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Conserved domains on  [gi|1664162086|ref|NP_001136007|]
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galectin-12 isoform 1 [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 ...
 33-159 2.52e-44

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: 147.35  E-value: 2.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086   33 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1664162086  113 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 196-314 4.04e-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: 86.88  E-value: 4.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  196 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 270
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162086  271 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 314
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 ...
 33-159 2.52e-44

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: 147.35  E-value: 2.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086   33 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1664162086  113 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-159 6.66e-43

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: 143.93  E-value: 6.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  26 PYVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHL 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNA-KRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGF 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1664162086 106 ALRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:cd00070    73 PFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-159 1.29e-40

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: 137.77  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  33 GGLHAGKMVMLQGVVPLDAhSRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSS 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDA-QRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1664162086 113 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:pfam00337  77 FELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 196-314 4.04e-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: 86.88  E-value: 4.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  196 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 270
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162086  271 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 314
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 196-314 9.68e-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: 49.95  E-value: 9.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086 196 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 268
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162086 269 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 314
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 194-314 1.43e-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: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086 194 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 269
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1664162086 270 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 314
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 ...
 33-159 2.52e-44

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: 147.35  E-value: 2.52e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086   33 GGLHAGKMVMLQGVVPLDAHsRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSS 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAK-RFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQP 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1664162086  113 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:smart00908  75 FELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-159 6.66e-43

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: 143.93  E-value: 6.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  26 PYVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHL 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNA-KRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGF 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1664162086 106 ALRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:cd00070    73 PFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-159 1.29e-40

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: 137.77  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  33 GGLHAGKMVMLQGVVPLDAhSRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSS 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDA-QRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1664162086 113 FLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 159
Cdd:pfam00337  77 FELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 27-161 3.89e-31

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 113.48  E-value: 3.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086   27 YVTTIFGGLHAGKMVMLQGVVPLDAhSRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLA 106
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDA-KRFSINLLTGGD-----DIALHFNPRFN--ENKIVCNSKLNGSWGSEEREGGFP 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1664162086  107 LRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAVGF 161
Cdd:smart00276  73 FQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 196-314 4.04e-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: 86.88  E-value: 4.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  196 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 270
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162086  271 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 314
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 196-314 9.68e-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: 49.95  E-value: 9.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086 196 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 268
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162086 269 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 314
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 194-314 5.20e-07

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 47.99  E-value: 5.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086  194 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTLAWISR----WGQKKLISApFLFYPQRFFEVL 269
Cdd:smart00276   4 PIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGDDIALHFNPRFNENKIVCNSKlngsWGSEEREGG-FPFQPGQPFDLT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1664162086  270 LLFQEGGLKLALNGQGLgATSMNQQALEQLRELRISGSVQLYCVH 314
Cdd:smart00276  83 IIVQPDHFQIFVNGVHI-TTFPHRLPLESIDYLSINGDVQLTSVS 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 194-314 1.43e-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: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162086 194 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 269
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1664162086 270 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 314
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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