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Conserved domains on  [gi|1700611629|ref|NP_001358316|]
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ORM1-like protein 1 isoform 3 [Homo sapiens]

Protein Classification

ORMDL family protein( domain architecture ID 10513350)

ORMDL family protein is a negative regulator of sphingolipid synthesis that forms a conserved complex with serine palmitoyltransferase, the first and rate-limiting enzyme in sphingolipid production

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ORMDL pfam04061
ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. ...
 11-109 5.19e-50

ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. Orm proteins have been identified as negative regulators of sphingolipid synthesis that form a conserved complex with serine palmitoyltransferase, the first and rate-limiting enzyme in sphingolipid production. This novel and conserved protein complex, has been termed the SPOTS complex (serine palmitoyltransferase, Orm1/2, Tsc3, and Sac1).


:

Pssm-ID: 461151  Cd Length: 135  Bit Score: 155.03  E-value: 5.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611629  11 NPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETpDQGKARLLTHWEQLD 90
Cdd:pfam04061   1 NPNASWVNSKGAWLIYIVLILLLKLLLLSIPGFSVEVAWTLTNLIHNIGTFIMFHWIKGTPFEF-DQGAYDNLTFWEQID 79

                          90
                  ....*....|....*....
gi 1700611629  91 YGVQFTSSRKFFTISPIIL 109
Cdd:pfam04061  80 NGAQYTPTRKFLTLVPIVL 98
 
Name Accession Description Interval E-value
ORMDL pfam04061
ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. ...
 11-109 5.19e-50

ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. Orm proteins have been identified as negative regulators of sphingolipid synthesis that form a conserved complex with serine palmitoyltransferase, the first and rate-limiting enzyme in sphingolipid production. This novel and conserved protein complex, has been termed the SPOTS complex (serine palmitoyltransferase, Orm1/2, Tsc3, and Sac1).


Pssm-ID: 461151  Cd Length: 135  Bit Score: 155.03  E-value: 5.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611629  11 NPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETpDQGKARLLTHWEQLD 90
Cdd:pfam04061   1 NPNASWVNSKGAWLIYIVLILLLKLLLLSIPGFSVEVAWTLTNLIHNIGTFIMFHWIKGTPFEF-DQGAYDNLTFWEQID 79

                          90
                  ....*....|....*....
gi 1700611629  91 YGVQFTSSRKFFTISPIIL 109
Cdd:pfam04061  80 NGAQYTPTRKFLTLVPIVL 98
COG5081 COG5081
Predicted membrane protein [Function unknown];
8-109 9.76e-20

Predicted membrane protein [Function unknown];


Pssm-ID: 227413  Cd Length: 180  Bit Score: 79.13  E-value: 9.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611629   8 SEVNPNTRVMNSRGMWLTYALGVGLLHIVLlSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETpDQGKARLLTHWE 87
Cdd:COG5081    30 VLPNMNATWVDQRGAWIIHVVVILLLKLFY-SLFGVTDELGWTLTNMTYNIGSFIMFHLIKGTPFDF-NGGAYDNLTMWE 107

                          90       100
                  ....*....|....*....|..
gi 1700611629  88 QLDYGVQFTSSRKFFTISPIIL 109
Cdd:COG5081   108 QLDEETLYTPDRKFLLLVPIIL 129
 
Name Accession Description Interval E-value
ORMDL pfam04061
ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. ...
 11-109 5.19e-50

ORMDL family; Evidence form suggests that ORMDLs are involved in protein folding in the ER. Orm proteins have been identified as negative regulators of sphingolipid synthesis that form a conserved complex with serine palmitoyltransferase, the first and rate-limiting enzyme in sphingolipid production. This novel and conserved protein complex, has been termed the SPOTS complex (serine palmitoyltransferase, Orm1/2, Tsc3, and Sac1).


Pssm-ID: 461151  Cd Length: 135  Bit Score: 155.03  E-value: 5.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611629  11 NPNTRVMNSRGMWLTYALGVGLLHIVLLSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETpDQGKARLLTHWEQLD 90
Cdd:pfam04061   1 NPNASWVNSKGAWLIYIVLILLLKLLLLSIPGFSVEVAWTLTNLIHNIGTFIMFHWIKGTPFEF-DQGAYDNLTFWEQID 79

                          90
                  ....*....|....*....
gi 1700611629  91 YGVQFTSSRKFFTISPIIL 109
Cdd:pfam04061  80 NGAQYTPTRKFLTLVPIVL 98
COG5081 COG5081
Predicted membrane protein [Function unknown];
8-109 9.76e-20

Predicted membrane protein [Function unknown];


Pssm-ID: 227413  Cd Length: 180  Bit Score: 79.13  E-value: 9.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1700611629   8 SEVNPNTRVMNSRGMWLTYALGVGLLHIVLlSIPFFSVPVAWTLTNIIHNLGMYVFLHAVKGTPFETpDQGKARLLTHWE 87
Cdd:COG5081    30 VLPNMNATWVDQRGAWIIHVVVILLLKLFY-SLFGVTDELGWTLTNMTYNIGSFIMFHLIKGTPFDF-NGGAYDNLTMWE 107

                          90       100
                  ....*....|....*....|..
gi 1700611629  88 QLDYGVQFTSSRKFFTISPIIL 109
Cdd:COG5081   108 QLDEETLYTPDRKFLLLVPIIL 129
 
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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