NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1664162082|ref|NP_149092|]
View 

galectin-12 isoform 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 33-158 4.27e-46

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: 151.97  E-value: 4.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082   33 GGLHAGKMVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSF 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1664162082  113 LILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 195-313 4.27e-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: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  195 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 269
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162082  270 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 313
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 ...
 33-158 4.27e-46

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: 151.97  E-value: 4.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082   33 GGLHAGKMVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSF 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1664162082  113 LILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-158 1.73e-44

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: 148.17  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  26 PYVTTIFGGLHAGKMVMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHLA 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGFP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1664162082 106 LRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:cd00070    74 FQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-158 2.19e-42

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: 142.39  E-value: 2.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  33 GGLHAGKMVMLQGVVPLDAHRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSSF 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162082 113 LILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 195-313 4.27e-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: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  195 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 269
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162082  270 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 313
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 195-313 9.82e-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: 9.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082 195 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 267
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162082 268 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 313
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 193-313 1.41e-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: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082 193 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 268
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1664162082 269 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 313
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 ...
 33-158 4.27e-46

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: 151.97  E-value: 4.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082   33 GGLHAGKMVMLQGVVPLDAHRFQVDFQCGcslcPRPDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLALRRGSSF 112
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCG----PNADIALHFNPRFD--EGTIVRNSKQNGKWGKEERSGGFPFQPGQPF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1664162082  113 LILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:smart00908  76 ELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 26-158 1.73e-44

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: 148.17  E-value: 1.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  26 PYVTTIFGGLHAGKMVMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHTtkPHVICNTLHGGRWQREARWPHLA 105
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSS-----DIALHFNPRFDE--NVIVRNSFLNGNWGPEERSGGFP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1664162082 106 LRRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:cd00070    74 FQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 33-158 2.19e-42

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: 142.39  E-value: 2.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  33 GGLHAGKMVMLQGVVPLDAHRFQVDFQCGcsLCPRPDIAFHFNPRFhtTKPHVICNTLHGGRWQREARWPHLALRRGSSF 112
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTG--VGPSDDIALHFNPRF--DENVIVRNSRQNGQWGQEEREGGFPFQPGQPF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162082 113 LILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAV 158
Cdd:pfam00337  78 ELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSV 123
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 27-160 1.70e-32

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 116.94  E-value: 1.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082   27 YVTTIFGGLHAGKMVMLQGVVPLDAHRFQVDFQCGCSlcprpDIAFHFNPRFHttKPHVICNTLHGGRWQREARWPHLAL 106
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD-----DIALHFNPRFN--ENKIVCNSKLNGSWGSEEREGGFPF 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1664162082  107 RRGSSFLILFLFGNEEVKVSVNGQHFLHFRYRLPLSHVDTLGIFGDILVEAVGF 160
Cdd:smart00276  74 QPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 195-313 4.27e-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: 4.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  195 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVLL 269
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAKRFSINLQcGPNADIALHFNPRFDEGTIvrnSKQNgKWGKEE-RSGGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1664162082  270 LFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 313
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFP-HRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 195-313 9.82e-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: 9.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082 195 PQGLSPGQVIIVRGLVLQEPKHFTVSLR-DQAAHAPVTLR--ASFADRTL---AWIS-RWGQkKLISAPFLFYPQRFFEV 267
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQRFSINLQtGVGPSDDIALHfnPRFDENVIvrnSRQNgQWGQ-EEREGGFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1664162082 268 LLLFQEGGLKLALNGQgLGATSMNQQALEQLRELRISGSVQLYCVH 313
Cdd:pfam00337  80 TILVGDDHFKIYVNGQ-HFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 193-313 5.23e-07

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 47.99  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082  193 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTLAWISR----WGQKKLISApFLFYPQRFFEVL 268
Cdd:smart00276   4 PIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGDDIALHFNPRFNENKIVCNSKlngsWGSEEREGG-FPFQPGQPFDLT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1664162082  269 LLFQEGGLKLALNGQGLgATSMNQQALEQLRELRISGSVQLYCVH 313
Cdd:smart00276  83 IIVQPDHFQIFVNGVHI-TTFPHRLPLESIDYLSINGDVQLTSVS 126
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 193-313 1.41e-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: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1664162082 193 ALPQGLSPGQVIIVRGLVLQEPKHFTVSLRDQAAHAPVTLRASFADRTL---AWIS-RWGQKKlISAPFLFYPQRFFEVL 268
Cdd:cd00070     5 PLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSDIALHFNPRFDENVIvrnSFLNgNWGPEE-RSGGFPFQPGQPFELT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1664162082 269 LLFQEGGLKLALNGQGLGATSmNQQALEQLRELRISGSVQLYCVH 313
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH