ID   SPTC1_MOUSE             Reviewed;         473 AA.
AC   O35704; O54813; Q8BH11;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Serine palmitoyltransferase 1;
DE            EC=2.3.1.50 {ECO:0000250|UniProtKB:O15269};
DE   AltName: Full=Long chain base biosynthesis protein 1;
DE            Short=LCB 1;
DE   AltName: Full=Serine-palmitoyl-CoA transferase 1;
DE            Short=SPT 1;
DE            Short=SPT1;
GN   Name=Sptlc1; Synonyms=Lcb1;
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].
RC   STRAIN=BALB/cJ; TISSUE=Kidney, and Liver;
RX   PubMed=9363775; DOI=10.1111/j.1432-1033.1997.00239.x;
RA   Weiss B., Stoffel W.;
RT   "Human and murine serine-palmitoyl-CoA transferase. Cloning, expression and
RT   characterization of the key enzyme in sphingolipid synthesis.";
RL   Eur. J. Biochem. 249:239-247(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney, and Testis;
RX   PubMed=9405408; DOI=10.1074/jbc.272.51.32108;
RA   Hanada K., Hara T., Nishijima M., Kuge O., Dickson R.C., Nagiec M.M.;
RT   "A mammalian homolog of the yeast LCB1 encodes a component of serine
RT   palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid
RT   synthesis.";
RL   J. Biol. Chem. 272:32108-32114(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, Hypothalamus, and Lung;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [5]
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=1317856; DOI=10.1016/s0021-9258(19)49887-6;
RA   Mandon E.C., Ehses I., Rother J., van Echten G., Sandhoff K.;
RT   "Subcellular localization and membrane topology of serine
RT   palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-
RT   acyltransferase in mouse liver.";
RL   J. Biol. Chem. 267:11144-11148(1992).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INDUCTION BY HIGH FAT DIET, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21994399; DOI=10.1523/jneurosci.3883-11.2011;
RA   Geekiyanage H., Chan C.;
RT   "MicroRNA-137/181c regulates serine palmitoyltransferase and in turn
RT   amyloid beta, novel targets in sporadic Alzheimer's disease.";
RL   J. Neurosci. 31:14820-14830(2011).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH RTN4.
RX   PubMed=26301690; DOI=10.1038/nm.3934;
RA   Cantalupo A., Zhang Y., Kothiya M., Galvani S., Obinata H., Bucci M.,
RA   Giordano F.J., Jiang X.C., Hla T., Di Lorenzo A.;
RT   "Nogo-B regulates endothelial sphingolipid homeostasis to control vascular
RT   function and blood pressure.";
RL   Nat. Med. 21:1028-1037(2015).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=27818258; DOI=10.1016/j.cmet.2016.10.002;
RA   Chaurasia B., Kaddai V.A., Lancaster G.I., Henstridge D.C., Sriram S.,
RA   Galam D.L., Gopalan V., Prakash K.N., Velan S.S., Bulchand S., Tsong T.J.,
RA   Wang M., Siddique M.M., Yuguang G., Sigmundsson K., Mellet N.A., Weir J.M.,
RA   Meikle P.J., Bin M Yassin M.S., Shabbir A., Shayman J.A., Hirabayashi Y.,
RA   Shiow S.T., Sugii S., Summers S.A.;
RT   "Adipocyte Ceramides Regulate Subcutaneous Adipose Browning, Inflammation,
RT   and Metabolism.";
RL   Cell Metab. 24:820-834(2016).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=28100772; DOI=10.1074/jbc.m116.756460;
RA   Alexaki A., Clarke B.A., Gavrilova O., Ma Y., Zhu H., Ma X., Xu L.,
RA   Tuymetova G., Larman B.C., Allende M.L., Dunn T.M., Proia R.L.;
RT   "De Novo Sphingolipid Biosynthesis Is Required for Adipocyte Survival and
RT   Metabolic Homeostasis.";
RL   J. Biol. Chem. 292:3929-3939(2017).
CC   -!- FUNCTION: Component of the serine palmitoyltransferase multisubunit
CC       enzyme (SPT) that catalyzes the initial and rate-limiting step in
CC       sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA
CC       (most commonly palmitoyl-CoA) to form long-chain bases
CC       (PubMed:28100772). The SPT complex is also composed of SPTLC2 or SPTLC3
CC       and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2
CC       or SPTLC3 forms the catalytic core. The composition of the serine
CC       palmitoyltransferase (SPT) complex determines the substrate preference.
CC       The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA
CC       substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and
CC       C16-CoA as substrates, with a slight preference for C14-CoA. The
CC       SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA
CC       substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability
CC       to use a broader range of acyl-CoAs, without apparent preference (By
CC       similarity). Required for adipocyte cell viability and metabolic
CC       homeostasis (PubMed:28100772). {ECO:0000250|UniProtKB:O15269,
CC       ECO:0000269|PubMed:28100772}.
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:0000250|UniProtKB:O15269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
CC         Evidence={ECO:0000250|UniProtKB:O15269};
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:0000250|UniProtKB:O15269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33684;
CC         Evidence={ECO:0000250|UniProtKB:O15269};
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:0000250|UniProtKB:O15269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
CC         Evidence={ECO:0000250|UniProtKB:O15269};
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:0000250|UniProtKB:O15269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
CC         Evidence={ECO:0000250|UniProtKB:O15269};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: SPT complex catalytic activity is negatively
CC       regulated by ORMDL proteins, including ORMDL3, in the presence of
CC       ceramides (By similarity). This mechanism allows to maintain ceramide
CC       levels at sufficient concentrations for the production of complex
CC       sphingolipids, but which prevents the accumulation of ceramides to
CC       levels that trigger apoptosis (Probable).
CC       {ECO:0000250|UniProtKB:O15269, ECO:0000305}.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000269|PubMed:28100772}.
CC   -!- SUBUNIT: Component of the serine palmitoyltransferase (SPT) complex,
CC       which is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB (By
CC       similarity). The heterodimer with SPTLC2 or SPTLC3 forms the catalytic
CC       core of the enzyme, while SPTSSA or SPTSSB subunits determine substrate
CC       specificity (By similarity). SPT also interacts with ORMDL proteins,
CC       especially ORMDL3, which negatively regulate SPT activity in the
CC       presence of ceramides (By similarity). Forms dimers of heterodimers
CC       with SPTLC2 (By similarity). Interacts with RTN4 (isoform B)
CC       (PubMed:26301690). {ECO:0000250|UniProtKB:O15269,
CC       ECO:0000269|PubMed:26301690}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:1317856, ECO:0000269|PubMed:26301690}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:1317856}.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. Highest
CC       expression in brain, kidney and liver (PubMed:21994399). Expressed in
CC       brown and white adipose tissues (PubMed:27818258).
CC       {ECO:0000269|PubMed:21994399, ECO:0000269|PubMed:27818258}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed after birth, expression decreases
CC       2 weeks after birth and is maintained until, at least, 18 months.
CC       {ECO:0000269|PubMed:21994399}.
CC   -!- INDUCTION: Expression levels at protein level increase upon high-fat
CC       diet. mRNA levels remain unchanged. {ECO:0000269|PubMed:21994399}.
CC   -!- DOMAIN: The transmembrane domain is involved in the interaction with
CC       ORMDL3. {ECO:0000250|UniProtKB:O15269}.
CC   -!- PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell
CC       survival. {ECO:0000250|UniProtKB:O15269}.
CC   -!- DISRUPTION PHENOTYPE: Knockout are lethal at embryonic stage
CC       (PubMed:28100772). Conditional knockouts specific to the adipose tissue
CC       develop adipose tissue but exhibit a striking age dependent loss of
CC       adipose tissue accompanied by evidence of adipocyte death, increased
CC       macrophage infiltration and tissue fibrosis. They also have elevated
CC       fasting blood glucose, fatty liver and insulin resistance. They show a
CC       significant reduction of total sphingomyelin levels in the adipose
CC       tissue (PubMed:28100772). {ECO:0000269|PubMed:28100772}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X95641; CAA64897.1; -; mRNA.
DR   EMBL; AF003823; AAC02264.1; -; mRNA.
DR   EMBL; AK053207; BAC35310.1; -; mRNA.
DR   EMBL; AK079578; BAC37690.1; -; mRNA.
DR   EMBL; AK084391; BAC39172.1; -; mRNA.
DR   EMBL; AK084445; BAC39185.1; -; mRNA.
DR   EMBL; BC046323; AAH46323.1; -; mRNA.
DR   CCDS; CCDS26521.1; -.
DR   RefSeq; NP_033295.2; NM_009269.2.
DR   AlphaFoldDB; O35704; -.
DR   SMR; O35704; -.
DR   BioGRID; 234529; 7.
DR   STRING; 10090.ENSMUSP00000021920; -.
DR   GuidetoPHARMACOLOGY; 2509; -.
DR   iPTMnet; O35704; -.
DR   PhosphoSitePlus; O35704; -.
DR   EPD; O35704; -.
DR   MaxQB; O35704; -.
DR   PaxDb; 10090-ENSMUSP00000021920; -.
DR   PeptideAtlas; O35704; -.
DR   ProteomicsDB; 257058; -.
DR   Pumba; O35704; -.
DR   Antibodypedia; 2269; 431 antibodies from 37 providers.
DR   DNASU; 268656; -.
DR   Ensembl; ENSMUST00000021920.8; ENSMUSP00000021920.7; ENSMUSG00000021468.9.
DR   GeneID; 268656; -.
DR   KEGG; mmu:268656; -.
DR   UCSC; uc007qnk.2; mouse.
DR   AGR; MGI:1099431; -.
DR   CTD; 10558; -.
DR   MGI; MGI:1099431; Sptlc1.
DR   VEuPathDB; HostDB:ENSMUSG00000021468; -.
DR   eggNOG; KOG1358; Eukaryota.
DR   GeneTree; ENSGT00550000074872; -.
DR   HOGENOM; CLU_015846_0_1_1; -.
DR   InParanoid; O35704; -.
DR   OMA; LTKYGCG; -.
DR   OrthoDB; 9643at2759; -.
DR   PhylomeDB; O35704; -.
DR   TreeFam; TF314877; -.
DR   Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR   UniPathway; UPA00222; -.
DR   BioGRID-ORCS; 268656; 28 hits in 83 CRISPR screens.
DR   PRO; PR:O35704; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; O35704; Protein.
DR   Bgee; ENSMUSG00000021468; Expressed in gastrula and 261 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0017059; C:serine C-palmitoyltransferase complex; ISA:MGI.
DR   GO; GO:0035339; C:SPOTS complex; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004758; F:serine C-palmitoyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IMP:MGI.
DR   GO; GO:0061724; P:lipophagy; ISO:MGI.
DR   GO; GO:1904504; P:positive regulation of lipophagy; ISO:MGI.
DR   GO; GO:1904649; P:regulation of fat cell apoptotic process; IMP:UniProtKB.
DR   GO; GO:0046511; P:sphinganine biosynthetic process; IMP:MGI.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:MGI.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IMP:UniProtKB.
DR   GO; GO:0006686; P:sphingomyelin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IMP:MGI.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   PANTHER; PTHR13693:SF2; SERINE PALMITOYLTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; O35704; MM.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW   Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..473
FT                   /note="Serine palmitoyltransferase 1"
FT                   /id="PRO_0000163855"
FT   TOPO_DOM        1..15
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..66
FT                   /note="Interaction with SPTLC2"
FT                   /evidence="ECO:0000250|UniProtKB:O15269"
FT   MOD_RES         164
FT                   /note="Phosphotyrosine; by ABL"
FT                   /evidence="ECO:0000250|UniProtKB:O15269"
FT   CONFLICT        6..7
FT                   /note="EQ -> DE (in Ref. 2; AAC02264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="V -> E (in Ref. 2; AAC02264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="T -> A (in Ref. 1; CAA64897 and 2; AAC02264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="S -> T (in Ref. 2; AAC02264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="I -> V (in Ref. 1; CAA64897 and 2; AAC02264)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  52535 MW;  5B037E344DDEB4A7 CRC64;
     MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLVF SKTYKLQERS DLTAKEKEEL
     IEEWQPEPLV PPVSKNHPAL NYNIVSGPPT HNIVVNGKEC VNFASFNFLG LLANPRVKAT
     AFSSLKKYGV GTCGPRGFYG TFDVHLDLEE RLAKFMKTEE AIIYSYGFST IASAIPAYSK
     RGDIIFVDSA ACFAIQKGLQ ASRSDIKLFK HNDVADLERL LKEQEIEDQK NPRKARVTRR
     FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGISIDDI
     DLISANMENA LASVGGFCCG RSFVVDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP
     DIFAVLKKKC QNIHKSLQGV SGLKVVGESL SPALHLQLEE STGSREKDVK LLQAIVDQCM
     DKGIALTQAR YLDKEEKCLP PPSIRVVVTV EQTEEELQRA ASTIREAAQA VLL
//