WPW"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:5WPW"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:5WPW"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 351..365
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 390..408
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:5WPW"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:5WPW"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:5WPW"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5WPW"
SQ SEQUENCE 466 AA; 52655 MW; A76B098015D96717 CRC64;
MGSSSLLSFS LCLLLLCHLS QAQFGSSQES PFQSPRRSVS SRNECRIERL NALEPTRTVR
SEAGVTDYFD EDNEQFRCAG VSTIRRVIEP RGLLLPSMSN APRLVYIVQG RGIVGLVMPG
CPETFQSFQR SEREEGERHR WSRDEHQKVY QFQEGDVLAV PNGFAYWCYN NGENPVVAIT
VLDTSNDANQ LDRSHRQFLL AGRQEQGRQR YGREGSIKEN ILRGFSTELL AAAFGVNMEL
ARKLQCRDDT RGEIVRAENG LQVLRPSGME EEEREEGRSI NGFEETYCSM KIKQNIGDPR
RADVFNPRGG RITTLNSEKL PILRFIQMSA ERVVLYRNAM VSPHWNINAH SIMYCTGGRG
RVEVADDRGE TVFDGELRQG QLLIVPQNFA MLERAGSEGF QLVSIKTSDR AMVSTIVGKT
SALRGMPVEV LMNSYRLSRD EARRVKLTRG DEVAIFTPRR ESRAEA
