Q8VCQ6 (SMS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylcholine:ceramide cholinephosphotransferase 1
EC=2.7.8.27

Alternative name(s):
Protein Mob
Sphingomyelin synthase 1
Transmembrane protein 23

Gene names

Name:	Sgms1
Synonyms:	Tmem23

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase By similarity. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. Required for cell growth. Ref.5
Catalytic activity	A ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol.
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Isoform 1 is widely expressed, isoform 2 shows a more narrow distribution and isoform 3 is detected only in testis and heart. Ref.1
Induction	Isoform 1 and isoform 2 are induced by TNF-alpha. Ref.1
Sequence similarities	Belongs to the sphingomyelin synthase family. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Apoptosis Lipid metabolism Sphingolipid metabolism
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell growth Inferred from direct assay. Source: HGNC negative regulation of apoptotic process Inferred from direct assay Ref.1. Source: MGI sphingomyelin biosynthetic process Inferred from sequence or structural similarity Ref.4. Source: UniProtKB
Cellular component	endoplasmic reticulum Traceable author statement. Source: HGNC integral to Golgi membrane Inferred from sequence or structural similarity Ref.4. Source: UniProtKB nucleus Traceable author statement. Source: HGNC plasma membrane Traceable author statement. Source: HGNC
Molecular function	ceramide cholinephosphotransferase activity Inferred from sequence or structural similarity Ref.4. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW sphingomyelin synthase activity Inferred from mutant phenotype. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VCQ6-1)

Also known as: SMS1-alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8VCQ6-2)

Also known as: SMS1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     215-419: Missing.

Isoform 3 (identifier: Q8VCQ6-3)

Also known as: SMS1-gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     215-217: SII → LSP
     218-419: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 419

419

Phosphatidylcholine:ceramide cholinephosphotransferase 1

PRO_0000221069

Regions

Transmembrane

142 – 162

21

Helical; Potential

Transmembrane

190 – 210

21

Helical; Potential

Transmembrane

221 – 241

21

Helical; Potential

Transmembrane

282 – 302

21

Helical; Potential

Transmembrane

310 – 330

21

Helical; Potential

Topological domain

331 – 419

89

Cytoplasmic Potential

Domain

13 – 76

64

SAM

Natural variations

Alternative sequence

215 – 419

205

Missing in isoform 2.

VSP_050673

Alternative sequence

215 – 217

3

SII → LSP in isoform 3.

VSP_027225

Alternative sequence

218 – 419

202

Missing in isoform 3.

VSP_027226

Experimental info

Sequence conflict

132

1

S → Y in BAC37590. Ref.2

Sequence conflict

406

1

L → I in BAE27428. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

419

Helix Strand Turn

Details...

Helix

17 – 24

8

Turn

28 – 36

9

Helix

39 – 43

5

Helix

47 – 51

5

Beta strand

52 – 57

6

Turn

60 – 63

4

Helix

64 – 76

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SMS1-alpha) [UniParc]. Last modified February 16, 2004. Version 2. Checksum: 554CC26609F5F345	FASTA	419	49,317
	10 20 30 40 50 60 MLSARTMKEV VYWSPKKVAD WLLENAMPEY CEPLEHFTGQ DLINLTQEDF KKPPLYRVSS 70 80 90 100 110 120 DNGQRLLDMI ETLKMEHHME AHKNGHANGH LSIGVDIPNP DGSFSIKTKP NGMPNGFRKE 130 140 150 160 170 180 MIKIPMPEPE RSQYPMEWGK TFLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF 190 200 210 220 230 240 DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYKSIISRR FFCIVGTLYL YRCITMYVTT 250 260 270 280 290 300 LPVPGMHFNC SPKLFGDWEA QVRRIMKLIA GGGLSITGSH NMCGDYLYSG HTVMLTLTYL 310 320 330 340 350 360 FIKEYSPRRL WWYHWICWLL SVVGIFCILL AHDHYTVDVV VAYYITTRLF WWYHTMANQQ 370 380 390 400 410 VLKEASQMNL LARVWWYRPF QYFEKNVQGI VPRSYHWPFP WPVVHLSRQV KYSRLVNDT
	Isoform 2 (SMS1-beta) [UniParc]. Checksum: EDFE8073E259AEC4	FASTA	214	24,852
	10 20 30 40 50 60 MLSARTMKEV VYWSPKKVAD WLLENAMPEY CEPLEHFTGQ DLINLTQEDF KKPPLYRVSS 70 80 90 100 110 120 DNGQRLLDMI ETLKMEHHME AHKNGHANGH LSIGVDIPNP DGSFSIKTKP NGMPNGFRKE 130 140 150 160 170 180 MIKIPMPEPE RSQYPMEWGK TFLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF 190 200 210 DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYK
	Isoform 3 (SMS1-gamma) [UniParc]. Checksum: 0CA3256DFE8073E2	FASTA	217	25,149
	10 20 30 40 50 60 MLSARTMKEV VYWSPKKVAD WLLENAMPEY CEPLEHFTGQ DLINLTQEDF KKPPLYRVSS 70 80 90 100 110 120 DNGQRLLDMI ETLKMEHHME AHKNGHANGH LSIGVDIPNP DGSFSIKTKP NGMPNGFRKE 130 140 150 160 170 180 MIKIPMPEPE RSQYPMEWGK TFLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF 190 200 210 DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYKLSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse sphingomyelin synthase 1 (SMS1) gene is alternatively spliced to yield multiple transcripts and proteins." Yang Z., Jean-Baptiste G., Khoury C., Greenwood M.T. Gene 363:123-132(2005) [PubMed: 16226406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, INDUCTION. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6J. Tissue: Bone marrow macrophage, Embryo, Embryonic heart, Embryonic spinal cord, Embryonic stem cell, Testis and Urinary bladder.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6 and FVB/N. Tissue: Kidney and Olfactory epithelium.
[4]	"Identification of a family of animal sphingomyelin synthases." Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C. EMBO J. 23:33-44(2004) [PubMed: 14685263] [Abstract] Cited for: IDENTIFICATION.
[5]	"Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-mediated cell death in yeast." Yang Z., Khoury C., Jean-Baptiste G., Greenwood M.T. FEMS Yeast Res. 6:751-762(2006) [PubMed: 16879426] [Abstract] Cited for: FUNCTION.
[6]	"Solution structure of the SAM-domain of mouse phosphatidyl ceramidecholinephosphotransferase 1." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-84.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY509044 mRNA. Translation: AAS90514.1.
AK076554 mRNA. Translation: BAC36390.1.
AK079254 mRNA. Translation: BAC37590.1.
AK082974 mRNA. Translation: BAC38717.1.
AK133967 mRNA. Translation: BAE21960.1.
AK146782 mRNA. Translation: BAE27428.1.
AK150272 mRNA. Translation: BAE29428.1.
AK151170 mRNA. Translation: BAE30173.1.
AK152312 mRNA. Translation: BAE31117.1.
AK153406 mRNA. Translation: BAE31966.1.
AK160539 mRNA. Translation: BAE35856.1.
BC019443 mRNA. Translation: AAH19443.2.
BC085298 mRNA. Translation: AAH85298.1.

IPI

IPI00400282.
IPI00854981.
IPI00970492.

RefSeq

NP_001161997.1. NM_001168525.1.
NP_001161998.1. NM_001168526.1.
NP_659041.3. NM_144792.4.

UniGene

Mm.329810.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D8C	NMR	-	A	1-84	[»]

ProteinModelPortal

Q8VCQ6.

SMR

Q8VCQ6. Positions 1-84.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8VCQ6.

PTM databases

PhosphoSite

Q8VCQ6.

Proteomic databases

PRIDE

Q8VCQ6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000099514; ENSMUSP00000097114; ENSMUSG00000040451.
ENSMUST00000142618; ENSMUSP00000117336; ENSMUSG00000040451.
ENSMUST00000151289; ENSMUSP00000123395; ENSMUSG00000040451.
ENSMUST00000152340; ENSMUSP00000119869; ENSMUSG00000040451.
ENSMUST00000163541; ENSMUSP00000132031; ENSMUSG00000040451.

GeneID

208449.

KEGG

mmu:208449.

UCSC

uc008hfc.2. mouse.
uc008hfh.1. mouse.

Organism-specific databases

CTD

259230.

MGI

MGI:2444110. Sgms1.

Phylogenomic databases

eggNOG

roNOG04227.

GeneTree

ENSGT00390000001630.

HOGENOM

HBG447279.

HOVERGEN

HBG048216.

InParanoid

Q8VCQ6.

OMA

LEHFTGR.

OrthoDB

EOG4D52XM.

PhylomeDB

Q8VCQ6.

Enzyme and pathway databases

BRENDA

2.7.8.27. 3474.

Gene expression databases

ArrayExpress

Q8VCQ6.

Bgee

Q8VCQ6.

CleanEx

MM_SGMS1.

Genevestigator

Q8VCQ6.

GermOnline

ENSMUSG00000040451. Mus musculus.

Family and domain databases

InterPro

IPR000326. P_Acid_Pase_2/haloperoxidase.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]

Gene3D

G3DSA:1.10.150.50. SAM_type. 1 hit.

KO

K04714.

Pfam

PF01569. PAP2. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

372295.

SOURCE

Search...

Entry information

Entry name

SMS1_MOUSE

Accession

Primary (citable) accession number: Q8VCQ6
Secondary accession number(s): Q3UIS8 , Q5J3R0, Q8C464, Q8C583, Q8C652

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	February 16, 2004
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program