SGSL_TRIAN
ID SGSL_TRIAN Reviewed; 519 AA.
AC U3KRF8; B3EWX5; U3KRF7;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Seed lectin {ECO:0000303|PubMed:23897472};
DE Short=SGSL {ECO:0000303|PubMed:23897472};
DE Contains:
DE RecName: Full=Seed lectin Aalpha chain {ECO:0000303|PubMed:23897472};
DE Contains:
DE RecName: Full=Seed lectin Abeta chain {ECO:0000303|PubMed:23897472};
DE Contains:
DE RecName: Full=Seed lectin B chain {ECO:0000303|PubMed:23897472};
DE Flags: Fragments;
OS Trichosanthes anguina (Snake gourd).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Trichosanthes.
OX NCBI_TaxID=50544 {ECO:0000303|PubMed:23897472};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 48-253 AND
RP 256-519, SUBUNIT, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC TISSUE=Seed {ECO:0000303|PubMed:23897472};
RX PubMed=23897472; DOI=10.1107/s0907444913010020;
RA Sharma A., Pohlentz G., Bobbili K.B., Jeyaprakash A.A., Chandran T.,
RA Mormann M., Swamy M.J., Vijayssan M.;
RT "The sequence and structure of snake gourd (Trichosanthes anguina) seed
RT lectin, a three-chain nontoxic homologue of type II RIPs.";
RL Acta Crystallogr. D 69:1493-1503(2013).
RN [2] {ECO:0000305}
RP FUNCTION, AND PRESENCE OF DISULFIDE BONDS.
RC TISSUE=Seed {ECO:0000303|PubMed:8799450};
RX PubMed=8799450; DOI=10.1080/15216549600201251;
RA Komath S.S., Nadimpalli S.K., Swamy M.J.;
RT "Purification in high yield and characterisation of the galactose-specific
RT lectin from the seeds of snake gourd (Trichosanthes anguina).";
RL Biochem. Mol. Biol. Int. 39:243-252(1996).
RN [3]
RP FUNCTION.
RX PubMed=10877067; DOI=10.1016/s1011-1344(00)00026-9;
RA Komath S.S., Kenoth R., Giribabu L., Maiya B.G., Swamy M.J.;
RT "Fluorescence and absorption spectroscopic studies on the interaction of
RT porphyrins with snake gourd (Trichosanthes anguina) seed lectin.";
RL J. Photochem. Photobiol. B 55:49-55(2000).
RN [4]
RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND
RP FUNCTION.
RX PubMed=11375527; DOI=10.1107/s0907444901004620;
RA Manoj N., Jeyaprakash A.A., Pratap J.V., Komath S.S., Kenoth R.,
RA Swamy M.J., Vijayan M.;
RT "Crystallization and preliminary X-ray studies of snake gourd lectin:
RT homology with type II ribosome-inactivating proteins.";
RL Acta Crystallogr. D 57:912-914(2001).
CC -!- FUNCTION: Seed lectin similar to type 2 ribosome-inactivating proteins
CC (PubMed:23897472, PubMed:11375527). The Aalpha and Abeta chains
CC constitute the rRNA glycosidase domain and the B chain the
CC carbohydrate-binding lectin domain (PubMed:23897472). Is predicted to
CC have no glycosidase activity and, hence, to be non-toxic, due to small
CC changes in both the nucleotide binding and carbohydrate binding
CC capabilities (PubMed:23897472, PubMed:11375527). Binds galactose and
CC derivatives with a preference for the beta-anomeric forms
CC (PubMed:8799450, PubMed:10877067). Binds prophyrins (PubMed:10877067).
CC Has hemagglutinating activity towards rabbit and human erythrocytes
CC (PubMed:8799450, PubMed:10877067). {ECO:0000269|PubMed:10877067,
CC ECO:0000269|PubMed:11375527, ECO:0000269|PubMed:23897472,
CC ECO:0000269|PubMed:8799450}.
CC -!- SUBUNIT: Heterotrimer consisting of Aalpha, Abeta and B chains with
CC Abeta and B being disulfide-linked.
CC -!- DOMAIN: The B chain is composed of two domains with each domain
CC consisting of 3 homologous subdomains (alpha, beta, gamma).
CC {ECO:0000250|UniProtKB:P02879}.
CC -!- MASS SPECTROMETRY: Mass=59028.6; Method=Electrospray; Note=The measured
CC range is 1-519.; Evidence={ECO:0000269|PubMed:23897472};
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a heterodimer. However, methods
CC used then would have missed the Aalpha chain.
CC {ECO:0000305|PubMed:8799450}.
CC -!- CAUTION: Based on similarity to other family members, it is assumed
CC that all three chains derive from a single precursor but the genomic
CC DNA sequence to support this is not yet available.
CC {ECO:0000305|PubMed:23897472}.
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DR PDB; 4HR6; X-ray; 2.25 A; B=48-253, C=256-519.
DR PDBsum; 4HR6; -.
DR AlphaFoldDB; U3KRF8; -.
DR SMR; U3KRF8; -.
DR UniLectin; U3KRF8; -.
DR iPTMnet; U3KRF8; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; PTHR33453; 3.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lectin; Repeat.
FT CHAIN 1..46
FT /note="Seed lectin Aalpha chain"
FT /evidence="ECO:0000269|PubMed:23897472"
FT /id="PRO_0000436385"
FT CHAIN 47..255
FT /note="Seed lectin Abeta chain"
FT /evidence="ECO:0000269|PubMed:23897472"
FT /id="PRO_0000436386"
FT CHAIN 256..519
FT /note="Seed lectin B chain"
FT /evidence="ECO:0000269|PubMed:23897472"
FT /id="PRO_0000436387"
FT DOMAIN 261..387
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 271..311
FT /note="1-alpha"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT REPEAT 312..352
FT /note="1-beta"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT REPEAT 356..388
FT /note="1-gamma"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT DOMAIN 390..518
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 401..438
FT /note="2-alpha"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT REPEAT 442..482
FT /note="2-beta"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT REPEAT 486..513
FT /note="2-gamma"
FT /evidence="ECO:0000250|UniProtKB:P02879"
FT BINDING 276..279
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT BINDING 296..298
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT BINDING 454
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT BINDING 491..494
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT BINDING 505..508
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT BINDING 512
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:4HR6"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23897472"
FT DISULFID 249..258
FT /note="Interchain (between Abeta and B chains)"
FT /evidence="ECO:0000269|PubMed:23897472"
FT DISULFID 274..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0007744|PDB:4HR6"
FT DISULFID 315..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0007744|PDB:4HR6"
FT DISULFID 404..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0007744|PDB:4HR6"
FT DISULFID 445..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0007744|PDB:4HR6"
FT NON_CONS 46..47
FT /evidence="ECO:0000305|PubMed:23897472"
FT NON_CONS 255..256
FT /evidence="ECO:0000305|PubMed:23897472"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 188..206
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 320..325
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:4HR6"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 441..453
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:4HR6"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:4HR6"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:4HR6"
SQ SEQUENCE 519 AA; 57815 MW; 26F6B1C48CF2CD4F CRC64;
NEQANLRLSE ANSGTYKTFI GRVREELGSE TYRLYGIPVL KHSLSNSNRF YLLTLTSNQD
ESITLAIDVE DMVAVAYQPA GSHESYFFLN APQIAFHTLF TDTHQNVLNF DNTFKSLENA
AGTTRQTIVL GVDPLDFAIS NLFNADPKLL PLSFLVIIQM VLEASKFRFI EQSVAYSFKN
EKTFLPDLAI VSLEDNWSEI SLQIQASTSL QGLFGSVVEL YNSNNELIEV DSIYYPIILA
NVALQLYHCQ VSTGDNECLV ETRTTRISGR DALCVDVAGA LTSDGSRLIL YPCGQQVNQK
WTFHSDGTVR SLGKCLATNN SKFGNLVVIY DCSKLAAEDI SWDVSVGGTI MNPNYEDLAL
TSNKATRSTN LTMEVNTYSA SQGWRVGNYV QPIIGSIVGL DDMCLEATDG NTNMWLEECV
PNQREQSWAL YSDGTIRVDD NRELCVTASS STYDNWKVIT ILNCDGSNNQ RWVFLADGSI
STPGNQRLAM DVARSDVDLK KIILHRPHGD LNQQWVLFY
