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Conserved domains on  [gi|216547832|ref|NP_001136010|]
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galectin-12 isoform 5 [Homo sapiens]

Protein Classification

galectin family protein( domain architecture ID 10658251)

galectin family protein may exclusively bind beta-galactosides such as lactose in a manner independent of metal ions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1-119 1.52e-42

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


:

Pssm-ID: 214904  Cd Length: 122  Bit Score: 141.19  E-value: 1.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832     1 MVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:smart00908   9 SITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELEILVE 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 216547832    81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 147-265 2.25e-21

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


:

Pssm-ID: 214904  Cd Length: 122  Bit Score: 86.49  E-value: 2.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   147 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 221
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 216547832   222 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 265
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1-119 1.52e-42

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 141.19  E-value: 1.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832     1 MVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:smart00908   9 SITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELEILVE 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 216547832    81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1-119 1.51e-39

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 133.53  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832    1 MVMLQGVVPLDAHRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:pfam00337   9 SLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELTILVG 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 216547832   81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:pfam00337  85 DDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1-119 3.02e-38

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 130.45  E-value: 3.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   1 MVMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:cd00070   15 TLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGFPFQPGQPFELTILVE 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 216547832  81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:cd00070   88 EDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 147-265 2.25e-21

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 86.49  E-value: 2.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   147 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 221
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 216547832   222 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 265
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 147-265 8.69e-08

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 49.56  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832  147 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 219
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 216547832  220 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 265
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 145-265 1.13e-05

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 43.78  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832 145 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 220
Cdd:cd00070    5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 216547832 221 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 265
Cdd:cd00070   84 ILVEEDKFQIFVNGQHFFSFP-HRLPLESIDYLSINGDVSLTSVE 127
 
Name Accession Description Interval E-value
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 1-119 1.52e-42

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 141.19  E-value: 1.52e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832     1 MVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:smart00908   9 SITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPFELEILVE 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 216547832    81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:smart00908  83 EDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 1-119 1.51e-39

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 133.53  E-value: 1.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832    1 MVMLQGVVPLDAHRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:pfam00337   9 SLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQPFELTILVG 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 216547832   81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:pfam00337  85 DDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 1-119 3.02e-38

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 130.45  E-value: 3.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   1 MVMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFG 80
Cdd:cd00070   15 TLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGFPFQPGQPFELTILVE 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 216547832  81 NEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 119
Cdd:cd00070   88 EDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 2-121 3.33e-28

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 104.62  E-value: 3.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832     2 VMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSFLILFLFGN 81
Cdd:smart00276  15 LTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFN--ENKIVCNSKLNGSWGSEEREGGFPFQPGQPFDLTIIVQP 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 216547832    82 EEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAVGF 121
Cdd:smart00276  88 DHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 147-265 2.25e-21

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 86.49  E-value: 2.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   147 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 221
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 216547832   222 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 265
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 147-265 8.69e-08

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 49.56  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832  147 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 219
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 216547832  220 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 265
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 145-265 3.79e-07

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 47.99  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832   145 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTLAWISR----WGQKKLISApFLFYPQRFFEVL 220
Cdd:smart00276   4 PIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGDDIALHFNPRFNENKIVCNSKlngsWGSEEREGG-FPFQPGQPFDLT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 216547832   221 LLFQEGGLKLALNGQGLgATSMNQQALEQLRELRISGSVQLYCVH 265
Cdd:smart00276  83 IIVQPDHFQIFVNGVHI-TTFPHRLPLESIDYLSINGDVQLTSVS 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 145-265 1.13e-05

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 43.78  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216547832 145 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 220
Cdd:cd00070    5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 216547832 221 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 265
Cdd:cd00070   84 ILVEEDKFQIFVNGQHFFSFP-HRLPLESIDYLSINGDVSLTSVE 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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