SPTC3_HUMAN
ID SPTC3_HUMAN Reviewed; 552 AA.
AC Q9NUV7; A2A2I4; B9EK64; Q05DQ8; Q5T1U4; Q9H1L1; Q9H1Z0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine palmitoyltransferase 3 {ECO:0000305};
DE EC=2.3.1.50 {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
DE AltName: Full=Long chain base biosynthesis protein 2b;
DE Short=LCB2b;
DE AltName: Full=Long chain base biosynthesis protein 3;
DE Short=LCB 3;
DE AltName: Full=Serine-palmitoyl-CoA transferase 3;
DE Short=SPT 3;
GN Name=SPTLC3 {ECO:0000312|HGNC:HGNC:16253}; Synonyms=C20orf38, SPTLC2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=17023427; DOI=10.1074/jbc.m608066200;
RA Hornemann T., Richard S., Ruetti M.F., Wei Y., von Eckardstein A.;
RT "Cloning and initial characterization of a new subunit for mammalian
RT serine-palmitoyltransferase.";
RL J. Biol. Chem. 281:37275-37281(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-140.
RC TISSUE=Brain, Placenta, and Urinary bladder;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=19648650; DOI=10.1074/jbc.m109.023192;
RA Hornemann T., Penno A., Ruetti M.F., Ernst D., Kivrak-Pfiffner F.,
RA Rohrer L., von Eckardstein A.;
RT "The SPTLC3 subunit of serine palmitoyltransferase generates short chain
RT sphingoid bases.";
RL J. Biol. Chem. 284:26322-26330(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE SPT COMPLEX.
RX PubMed=19416851; DOI=10.1073/pnas.0811269106;
RA Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P., Eichler F.,
RA Brown R.H. Jr., Harmon J.M., Dunn T.M.;
RT "Identification of small subunits of mammalian serine palmitoyltransferase
RT that confer distinct acyl-CoA substrate specificities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009).
CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed
CC with LCB1/SPTLC1 constitutes the catalytic core. The composition of the
CC serine palmitoyltransferase (SPT) complex determines the substrate
CC preference. SPT complexes containing SPTLC3 generate shorter chain
CC sphingoid bases compared to complexes containing SPTLC2. The SPTLC1-
CC SPTLC3-SPTSSA isozyme uses C12-CoA, C14-CoA and C16-CoA as substrates,
CC with a slight preference for C14-CoA. On the other hand, the SPTLC1-
CC SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs
CC without apparent preference. {ECO:0000269|PubMed:19416851,
CC ECO:0000269|PubMed:19648650}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC Evidence={ECO:0000269|PubMed:17023427, ECO:0000269|PubMed:19416851,
CC ECO:0000269|PubMed:19648650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC Evidence={ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-oxotetradecasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:35679, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
CC Evidence={ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC Evidence={ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-oxohexadecasphinganine
CC + CO2 + CoA; Xref=Rhea:RHEA:35675, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
CC Evidence={ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC Evidence={ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-serine + octadecanoyl-CoA = 3-oxoeicosasphinganine +
CC CO2 + CoA; Xref=Rhea:RHEA:33683, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:65073;
CC Evidence={ECO:0000269|PubMed:19416851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC Evidence={ECO:0000269|PubMed:19416851};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 mM for hexadecanoyl-CoA {ECO:0000269|PubMed:19648650};
CC KM=0.03 mM for tetradecanoyl-CoA {ECO:0000269|PubMed:19648650};
CC Vmax=120 pmol/min/mg enzyme toward hexadecanoyl-CoA
CC {ECO:0000269|PubMed:19648650};
CC Vmax=60 pmol/min/mg enzyme toward tetradecanoyl-CoA
CC {ECO:0000269|PubMed:19648650};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650}.
CC -!- SUBUNIT: Heterodimer with SPTLC2 or SPTLC3. Component of the serine
CC palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2
CC or SPTLC3, and either SPTSSA or SPTSSB. The composition of the complex
CC will define the substrate specificity. {ECO:0000269|PubMed:19416851}.
CC -!- INTERACTION:
CC Q9NUV7; O15269: SPTLC1; NbExp=3; IntAct=EBI-11614219, EBI-1044323;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:19416851}; Single-pass membrane protein
CC {ECO:0000305|PubMed:19416851}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUV7-2; Sequence=VSP_028167, VSP_028168;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, except peripheral blood
CC cells and bone marrow, with highest levels in heart, kidney, liver,
CC uterus and skin. {ECO:0000269|PubMed:17023427}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05205.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK001974; BAA92012.1; -; mRNA.
DR EMBL; AL133331; CAM13116.1; -; Genomic_DNA.
DR EMBL; AL050320; CAM13116.1; JOINED; Genomic_DNA.
DR EMBL; AL109983; CAM13116.1; JOINED; Genomic_DNA.
DR EMBL; AL445589; CAM13116.1; JOINED; Genomic_DNA.
DR EMBL; AL445589; CAM16427.1; -; Genomic_DNA.
DR EMBL; AL050320; CAM16427.1; JOINED; Genomic_DNA.
DR EMBL; AL109983; CAM16427.1; JOINED; Genomic_DNA.
DR EMBL; AL133331; CAM16427.1; JOINED; Genomic_DNA.
DR EMBL; AL050320; CAM27358.1; -; Genomic_DNA.
DR EMBL; AL109983; CAM27358.1; JOINED; Genomic_DNA.
DR EMBL; AL133331; CAM27358.1; JOINED; Genomic_DNA.
DR EMBL; AL445589; CAM27358.1; JOINED; Genomic_DNA.
DR EMBL; AL109983; CAM28300.1; -; Genomic_DNA.
DR EMBL; AL050320; CAM28300.1; JOINED; Genomic_DNA.
DR EMBL; AL133331; CAM28300.1; JOINED; Genomic_DNA.
DR EMBL; AL445589; CAM28300.1; JOINED; Genomic_DNA.
DR EMBL; BC005205; AAH05205.1; ALT_SEQ; mRNA.
DR EMBL; BC020656; AAH20656.1; -; mRNA.
DR EMBL; BC150644; AAI50645.1; -; mRNA.
DR CCDS; CCDS13115.2; -. [Q9NUV7-1]
DR RefSeq; NP_060797.2; NM_018327.2. [Q9NUV7-1]
DR AlphaFoldDB; Q9NUV7; -.
DR SMR; Q9NUV7; -.
DR BioGRID; 120590; 9.
DR ComplexPortal; CPX-6665; Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSA variant.
DR ComplexPortal; CPX-6681; Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSB variant.
DR CORUM; Q9NUV7; -.
DR DIP; DIP-60753N; -.
DR IntAct; Q9NUV7; 5.
DR STRING; 9606.ENSP00000381968; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR SwissLipids; SLP:000000153; -.
DR iPTMnet; Q9NUV7; -.
DR PhosphoSitePlus; Q9NUV7; -.
DR SwissPalm; Q9NUV7; -.
DR BioMuta; SPTLC3; -.
DR DMDM; 158931158; -.
DR EPD; Q9NUV7; -.
DR jPOST; Q9NUV7; -.
DR MassIVE; Q9NUV7; -.
DR MaxQB; Q9NUV7; -.
DR PaxDb; Q9NUV7; -.
DR PeptideAtlas; Q9NUV7; -.
DR PRIDE; Q9NUV7; -.
DR ProteomicsDB; 82722; -. [Q9NUV7-1]
DR ProteomicsDB; 82723; -. [Q9NUV7-2]
DR Antibodypedia; 70994; 65 antibodies from 12 providers.
DR DNASU; 55304; -.
DR Ensembl; ENST00000399002.7; ENSP00000381968.2; ENSG00000172296.13. [Q9NUV7-1]
DR GeneID; 55304; -.
DR KEGG; hsa:55304; -.
DR MANE-Select; ENST00000399002.7; ENSP00000381968.2; NM_018327.4; NP_060797.2.
DR UCSC; uc002wod.2; human. [Q9NUV7-1]
DR CTD; 55304; -.
DR DisGeNET; 55304; -.
DR GeneCards; SPTLC3; -.
DR HGNC; HGNC:16253; SPTLC3.
DR HPA; ENSG00000172296; Low tissue specificity.
DR MIM; 611120; gene.
DR neXtProt; NX_Q9NUV7; -.
DR OpenTargets; ENSG00000172296; -.
DR PharmGKB; PA162404677; -.
DR VEuPathDB; HostDB:ENSG00000172296; -.
DR eggNOG; KOG1357; Eukaryota.
DR GeneTree; ENSGT00940000158513; -.
DR HOGENOM; CLU_015846_7_1_1; -.
DR InParanoid; Q9NUV7; -.
DR OMA; YPYFRPI; -.
DR OrthoDB; 438936at2759; -.
DR PhylomeDB; Q9NUV7; -.
DR TreeFam; TF300452; -.
DR BioCyc; MetaCyc:HS16070-MON; -.
DR BRENDA; 2.3.1.50; 2681.
DR PathwayCommons; Q9NUV7; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SignaLink; Q9NUV7; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 55304; 7 hits in 1075 CRISPR screens.
DR GenomeRNAi; 55304; -.
DR Pharos; Q9NUV7; Tbio.
DR PRO; PR:Q9NUV7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NUV7; protein.
DR Bgee; ENSG00000172296; Expressed in buccal mucosa cell and 154 other tissues.
DR ExpressionAtlas; Q9NUV7; baseline and differential.
DR Genevisible; Q9NUV7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017059; C:serine C-palmitoyltransferase complex; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046520; P:sphingoid biosynthetic process; IDA:MGI.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IDA:ComplexPortal.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Serine palmitoyltransferase 3"
FT /id="PRO_0000079426"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 102..175
FT /note="DFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGPLFDLMERVSDDYNWTFR
FT FTGRVIKDVINMGSYNFLGLAA -> VRMRTSLDLCQCLLLSKVFSEVVMQVQILESMR
FT CSGTIQGKFHSSPPPKPHYPWAYGPVFTNISWATTICHIPN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028167"
FT VAR_SEQ 176..552
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028168"
FT VARIANT 140
FT /note="L -> V (in dbSNP:rs243887)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048230"
FT VARIANT Q9NUV7-2:149
FT /note="P -> A (in dbSNP:rs934335)"
FT /evidence="ECO:0000305"
FT /id="VAR_082794"
SQ SEQUENCE 552 AA; 62049 MW; EED341220DCA683A CRC64;
MANPGGGAVC NGKLHNHKKQ SNGSQSRNCT KNGIVKEAQQ NGKPHFYDKL IVESFEEAPL
HVMVFTYMGY GIGTLFGYLR DFLRNWGIEK CNAAVERKEQ KDFVPLYQDF ENFYTRNLYM
RIRDNWNRPI CSAPGPLFDL MERVSDDYNW TFRFTGRVIK DVINMGSYNF LGLAAKYDES
MRTIKDVLEV YGTGVASTRH EMGTLDKHKE LEDLVAKFLN VEAAMVFGMG FATNSMNIPA
LVGKGCLILS DELNHTSLVL GARLSGATIR IFKHNNTQSL EKLLRDAVIY GQPRTRRAWK
KILILVEGVY SMEGSIVHLP QIIALKKKYK AYLYIDEAHS IGAVGPTGRG VTEFFGLDPH
EVDVLMGTFT KSFGASGGYI AGRKDLVDYL RVHSHSAVYA SSMSPPIAEQ IIRSLKLIMG
LDGTTQGLQR VQQLAKNTRY FRQRLQEMGF IIYGNENASV VPLLLYMPGK VAAFARHMLE
KKIGVVVVGF PATPLAEARA RFCVSAAHTR EMLDTVLEAL DEMGDLLQLK YSRHKKSARP
ELYDETSFEL ED
