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Sphingomyelin synthase-related protein 1 (SMSr) (EC 2.7.8.-) (Ceramide phosphoethanolamine synthase) (CPE synthase) (Sterile alpha motif domain-containing protein 8) (SAM domain-containing protein 8)

 SAMD8_HUMAN             Reviewed;         415 AA.
Q96LT4; Q5JSC5; Q5JSC8; Q66K52;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
27-SEP-2017, entry version 132.
RecName: Full=Sphingomyelin synthase-related protein 1;
Short=SMSr;
EC=2.7.8.-;
AltName: Full=Ceramide phosphoethanolamine synthase;
Short=CPE synthase;
AltName: Full=Sterile alpha motif domain-containing protein 8;
Short=SAM domain-containing protein 8;
Name=SAMD8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:BAB71586.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Huitema K.;
Submitted (FEB-2003) to UniProtKB.
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum {ECO:0000312|EMBL:BAB71586.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 198-359 (ISOFORM 1).
Ebert L., Heil O., Hennig S., Neubert P., Partsch E., Peters M.,
Radelof U., Schneider D., Korn B.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
IDENTIFICATION.
PubMed=14685263; DOI=10.1038/sj.emboj.7600034;
Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.;
"Identification of a family of animal sphingomyelin synthases.";
EMBO J. 23:33-44(2004).
[8]
SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF
ASP-348, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19506037; DOI=10.1083/jcb.200903152;
Vacaru A.M., Tafesse F.G., Ternes P., Kondylis V., Hermansson M.,
Brouwers J.F., Somerharju P., Rabouille C., Holthuis J.C.;
"Sphingomyelin synthase-related protein SMSr controls ceramide
homeostasis in the ER.";
J. Cell Biol. 185:1013-1027(2009).
-!- FUNCTION: Sphingomyelin synthases synthesize sphingolipids through
transfer of a phosphatidyl head group on to the primary hydroxyl
of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase
that has no sphingomyelin synthase activity but can convert
phosphatidylethanolamine (PE) and ceramide to ceramide
phosphoethanolamine (CPE) albeit with low product yield. Appears
to operate as a ceramide sensor to control ceramide homeostasis in
the endoplasmic reticulum rather than a converter of ceramides.
Seems to be critical for the integrity of the early secretory
pathway. {ECO:0000269|PubMed:19506037}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:19506037}; Multi-pass membrane protein
{ECO:0000269|PubMed:19506037}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96LT4-1; Sequence=Displayed;
Name=2;
IsoId=Q96LT4-2; Sequence=VSP_038403, VSP_038404;
-!- DOMAIN: The SAM domain is required to retain SMAD8 in the
endoplasmic reticulum.
-!- SIMILARITY: Belongs to the sphingomyelin synthase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH80593.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK057811; BAB71586.1; -; mRNA.
EMBL; AL392111; CAI40906.1; -; Genomic_DNA.
EMBL; AL392111; CAI40909.1; -; Genomic_DNA.
EMBL; CH471083; EAW54566.1; -; Genomic_DNA.
EMBL; CH471083; EAW54567.1; -; Genomic_DNA.
EMBL; BC080593; AAH80593.1; ALT_INIT; mRNA.
EMBL; BX280496; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS53543.1; -. [Q96LT4-1]
CCDS; CCDS7347.1; -. [Q96LT4-2]
RefSeq; NP_001167627.1; NM_001174156.1. [Q96LT4-1]
RefSeq; NP_653261.1; NM_144660.2. [Q96LT4-2]
RefSeq; XP_005269598.1; XM_005269541.4. [Q96LT4-1]
RefSeq; XP_011537613.1; XM_011539311.1.
RefSeq; XP_011537614.1; XM_011539312.2. [Q96LT4-1]
RefSeq; XP_016871228.1; XM_017015739.1. [Q96LT4-1]
UniGene; Hs.744986; -.
ProteinModelPortal; Q96LT4; -.
BioGrid; 126778; 1.
IntAct; Q96LT4; 2.
STRING; 9606.ENSP00000438042; -.
SwissLipids; SLP:000000704; -.
iPTMnet; Q96LT4; -.
PhosphoSitePlus; Q96LT4; -.
BioMuta; SAMD8; -.
DMDM; 44888529; -.
EPD; Q96LT4; -.
MaxQB; Q96LT4; -.
PaxDb; Q96LT4; -.
PeptideAtlas; Q96LT4; -.
PRIDE; Q96LT4; -.
DNASU; 142891; -.
Ensembl; ENST00000372687; ENSP00000361772; ENSG00000156671. [Q96LT4-2]
Ensembl; ENST00000542569; ENSP00000438042; ENSG00000156671. [Q96LT4-1]
GeneID; 142891; -.
KEGG; hsa:142891; -.
UCSC; uc001jwx.2; human. [Q96LT4-1]
CTD; 142891; -.
EuPathDB; HostDB:ENSG00000156671.12; -.
GeneCards; SAMD8; -.
HGNC; HGNC:26320; SAMD8.
HPA; HPA044402; -.
MIM; 611575; gene.
neXtProt; NX_Q96LT4; -.
OpenTargets; ENSG00000156671; -.
PharmGKB; PA134868247; -.
eggNOG; KOG3058; Eukaryota.
eggNOG; ENOG410XNSC; LUCA.
GeneTree; ENSGT00390000001630; -.
HOGENOM; HOG000233822; -.
HOVERGEN; HBG048216; -.
InParanoid; Q96LT4; -.
PhylomeDB; Q96LT4; -.
TreeFam; TF314547; -.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
GenomeRNAi; 142891; -.
PRO; PR:Q96LT4; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000156671; -.
CleanEx; HS_SAMD8; -.
ExpressionAtlas; Q96LT4; baseline and differential.
Genevisible; Q96LT4; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IBA:GO_Central.
GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; TAS:Reactome.
GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
GO; GO:1905373; P:ceramide phosphoethanolamine biosynthetic process; IEA:Ensembl.
GO; GO:2000303; P:regulation of ceramide biosynthetic process; IDA:UniProtKB.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
GO; GO:0006686; P:sphingomyelin biosynthetic process; NAS:UniProtKB.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR025749; Sphingomyelin_synth-like_dom.
Pfam; PF14360; PAP2_C; 1.
Pfam; PF00536; SAM_1; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Lipid metabolism; Membrane; Reference proteome;
Sphingolipid metabolism; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 415 Sphingomyelin synthase-related protein 1.
/FTId=PRO_0000221080.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TRANSMEM 201 221 Helical. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TRANSMEM 277 297 Helical. {ECO:0000255}.
TRANSMEM 322 342 Helical. {ECO:0000255}.
TRANSMEM 347 367 Helical. {ECO:0000255}.
TOPO_DOM 368 415 Cytoplasmic. {ECO:0000255}.
DOMAIN 12 78 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ACT_SITE 301 301 {ECO:0000250}.
ACT_SITE 344 344 {ECO:0000250}.
ACT_SITE 348 348
VAR_SEQ 315 326 YTPRSWNFLHTL -> CKYLFSASMRIR (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_038403.
VAR_SEQ 327 415 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038404.
MUTAGEN 348 348 D->E: Abolishes CPE synthase activity.
{ECO:0000269|PubMed:19506037}.
SEQUENCE 415 AA; 48321 MW; AAED366F56C9CDC9 CRC64;
MAGPNQLCIR RWTTKHVAVW LKDEGFFEYV DILCNKHRLD GITLLTLTEY DLRSPPLEIK
VLGDIKRLML SVRKLQKIHI DVLEEMGYNS DSPMGSMTPF ISALQSTDWL CNGELSHDCD
GPITDLNSDQ YQYMNGKNKH SVRRLDPEYW KTILSCIYVF IVFGFTSFIM VIVHERVPDM
QTYPPLPDIF LDSVPRIPWA FAMTEVCGMI LCYIWLLVLL LHKHRSILLR RLCSLMGTVF
LLRCFTMFVT SLSVPGQHLQ CTGKIYGSVW EKLHRAFAIW SGFGMTLTGV HTCGDYMFSG
HTVVLTMLNF FVTEYTPRSW NFLHTLSWVL NLFGIFFILA AHEHYSIDVF IAFYITTRLF
LYYHTLANTR AYQQSRRARI WFPMFSFFEC NVNGTVPNEY CWPFSKPAIM KRLIG


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