GENTAUR Molecular Products.

 SAMD8_HUMAN             Reviewed;         415 AA.
 Q96LT4; Q5JSC5; Q5JSC8; Q66K52;
 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2004, sequence version 2.
 05-DEC-2018, entry version 139.
 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};
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AK057811; BAB71586.1; -; mRNA.
 EMBL; AL392111; -; NOT_ANNOTATED_CDS; 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; -.
 MaxQB; Q96LT4; -.
 PaxDb; Q96LT4; -.
 PeptideAtlas; Q96LT4; -.
 PRIDE; Q96LT4; -.
 ProteomicsDB; 77245; -.
 ProteomicsDB; 77246; -. [Q96LT4-2]
 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; ENSGT00940000155540; -.
 HOGENOM; HOG000233822; -.
 HOVERGEN; HBG048216; -.
 InParanoid; Q96LT4; -.
 KO; K22697; -.
 PhylomeDB; Q96LT4; -.
 TreeFam; TF314547; -.
 Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
 GenomeRNAi; 142891; -.
 PRO; PR:Q96LT4; -.
 Proteomes; UP000005640; Chromosome 10.
 Bgee; ENSG00000156671; Expressed in 204 organ(s), highest expression level in brain.
 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; IBA:GO_Central.
 GO; GO:0006686; P:sphingomyelin biosynthetic process; NAS:UniProtKB.
 InterPro; IPR001660; SAM.
 InterPro; IPR013761; SAM/pointed_sf.
 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

Related products :