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Interpro entry: Legume-like lectin
Regions of secondary structure in
rat ERGIC-53 and yeast Emp47p are indicated above the
alignment and coloured as in the the structure of ERGIC-53, left. Beta-strands are numbered b1-b15 and highlighted
yellow (concave sheet),
dark blue
(convex sheet) and
blue (hairpin).
Helices are highlighted in red:
310, 310 helix, a, alpha-helix. Amino acid residues
conserved in the animal L-type lectins, and the equivalent residues in other
L-type lectins, are highlighted in green where identical and in cyan
where the character of the
residue is preserved. Cysteine
residues forming a disulphide bond are highlighted in
yellow.
Residues that contribute directly to sugar binding in the structures of concanavalin A
and Erythrina corallodendron lectin, and the equivalents in other proteins, are highlighted
in magenta where identical,
pink where the character of the
residue is preserved, and light pink
where the character of the residue is not preserved.
Residues highlighted in
blue and
red are involved in the coordination of the Ca2+
ions
in ERGIC-53
at sites 1 and 2 respectively; the residue highlighted in
purple contributes to both sites.
Site 2 is identical to the second metal binding
site in plant lectins, which also binds Ca2+.
Emp46p
residues highlighted in
orange are involved in K+ coordination.
The His residue highlighted in gold
is essential for lectin activity in both ERGIC-53 and VIP36, and may serve as a
pH sensor.
Accession numbers
HS =
human BT = cow CE = C elegans DM = Drosophila DD = Dictyostelium discoideum SC =
Saccharomyces cerevisiae SP = Schizosaccharomyces pombe AT = Arabidopsis thaliana
ERGIC-53:
HS
P49257
DM
Q9V3A8
CE
G5EDE8
DD
Q8T2J5
ERGL: HS
Q9HAT1
BT
21425
VIPL: HS
Q9H0V9
XT
Q5M7Q0
DM
Q9VCC2 CE
Q22170
VIP36: HS
Q12907
XT
006741
SC EMP47
P43555 SC EMP46
Q12396 SC Uip5
P36137 AT 1
Q9LK72; AT 2
O81292
SP CC126.08c (VIPL?)
O94401 SP BC4F6.05c
O42707 TC Antigen 38
Q9GPB0
Concanavalin A
P02866
ECorL
P16404
If alignments appear scrambled
please maximize the width of your browser window. |
Crystal structure of rat ERGIC-53 with bound
Ca2+
Beta-strands in one sheet are coloured dark blue and those in the opposing
sheet are coloured yellow. The beta-hairpin structure is coloured blue
and helices are coloured red. The Ca2+ ions are shown in pink.
Protein Data Bank structure ID:
1R1Z. |
Rat ERGIC-53
b1 310 b1
Yeast
Emp47p
310
b2
b3
b4
b5
b6
HS ERGIC PAVALPHRRFEYKYSFKGPHLVQS---DGTV-PFWAHAGNAIPS-SDQIRVAPSLKSQ--RGSVWTKTKAA-FENWEVEVTFRVTGRG--RIGAD
DM ERGIC PGAVGVHRRFEYKYSFKPPYLAQK---DGTV-PFWEYGGNAIAS-SESVRVAPSLRSQ--KGAIWTKSQTN-FDWWDVEIVFRVTGRG--RIGAD
CE ERGIC AQNTPVFKKFEYKHSFRAPNLAQR---DGSI-PFWIVSGDAIAS-GEQLRLAPSMRSR--KGIAWNKRAFLESENFQVDIALKIGGQG--RVGAD
DD ERGIC
GGSNSANIRREDRHSFRAPFLQSG---TGIL--YWDIEGSTIVN-DDFIRLTSDQKSL--HGAIWNTEPME-QPWWEVVFEFRVHGAG--RIGAD
HS ERGL -----PLRRFEYKLSFKGPRLALP---GAGI-PFWSHHGDAILGLEE-VRLTPSMRNR--SGAVWSRASVP-FSAWEVEVQMRVTGLG--RRGAH
BT
ERGL
EMGHLPQRRFEYKLSFKGPRLALP---GVGI-PFWSHHGDAIPGLEE-VRLAPSMRNR--SGAVWSTNPVL-FPAWEVEIQMRVTGPG--RWGAQ
DM VIPL
DMPR-EPDYMKREHSLVRPFQGVG----VIL-PHWDFLGNTMVT-SNYIRLTPDLQSK--SGALWNYSPVM-TRNWEVHVGFKVHGKG-TELFGD
CE VIPL
QTVHEFRGYYKREHSLIKPYTGSG----ADI-PNWNIIGSTFVS-SNQIRLTADEQSK--AGALWNTQPVW-SRDWELQVSFKVTGST-GDLFGD
HS
VIPL
VGAGQTFEYLKREHSLSKPYQGVGTG-SSSL---WNLMGNAMVM-TQYIRLTPDMQSK--QGALWNRVPCF-LRDWELQVHFKIHGQGKKNLHGD
XT VIPL
GTADQTEEYLKREHSLSKPYQGVGSS-TSSL---WDLLGNSLVT-PQYVRLTPDLQSK--QGAVWNRVPCY-LRDWEMQVHFKIHGQGKKNLNGD
HS
VIP36
DITDGNSEHLKREHSLIKPYQGVG---SSSM-PLWDFQGSTMLT-SQYVRLTPDERSK--EGSIWNHQPCF-LKDWEMHVHFKVHGTGKKNLHGD
XT VIP36
DLTDGNSEYLKREHSLIKPYQGVG---SSSM-PMWDFSGSTMLT-SQYVRLTTDERSK--EGSIWNRLPCF-LKDWELHVQFRIHGSGKKNLHGD
TC Ag38
EQHHRTSERVIEHHSFSPPLLRNYY-GEDELR-HWAIGGTTVIT-DNYVRLTADRPGQ--VGHLWNTEPLD-MPSFEIVVGFHLHGKG---TGAD
SP CC126.08c
VLGALAETSHLERLSLEAPYINHG---MRNL--WWEYGGSTVIDRKNGIFLTQDVQNQ--QGWISTRLPTP-SSSFEVLFQFRINSES-TSLFGD
SP BC4F6.05c YAVPKSQFLQLHSLSNAIPVE-------------WKWYGSVDED-SGYVYLTSKDSNEARSGSLWSTSVLR-QVGWQLSTSFVAHVSENENTF--
SC EMP47 LGDTSDASKLSSDYSL--PDLINARK----VPNNW-QTGEQASLEEGRIVLTSKQNSK---GSLWLKQGFDLKDSFTMEWTFRSVGYS-GQTDG-
SC EMP46
KVTQKDELKWNKGYSL--PNLLEVTDQQKEL-SQW-TLGDKVKLEEGRFVLTPGKNTK---GSLWLKPEYSIKDAMTIEWTFRSFGFR-GSTKG-
SC Uip5
RGRSHVTRVPNHDASLSIPFLDKINQ-------FWHVGGATQIRNIQSIKLTQDRDQDKHGLVLSNGIGDNTINDFEIVFTFRISHDPTTQLTGD
AT 1 AAFAVKFNFDSFDGSNLLFLGDAELG--PSSDG-VSRSGALSMTRDENPFSHGQGLYI--NQIPFKPSNTSSPFSFETSFTFSITPRTK-PNSGQ
AT 2 PLNSSSQSLNFTYNSFHRPPTNIS---IQGIAT-VTSNGILKLT-DKTVISTGHAFYT--EPIRFKDSPNDTVSSFSTTFVIGIYSGIP-TISGH
CON A NALHFMFNQFSKDQK-DLILQGDA---TTGTDG-NLELTRVSSNGSPQGSSVGRALFY--APVHIWESSAV-VASFDATFTFLIKSPDS--HPAD
ECORL ETISFSFSEFEPGND-NLTLQGAA---LITQSG-VLQLTKINQNGMPAWDSTGRTLYA--KPVHIWDMTTGTVASFETRFSFSIEQPYTRPLPAD
Rat ERGIC-53
a
Yeast
Emp47p
b7
b8
b9
a b10
HS ERGIC
GLAIWYAENQ-------GLEGPVFGSA------------------DLWNGVGIFFDTFDNDG---KKNNPAIVIIGNNGQIHYDHQNDGASQALAS--
DM ERGIC
GLAFWYTTEK------GDYNGPVFGSS------------------DRWNGLAIMFDSFDNDN---KHNNPYISAVLNDGTKLYDHAEDGTTQLLAG--
CE ERGIC
GLGIWYTSQL-------GALGPVFGGN------------------DFWTGMGLFLDSFDNDG---QKNNPQVSLMLNDGTRSYDHHTDGSQQILSS--
DD
ERGIC
GIALWLVDRK----EGNSQDFSIYGSK------------------NLWKGLAIIFDTFDNDQ---NGDHPLISVFYNDGTKFYETAKDGSNMKLGS--
HS ERGL
GMAVWYTRGR-------GHVGSVLGGL------------------ASWDGIGIFFDSPAEDT----QDSPAIRVLASDGHIPSEQPGDGASQGLGS--
BT
ERGL
GMAVWYTRGR-------GQVGPVLGEP------------------DLGDGIGILFDSSAQDP----QNSPAIYVLARDRHTLYEPLGDGGSLLLGS--
DM VIPL
GFAIWYTKER-------MQTGPVFGSK------------------DHFSGLAIILDTYSNHNGPHNHQHPYLSAMVNNGSWSYDHDRDGTHTQLAG--
CE
VIPL
GMAIWYTSEP-------NILGPVFGGK------------------DYFRGLAVFLDTYSNHNGPHQHGHPFISAMVSDGSLHYDHDKDGTHTQLGG--
HS
VIPL
GLAIWYTKDR-------MQPGPVFGNM------------------DKFVGLGVFVDTYPNEEKQQERVFPYISAMVNNGSLSYDHERDGRPTELGG--
XT VIPL
GFAIWYTKDR-------MQAGPVFGSK------------------DNFVGLGLFVDTYPNEEKQHERVFPYISAMVSNGSITYDHSRDGRTTELGG--
HS VIP36
GIALWYTRDR-------LVPGPVFGSK------------------DNFHGLAIFLDTYPNDE-TTERVFPYISVMVNNGSLSYDHSKDGRWTELAG--
XT
VIP36
GFALWYAKDR-------LQPGPVFGNH------------------DKFHGLAVFLDTYPNDE-TTERVFPYISVMVNNGSLEYDHSKDGRTVELAG--
TC Ag38
GFALWITTDR------PSHNGPLMGRP------------------MEFTGLGIIFDTYDNDG---LRDNPAVYVLFNDETQRNRQYNTQKDFKGEY--
SP
CC126.08c
GLAFFLAAER-------AKPGPVFGFT------------------DKFNGYGIFIDTYNNHRPGT--LFPRVIVMKGDGHTPYDYENDGKANEIAS--
SP BC4F6.05c
-FAIWYTSAV-------GSEGPVVFGA-----------------SDKWDGLLISQEIDQT-------GKIFVRGYLNDKSFELAQFTDPDLPPFAK--
SC EMP47
GISFWFVQDSNVPRDKQLYNGPVN-----------------------YDGLQLLVDNN-------GPLGPTLRGQLNDGQKPVDKTKI-YDQSFAS--
SC EMP46
GLAFWLKQGNEGDSTEL------FGGSSKK-----------------FNGLMILLRLD-------DKLGESVTAYLNDGTKDLDIESS---PYFAS--
SC Uip5
GMCFAITPENGFLTQNLQSSYAKKQYMMNSQGVIADNTDLMGFPKNLP-GLFIVLDTYRNQGHD----HKEVPFMDVFINVAPESDWYDINSDGELST
AT 1
GFAFFITPEADNS---GASDGGYLGILNKTNDGK-----------PENHILAIEFDTFQNKE-FLDISGNHVGVNIN-SMTSLVAEKAGYWVQTRV--
AT 2
GMAFFIAPNPVLS---SAMASQYLGLFSSTNNGN-----------DTNHILAVEFDTIMNPEFD-DTNDNHVGININ-SLTSVKSSLVGYWDEINQ--
CON A
GIAFFISNIDSSI--PSGSTGRLLGLFPDANVIRNSTTIDFNAAYNADTIVAVELDTYPNTDIG-DPNYPHIGIDIK----SVRSKKTAKWNMQNG--
ECORL
GLVFFMGPTKSKP----AQGYGYLGIFNNSKQD------------NSYQTLGVEFDTFSNPWD--PPQVPHIGIDVN----SIRSIKTQPFQLDNG--
Rat ERGIC-53
--
Yeast
Emp47p
b11
b12
b13
--
b14
b15
HS ERGIC ----------CQRDFRNKPY-PVRAKITYYQNTLTVMINNG--FTPDKNDYEFCAKVENMII-PA-----QGHFGISAATGG---LADDHDVLSFLTFQLT
DM
ERGIC ----------CLRDFRNKPF-PTRARIEYYNNVLTVMIHNG--MSNNNDDYELCLRADGVNL-PK-----NGYFGISAATGG---LADDHDVFHFLTTSLH
CE ERGIC ----------CQRDFRNKPY-PVRIRIEYLKNVLTVHIDDG--MQPTPR-YELCMRAENIFL-PR-----NGYFGVSAATGG---LADDHDVLDFSVFSLF
DD
ERGIC ----------CSSRYRNDKH-NAKSRIRYYHGLLSVEID----PNGSGI-FEKCVQDVRLDI-PT-----RYTFGVSAATGG---LTDNHDVYSFDTFSLD
HS ERGL ----------CHWDFRNRPH-PFRARITYWGQRLRMSLNSG—-LTPSDPG-EFCVDVGPLLLVP------GGFFGVSAATGT---LADDHDVLSFLTFSLS
BT
ERGL ----------CRQDFRNRPY-PFRARITYWGQRLRVSLNSG--LTPSGPD-EVCVDVGPLLLAP------GGFFGVSAATSI---LADDHDVLSFLTFSLW
DM VIPL ----------CEVRFRNVEY-ETLVSIRYENDILSVSTD----LENRNE-WKNCFVVANVEL-PT-----GYHFGMSATTGD---LSDNHDIHSFKFYDLD
CE VIPL
------ENTGCTAKFRNKDH-DTQVLIRYVGDTLSIFSD----IENKGI-WNLCMSVNNVQL-PT-----GYYIGVSAATGD---LSDAHDVVSLKMFEQE
HS
VIPL ----------CTAIVRNLHY-DTFLVIRYVKRHLTIMMD----IDGKHE-WRDCIEVPGVRL-PR-----GYYFGTSSITGD---LSDNHDVISLKLFELT
XT VIPL
----------CTAMVRNLNH-DTFLVIRYVKRRLTIMVD----IDGKQE-WKDCVDVPGVRL-PR-----GYFFGASAVTGD---LSDNHDVISLKLYQLS
HS VIP36 ----------CTADFRNRDH-DTFLAVRYSRGRLTVMTD----LEDKNE-WKNCIDITGVRL-PT-----GYYFGASAGTGD---LSDNHDIISMKLFQLM
XT
VIP36 ----------CTVDVRNKNH-DTFLAIRYSQGRLTVMTD----IEDKNE-WKNCLDISGVRL-PT-----GYYFGASAATGD---LSDNHDIISMKLYQLM
TC
Ag38
-------VGRCNYAYRQTSALPSTARIRYEGNTLQIFLSLD---GERNELQLQCTTISDLRL-PIGKG--GYYIGLSAETGD---LTDSHDILFVHTMPIE
SP
CC126.08c ----------CSALNVRGND-YNLGKLKYDKNAKKLRFEIAYQGSSS---FIKCFDLNEVEL-PL-----TTFMSFSAHTGD---LSESHEIASILSRTIT
SP BC4F6.05c ----------CTIESSPEAL--NNIILKYGDQSGLELFVNDKP----------CFQVKDVIL-PQ-----GYYFGVSSQSTSAKDLVALSNLNILPPDTSN
SC EMP47 ----------CLMGYQDSSV-PSTIRVTYDLEDDNLLKVQVDN--------KVCFQTRKVRF-PSG----SYRIGVTAQNGAVNNNAESFEIFKMQFFNGV
SC EMP46
----------CLFQYQDSMV-PSTLRLTYNPLDNHLLKLQMDN--------RVCFQTRKVKFMGSS----PFRIGTSAINDA---SKESFEILKMKLYDGV
SC Uip5
SLRLNSRGHIKLKKNALWNR-VTKLRIIYLESISFLKIDVQYA--KEGNYWIELFQTTENLL-PKNMHTGQRYIGCSALNGQ---LTETVELLDVSTSEFH
AT 1 GKRKVWSFKDVNLSSGER--FKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLL--QNMY-----AGFAGSMGRAVER---HDIWSWSFENAA
AT 2 -------FNNLTLISRKR--MQVWVDYDDRTNQIDVTMAPFGEVKPRKALVSVVRDLSSVFL--QDMY-----LGFSAATGYVLSE---HFVFGWSFMVKG
CON A -----------KVGTAHII-YNSVGKRLSAVVSYPNGDS-----ATVSYDVDL----DNV-L-PEWVR-----VGLSASTGLYKET---NTILSWSFTSKL
ECORL -----------QVANVVIK-YDASSKILHAVLVYPSSGA----IYTIAEIVDV----KQV-L-PEWVD-----VGLSGATGAQRDAAETHDVYSWSFQASL
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Wednesday, 01 January 2014
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Animal lectins
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- Kurt Drickamer
- Division of Molecular Biosciences
- Faculty of Natural Sciences
- Imperial College London
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- Email:
k.drickamer@imperial.ac.uk
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