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O54694

- SPTC2_CRIGR

UniProt

O54694 - SPTC2_CRIGR

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Protein

Serine palmitoyltransferase 2

Gene

SPTLC2

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate (By similarity).By similarity

Catalytic activityi

Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2.

Cofactori

Pathwayi

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. serine C-palmitoyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. sphingolipid metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine palmitoyltransferase 2 (EC:2.3.1.50)
Alternative name(s):
Long chain base biosynthesis protein 2
Short name:
LCB 2
Long chain base biosynthesis protein 2a
Short name:
LCB2a
Serine-palmitoyl-CoA transferase 2
Short name:
SPT 2
Gene namesi
Name:SPTLC2
Synonyms:LCB2
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Serine palmitoyltransferase 2PRO_0000163857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei377 – 3771N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiO54694.

Interactioni

Subunit structurei

Heterodimer with SPTLC1. Component of the serine palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2 (SPTLC2 or SPTLC3) and ssPT (SPTSSA or SPTSSB) (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO54694.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG002230.
KOiK00654.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54694-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPEPGGCCC RRPLRANGCV KNGEVRNGYV RSSTATAAAA GQIHHVTENG
60 70 80 90 100
GLYKRPFNEV FEETPMLVAV LTYVGYGVLT LFGYLRDFLR HWRIEKCHHA
110 120 130 140 150
TEREEQKDFV SLYQDFENFY TRNLYMRIRD NWNRPICSVP GARVDIMERQ
160 170 180 190 200
SHDYNWSFKY TGNIIKGVIN MGSYNYLGFA RNTGSCQEAA AEVLKEYGAG
210 220 230 240 250
VCSTRQEIGN LDKHEELEKL VARFLGVEAA MTYGMGFATN SMNIPALVGK
260 270 280 290 300
GCLILSDELN HASLVLGARL SGATIRIFKH NNMQSLEKLL KDAIVYGQPR
310 320 330 340 350
TRRPWKKILI LVEGIYSMEG SIVRLPEVIA LKKKYKAYLY LDEAHSIGAL
360 370 380 390 400
GPSGRGVVDY FGLDPEDVDV MMGTFTKSFG ASGGYIGGKK ALIDYLRTHS
410 420 430 440 450
HSAVYATSMS PPVMEQIITS MKCIMGQDGT SLGKECVQQL AENTKYFRRR
460 470 480 490 500
LKEMGFIIYG NEDSPVVPLM LYMPAKIGAF GREMLKRNVG VVVVGFPATP
510 520 530 540 550
IIESRARFCL SAAHTKEILD TALKEIDEVG DLLQLKYSRR RLVPLLDRPF
560
DETTYEETED
Length:560
Mass (Da):62,882
Last modified:June 1, 1998 - v1
Checksum:iC835A5E0244878E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004830 mRNA. Translation: AAC53504.1.
RefSeqiNP_001233609.1. NM_001246680.1.

Genome annotation databases

GeneIDi100689415.
KEGGicge:100689415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004830 mRNA. Translation: AAC53504.1 .
RefSeqi NP_001233609.1. NM_001246680.1.

3D structure databases

ProteinModelPortali O54694.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O54694.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689415.
KEGGi cge:100689415.

Organism-specific databases

CTDi 9517.

Phylogenomic databases

HOVERGENi HBG002230.
KOi K00654.

Enzyme and pathway databases

UniPathwayi UPA00222 .

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis."
    Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.
    J. Biol. Chem. 272:32108-32114(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiSPTC2_CRIGR
AccessioniPrimary (citable) accession number: O54694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 26, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3