SMS1_MOUSE
ID SMS1_MOUSE Reviewed; 419 AA.
AC Q8VCQ6; Q3UIS8; Q5J3R0; Q8C464; Q8C583; Q8C652;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1;
DE EC=2.7.8.27 {ECO:0000269|PubMed:27892528};
DE AltName: Full=Protein Mob;
DE AltName: Full=Sphingomyelin synthase 1;
DE AltName: Full=Transmembrane protein 23;
GN Name=Sgms1; Synonyms=Tmem23;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=16226406; DOI=10.1016/j.gene.2005.07.036;
RA Yang Z., Jean-Baptiste G., Khoury C., Greenwood M.T.;
RT "The mouse sphingomyelin synthase 1 (SMS1) gene is alternatively spliced to
RT yield multiple transcripts and proteins.";
RL Gene 363:123-132(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow macrophage, Embryo, Embryonic heart,
RC Embryonic spinal cord, Embryonic stem cell, Testis, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Kidney {ECO:0000269|PubMed:15489334}, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION.
RX PubMed=14685263; DOI=10.1038/sj.emboj.7600034;
RA Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.;
RT "Identification of a family of animal sphingomyelin synthases.";
RL EMBO J. 23:33-44(2004).
RN [5]
RP FUNCTION.
RX PubMed=16879426; DOI=10.1111/j.1567-1364.2006.00052.x;
RA Yang Z., Khoury C., Jean-Baptiste G., Greenwood M.T.;
RT "Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-
RT mediated cell death in yeast.";
RL FEMS Yeast Res. 6:751-762(2006).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22580896; DOI=10.1161/atvbaha.112.251538;
RA Li Z., Fan Y., Liu J., Li Y., Huan C., Bui H.H., Kuo M.S., Park T.S.,
RA Cao G., Jiang X.C.;
RT "Impact of sphingomyelin synthase 1 deficiency on sphingolipid metabolism
RT and atherosclerosis in mice.";
RL Arterioscler. Thromb. Vasc. Biol. 32:1577-1584(2012).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=22641779; DOI=10.1113/jphysiol.2012.235846;
RA Lu M.H., Takemoto M., Watanabe K., Luo H., Nishimura M., Yano M.,
RA Tomimoto H., Okazaki T., Oike Y., Song W.J.;
RT "Deficiency of sphingomyelin synthase-1 but not sphingomyelin synthase-2
RT causes hearing impairments in mice.";
RL J. Physiol. (Lond.) 590:4029-4044(2012).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27892528; DOI=10.1038/srep37829;
RA Taniguchi M., Tasaki T., Ninomiya H., Ueda Y., Kuremoto K.I., Mitsutake S.,
RA Igarashi Y., Okazaki T., Takegami T.;
RT "Sphingomyelin generated by sphingomyelin synthase 1 is involved in
RT attachment and infection with Japanese encephalitis virus.";
RL Sci. Rep. 6:37829-37829(2016).
RN [9]
RP STRUCTURE BY NMR OF 1-84.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAM-domain of mouse phosphatidyl
RT ceramidecholinephosphotransferase 1.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Major sphingomyelin synthase at the Golgi apparatus (By
CC similarity). Catalyzes the reversible transfer of phosphocholine moiety
CC in sphingomyelin biosynthesis: in the forward reaction transfers
CC phosphocholine head group of phosphatidylcholine (PC) on to ceramide
CC (CER) to form ceramide phosphocholine (sphingomyelin, SM) and
CC diacylglycerol (DAG) as by-product, and in the reverse reaction
CC transfers phosphocholine from SM to DAG to form PC and CER. The
CC direction of the reaction depends on the levels of CER and DAG in Golgi
CC membranes (By similarity). Does not use free phosphorylcholine or CDP-
CC choline as donor. Regulates receptor-mediated signal transduction via
CC mitogenic DAG and proapoptotic CER, as well as via SM, a structural
CC component of membrane rafts that serve as platforms for signal
CC transduction and protein sorting (PubMed:22580896, PubMed:16879426) (By
CC similarity). Plays a role in secretory transport via regulation of DAG
CC pool at the Golgi apparatus and its downstream effects on PRKD1 (By
CC similarity). {ECO:0000250|UniProtKB:Q86VZ5,
CC ECO:0000269|PubMed:16879426, ECO:0000269|PubMed:22580896}.
CC -!- FUNCTION: (Microbial infection) Contributes to the brain SM production
CC for Japanese encephalitis virus attachment and infection.
CC {ECO:0000269|PubMed:27892528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-
CC enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin;
CC Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27;
CC Evidence={ECO:0000269|PubMed:27892528};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766;
CC Evidence={ECO:0000305|PubMed:27892528};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-acyl-sn-3-glycerol + a sphingomyelin = a
CC 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + an N-
CC acylsphing-4-enine; Xref=Rhea:RHEA:43320, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:78421, ChEBI:CHEBI:82983;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-
CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC sphinganine-1-phosphocholine; Xref=Rhea:RHEA:41796,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:78647; Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-
CC (4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC (4R)-hydroxysphinganine-phosphocholine; Xref=Rhea:RHEA:42140,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:65107,
CC ChEBI:CHEBI:78650; Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142;
CC Evidence={ECO:0000250|UniProtKB:Q86VZ5};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:27892528}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q86VZ5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SMS1-alpha;
CC IsoId=Q8VCQ6-1; Sequence=Displayed;
CC Name=2; Synonyms=SMS1-beta;
CC IsoId=Q8VCQ6-2; Sequence=VSP_050673;
CC Name=3; Synonyms=SMS1-gamma;
CC IsoId=Q8VCQ6-3; Sequence=VSP_027225, VSP_027226;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed, isoform 2 shows a
CC more narrow distribution and isoform 3 is detected only in testis and
CC heart. {ECO:0000269|PubMed:16226406}.
CC -!- INDUCTION: [Isoform 1]: Induced by TNF-alpha.
CC {ECO:0000269|PubMed:16226406}.
CC -!- INDUCTION: [Isoform 2]: Induced by TNF-alpha.
CC {ECO:0000269|PubMed:16226406}.
CC -!- DISRUPTION PHENOTYPE: Null mice have hearing impairments with stria
CC vascularis (SV) in these mice exhibiting atrophy and disorganized
CC marginal cells resulting in significantly smaller endocochlear
CC potentials (EPs). These decreased EPs, together with abnormal KCNQ1
CC expression patterns, increase with age. There is a decrease in plasma,
CC liver, and macrophage sphingomyelin (59%, 45%, and 54%, respectively)
CC and a dramatic increase in glycosphingolipids. No change in ceramide,
CC total cholesterol, phospholipids nor triglycerides levels. Diminished
CC macrophage MAP kinase and NFKB1 activation is observed. Atherosclerosis
CC in SMS1(-/-)/LDLR(-/-) mice is significantly decreased.
CC {ECO:0000269|PubMed:22580896, ECO:0000269|PubMed:22641779}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; AY509044; AAS90514.1; -; mRNA.
DR EMBL; AK076554; BAC36390.1; -; mRNA.
DR EMBL; AK079254; BAC37590.1; -; mRNA.
DR EMBL; AK082974; BAC38717.1; -; mRNA.
DR EMBL; AK133967; BAE21960.1; -; mRNA.
DR EMBL; AK146782; BAE27428.1; -; mRNA.
DR EMBL; AK150272; BAE29428.1; -; mRNA.
DR EMBL; AK151170; BAE30173.1; -; mRNA.
DR EMBL; AK152312; BAE31117.1; -; mRNA.
DR EMBL; AK153406; BAE31966.1; -; mRNA.
DR EMBL; AK160539; BAE35856.1; -; mRNA.
DR EMBL; BC019443; AAH19443.2; -; mRNA.
DR EMBL; BC085298; AAH85298.1; -; mRNA.
DR CCDS; CCDS29750.1; -. [Q8VCQ6-1]
DR RefSeq; NP_001161997.1; NM_001168525.1. [Q8VCQ6-1]
DR RefSeq; NP_001161998.1; NM_001168526.1. [Q8VCQ6-1]
DR RefSeq; NP_659041.3; NM_144792.4. [Q8VCQ6-1]
DR RefSeq; XP_006526881.1; XM_006526818.3. [Q8VCQ6-1]
DR RefSeq; XP_006526882.1; XM_006526819.1. [Q8VCQ6-1]
DR RefSeq; XP_006526883.1; XM_006526820.3. [Q8VCQ6-1]
DR RefSeq; XP_011245503.1; XM_011247201.2.
DR RefSeq; XP_011245504.1; XM_011247202.2. [Q8VCQ6-1]
DR RefSeq; XP_011245505.1; XM_011247203.2. [Q8VCQ6-1]
DR RefSeq; XP_017173594.1; XM_017318105.1. [Q8VCQ6-3]
DR PDB; 2D8C; NMR; -; A=1-84.
DR PDBsum; 2D8C; -.
DR AlphaFoldDB; Q8VCQ6; -.
DR SMR; Q8VCQ6; -.
DR STRING; 10090.ENSMUSP00000117336; -.
DR BindingDB; Q8VCQ6; -.
DR ChEMBL; CHEMBL4523408; -.
DR PhosphoSitePlus; Q8VCQ6; -.
DR MaxQB; Q8VCQ6; -.
DR PaxDb; Q8VCQ6; -.
DR PRIDE; Q8VCQ6; -.
DR ProteomicsDB; 261459; -. [Q8VCQ6-1]
DR ProteomicsDB; 261460; -. [Q8VCQ6-2]
DR ProteomicsDB; 261461; -. [Q8VCQ6-3]
DR Antibodypedia; 27870; 206 antibodies from 25 providers.
DR DNASU; 208449; -.
DR Ensembl; ENSMUST00000099514; ENSMUSP00000097114; ENSMUSG00000040451. [Q8VCQ6-1]
DR Ensembl; ENSMUST00000142618; ENSMUSP00000117336; ENSMUSG00000040451. [Q8VCQ6-1]
DR Ensembl; ENSMUST00000151289; ENSMUSP00000123395; ENSMUSG00000040451. [Q8VCQ6-1]
DR Ensembl; ENSMUST00000152340; ENSMUSP00000119869; ENSMUSG00000040451. [Q8VCQ6-3]
DR GeneID; 208449; -.
DR KEGG; mmu:208449; -.
DR UCSC; uc008hfc.2; mouse. [Q8VCQ6-1]
DR UCSC; uc008hfh.1; mouse. [Q8VCQ6-2]
DR CTD; 259230; -.
DR MGI; MGI:2444110; Sgms1.
DR VEuPathDB; HostDB:ENSMUSG00000040451; -.
DR eggNOG; KOG3058; Eukaryota.
DR GeneTree; ENSGT00940000158306; -.
DR HOGENOM; CLU_027104_1_0_1; -.
DR InParanoid; Q8VCQ6; -.
DR OMA; WICWTLS; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q8VCQ6; -.
DR TreeFam; TF314547; -.
DR BRENDA; 2.7.8.27; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 208449; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Sgms1; mouse.
DR EvolutionaryTrace; Q8VCQ6; -.
DR PRO; PR:Q8VCQ6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VCQ6; protein.
DR Bgee; ENSMUSG00000040451; Expressed in spermatid and 254 other tissues.
DR ExpressionAtlas; Q8VCQ6; baseline and differential.
DR Genevisible; Q8VCQ6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:HGNC-UCL.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:HGNC-UCL.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; IMP:MGI.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Golgi apparatus; Kinase;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 1"
FT /id="PRO_0000221069"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..76
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184,
FT ECO:0000305"
FT ACT_SITE 291
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 334
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VZ5"
FT VAR_SEQ 215..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16226406"
FT /id="VSP_050673"
FT VAR_SEQ 215..217
FT /note="SII -> LSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16226406"
FT /id="VSP_027225"
FT VAR_SEQ 218..419
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16226406"
FT /id="VSP_027226"
FT CONFLICT 132
FT /note="S -> Y (in Ref. 2; BAC37590)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> I (in Ref. 2; BAE27428)"
FT /evidence="ECO:0000305"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2D8C"
FT TURN 28..36
FT /evidence="ECO:0007829|PDB:2D8C"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2D8C"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:2D8C"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2D8C"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2D8C"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:2D8C"
SQ SEQUENCE 419 AA; 49317 MW; 554CC26609F5F345 CRC64;
MLSARTMKEV VYWSPKKVAD WLLENAMPEY CEPLEHFTGQ DLINLTQEDF KKPPLYRVSS
DNGQRLLDMI ETLKMEHHME AHKNGHANGH LSIGVDIPNP DGSFSIKTKP NGMPNGFRKE
MIKIPMPEPE RSQYPMEWGK TFLAFLYALS CFVLTTVMIS VVHERVPPKE VQPPLPDTFF
DHFNRVQWAF SICEINGMIL VGLWLFQWLL LKYKSIISRR FFCIVGTLYL YRCITMYVTT
LPVPGMHFNC SPKLFGDWEA QVRRIMKLIA GGGLSITGSH NMCGDYLYSG HTVMLTLTYL
FIKEYSPRRL WWYHWICWLL SVVGIFCILL AHDHYTVDVV VAYYITTRLF WWYHTMANQQ
VLKEASQMNL LARVWWYRPF QYFEKNVQGI VPRSYHWPFP WPVVHLSRQV KYSRLVNDT
