SPTC2_HUMAN
ID SPTC2_HUMAN Reviewed; 562 AA.
AC O15270; Q16685;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Serine palmitoyltransferase 2 {ECO:0000305};
DE EC=2.3.1.50 {ECO:0000269|PubMed:19416851};
DE AltName: Full=Long chain base biosynthesis protein 2;
DE Short=LCB 2;
DE AltName: Full=Long chain base biosynthesis protein 2a;
DE Short=LCB2a;
DE AltName: Full=Serine-palmitoyl-CoA transferase 2;
DE Short=SPT 2;
GN Name=SPTLC2 {ECO:0000312|HGNC:HGNC:11278}; Synonyms=KIAA0526, LCB2;
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].
RC TISSUE=Pancreas;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 60-470.
RC TISSUE=Pancreatic islet;
RX PubMed=8921873; DOI=10.1016/0378-1119(96)00309-5;
RA Nagiec M.M., Lester R.L., Dickson R.C.;
RT "Sphingolipid synthesis: identification and characterization of mammalian
RT cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase.";
RL Gene 177:237-241(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-144.
RC TISSUE=Pancreatic islet;
RX PubMed=7506601; DOI=10.1093/hmg/2.11.1793;
RA Takeda J., Yano H., Eng S., Zeng Y., Bell G.I.;
RT "A molecular inventory of human pancreatic islets: sequence analysis of
RT 1000 cDNA clones.";
RL Hum. Mol. Genet. 2:1793-1798(1993).
RN [7]
RP TISSUE 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 [8]
RP FUNCTION.
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 [9]
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).
RN [10]
RP FUNCTION, VARIANTS HSAN1C MET-359; VAL-382 AND PHE-504, AND
RP CHARACTERIZATION OF VARIANTS HSAN1C MET-359; VAL-382 AND PHE-504.
RX PubMed=20920666; DOI=10.1016/j.ajhg.2010.09.010;
RA Rotthier A., Auer-Grumbach M., Janssens K., Baets J., Penno A.,
RA Almeida-Souza L., Van Hoof K., Jacobs A., De Vriendt E.,
RA Schlotter-Weigel B., Loscher W., Vondracek P., Seeman P., De Jonghe P.,
RA Van Dijck P., Jordanova A., Hornemann T., Timmerman V.;
RT "Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause
RT hereditary sensory and autonomic neuropathy type I.";
RL Am. J. Hum. Genet. 87:513-522(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INDUCTION IN ALZHEIMER DISEASE.
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 [13]
RP VARIANT HSAN1C PRO-182, CHARACTERIZATION OF VARIANT HSAN1C PRO-182, AND
RP PATHOLOGICAL MECHANISM.
RX PubMed=23658386; DOI=10.1212/wnl.0b013e318295d789;
RA Murphy S.M., Ernst D., Wei Y., Laura M., Liu Y.T., Polke J., Blake J.,
RA Winer J., Houlden H., Hornemann T., Reilly M.M.;
RT "Hereditary sensory and autonomic neuropathy type 1 (HSANI) caused by a
RT novel mutation in SPTLC2.";
RL Neurology 80:2106-2111(2013).
RN [14]
RP VARIANT HSAN1C TRP-183, AND CHARACTERIZATION OF VARIANT HSAN1C TRP-183.
RX PubMed=26573920; DOI=10.1007/s12017-015-8379-1;
RA Suriyanarayanan S., Auranen M., Toppila J., Paetau A., Shcherbii M.,
RA Palin E., Wei Y., Lohioja T., Schlotter-Weigel B., Schoen U., Abicht A.,
RA Rautenstrauss B., Tyynismaa H., Walter M.C., Hornemann T., Ylikallio E.;
RT "The Variant p.(Arg183Trp) in SPTLC2 Causes Late-Onset Hereditary Sensory
RT Neuropathy.";
RL NeuroMolecular Med. 18:81-90(2016).
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. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference
CC for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays
CC a preference for C18-CoA substrate. Plays an important role in de novo
CC sphyngolipid biosynthesis which is crucial for adipogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P97363,
CC ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650,
CC ECO:0000269|PubMed:20920666}.
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:19416851};
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 -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer with SPTLC1. 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P97363}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P97363}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17023427}.
CC -!- INDUCTION: Expression at protein level is highly increased in brains of
CC patients with Alzheimer disease. No changes are observed at mRNA level.
CC {ECO:0000269|PubMed:21994399}.
CC -!- DISEASE: Neuropathy, hereditary sensory and autonomic, 1C (HSAN1C)
CC [MIM:613640]: A form of hereditary sensory and autonomic neuropathy, a
CC genetically and clinically heterogeneous group of disorders
CC characterized by degeneration of dorsal root and autonomic ganglion
CC cells, and by prominent sensory abnormalities with a variable degree of
CC motor and autonomic dysfunction. The neurological phenotype is often
CC complicated by severe infections, osteomyelitis, and amputations.
CC HSAN1C symptoms include loss of touch and vibration in the feet,
CC dysesthesia and severe panmodal sensory loss in the upper and lower
CC limbs, distal lower limb sensory loss with ulceration and
CC osteomyelitis, and distal muscle weakness.
CC {ECO:0000269|PubMed:20920666, ECO:0000269|PubMed:23658386,
CC ECO:0000269|PubMed:26573920}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. SPTLC2 disease mutations
CC cause a shift in the substrate specificity of SPT resulting in the
CC alternative use of L-alanine and L-glycine over its canonical substrate
CC L-serine. This leads to the production of 1-deoxysphingolipids that
CC cannot be correctly metabolized (PubMed:23658386).
CC {ECO:0000269|PubMed:23658386, ECO:0000269|PubMed:26573920}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25452.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y08686; CAA69942.1; -; mRNA.
DR EMBL; AB011098; BAA25452.2; ALT_INIT; mRNA.
DR EMBL; AF111168; AAD09621.1; -; Genomic_DNA.
DR EMBL; BC005123; AAH05123.1; -; mRNA.
DR EMBL; U15555; AAC50871.1; -; mRNA.
DR CCDS; CCDS9865.1; -.
DR PIR; I38873; I38873.
DR RefSeq; NP_004854.1; NM_004863.3.
DR PDB; 6M4N; EM; 3.80 A; B/F=1-562.
DR PDB; 6M4O; EM; 3.40 A; T=1-562.
DR PDB; 7CQI; EM; 3.20 A; T=1-562.
DR PDB; 7CQK; EM; 3.30 A; T=1-562.
DR PDB; 7K0I; EM; 3.30 A; B/E=1-544.
DR PDB; 7K0J; EM; 3.10 A; B=1-562.
DR PDB; 7K0K; EM; 2.60 A; B=1-562.
DR PDB; 7K0L; EM; 3.40 A; B=1-562.
DR PDB; 7K0M; EM; 2.90 A; B/F=1-544.
DR PDB; 7K0N; EM; 3.10 A; B/F=1-562.
DR PDB; 7K0O; EM; 3.10 A; B/F=1-544.
DR PDB; 7K0P; EM; 3.10 A; B/F=1-544.
DR PDB; 7K0Q; EM; 3.30 A; B=1-562.
DR PDBsum; 6M4N; -.
DR PDBsum; 6M4O; -.
DR PDBsum; 7CQI; -.
DR PDBsum; 7CQK; -.
DR PDBsum; 7K0I; -.
DR PDBsum; 7K0J; -.
DR PDBsum; 7K0K; -.
DR PDBsum; 7K0L; -.
DR PDBsum; 7K0M; -.
DR PDBsum; 7K0N; -.
DR PDBsum; 7K0O; -.
DR PDBsum; 7K0P; -.
DR PDBsum; 7K0Q; -.
DR AlphaFoldDB; O15270; -.
DR SMR; O15270; -.
DR BioGRID; 114894; 116.
DR ComplexPortal; CPX-6663; Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSA variant.
DR ComplexPortal; CPX-6664; Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSB variant.
DR CORUM; O15270; -.
DR DIP; DIP-34604N; -.
DR IntAct; O15270; 30.
DR MINT; O15270; -.
DR STRING; 9606.ENSP00000216484; -.
DR BindingDB; O15270; -.
DR ChEMBL; CHEMBL1250344; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00133; Serine.
DR iPTMnet; O15270; -.
DR PhosphoSitePlus; O15270; -.
DR SwissPalm; O15270; -.
DR BioMuta; SPTLC2; -.
DR EPD; O15270; -.
DR jPOST; O15270; -.
DR MassIVE; O15270; -.
DR MaxQB; O15270; -.
DR PaxDb; O15270; -.
DR PeptideAtlas; O15270; -.
DR PRIDE; O15270; -.
DR ProteomicsDB; 48559; -.
DR Antibodypedia; 26092; 278 antibodies from 29 providers.
DR DNASU; 9517; -.
DR Ensembl; ENST00000216484.7; ENSP00000216484.2; ENSG00000100596.8.
DR GeneID; 9517; -.
DR KEGG; hsa:9517; -.
DR MANE-Select; ENST00000216484.7; ENSP00000216484.2; NM_004863.4; NP_004854.1.
DR UCSC; uc001xub.4; human.
DR CTD; 9517; -.
DR DisGeNET; 9517; -.
DR GeneCards; SPTLC2; -.
DR HGNC; HGNC:11278; SPTLC2.
DR HPA; ENSG00000100596; Low tissue specificity.
DR MalaCards; SPTLC2; -.
DR MIM; 605713; gene.
DR MIM; 613640; phenotype.
DR neXtProt; NX_O15270; -.
DR OpenTargets; ENSG00000100596; -.
DR Orphanet; 36386; Hereditary sensory and autonomic neuropathy type 1.
DR PharmGKB; PA36107; -.
DR VEuPathDB; HostDB:ENSG00000100596; -.
DR eggNOG; KOG1357; Eukaryota.
DR GeneTree; ENSGT00940000155786; -.
DR HOGENOM; CLU_015846_7_1_1; -.
DR InParanoid; O15270; -.
DR OMA; IEDEPPY; -.
DR OrthoDB; 438936at2759; -.
DR PhylomeDB; O15270; -.
DR TreeFam; TF300452; -.
DR BioCyc; MetaCyc:HS02117-MON; -.
DR BRENDA; 2.3.1.50; 2681.
DR PathwayCommons; O15270; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR SABIO-RK; O15270; -.
DR SignaLink; O15270; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 9517; 98 hits in 1094 CRISPR screens.
DR ChiTaRS; SPTLC2; human.
DR GeneWiki; SPTLC2; -.
DR GenomeRNAi; 9517; -.
DR Pharos; O15270; Tchem.
DR PRO; PR:O15270; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O15270; protein.
DR Bgee; ENSG00000100596; Expressed in corpus callosum and 192 other tissues.
DR ExpressionAtlas; O15270; baseline and differential.
DR Genevisible; O15270; 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:0060612; P:adipose tissue development; ISS:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR GO; GO:1904504; P:positive regulation of lipophagy; IDA:MGI.
DR GO; GO:0046511; P:sphinganine biosynthetic process; IEA:Ensembl.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IEA:Ensembl.
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 3D-structure; Acyltransferase; Disease variant; Endoplasmic reticulum;
KW Lipid metabolism; Membrane; Neurodegeneration; Neuropathy;
KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..562
FT /note="Serine palmitoyltransferase 2"
FT /id="PRO_0000163858"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 379
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VARIANT 182
FT /note="A -> P (in HSAN1C; reduced activity with L-serine as
FT substrate; increased activity toward L-alanine resulting in
FT the accumulation of 1-deoxy-sphinganine;
FT dbSNP:rs864621998)"
FT /evidence="ECO:0000269|PubMed:23658386"
FT /id="VAR_069525"
FT VARIANT 183
FT /note="R -> W (in HSAN1C; late onset; slightly increased
FT activity with L-serine as substrate; highly increased
FT activity toward L-alanine resulting in the accumulation of
FT 1-deoxy-sphinganine; dbSNP:rs775437084)"
FT /evidence="ECO:0000269|PubMed:26573920"
FT /id="VAR_081286"
FT VARIANT 359
FT /note="V -> M (in HSAN1C; partial loss of normal activity
FT as measured by reduced formation of sphinganine; affects
FT enzymatic affinity resulting in the accumulation of the
FT alternative metabolite 1-deoxy-sphinganine;
FT dbSNP:rs267607090)"
FT /evidence="ECO:0000269|PubMed:20920666"
FT /id="VAR_064798"
FT VARIANT 382
FT /note="G -> V (in HSAN1C; complete loss of normal activity
FT as measured by lack of formation of sphinganine; affects
FT enzymatic affinity resulting in the accumulation of the
FT alternative metabolite 1-deoxy-sphinganine;
FT dbSNP:rs267607089)"
FT /evidence="ECO:0000269|PubMed:20920666"
FT /id="VAR_064799"
FT VARIANT 504
FT /note="I -> F (in HSAN1C; partial loss of normal activity
FT as measured by reduced formation of sphinganine; affects
FT enzymatic affinity resulting in the accumulation of the
FT alternative metabolite 1-deoxy-sphinganine;
FT dbSNP:rs267607091)"
FT /evidence="ECO:0000269|PubMed:20920666"
FT /id="VAR_064800"
FT CONFLICT 61..64
FT /note="EAFE -> TLAR (in Ref. 5; AAC50871)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..469
FT /note="KECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVV -> NGITIHEVVQTRNT
FT YHRFSPLSPVFSHQCLWIML (in Ref. 5)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6M4O"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:7CQI"
FT HELIX 68..93
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7CQI"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7K0J"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:7CQI"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:7K0N"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7CQI"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7K0N"
FT TURN 207..211
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 346..351
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:7K0N"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 378..381
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:7K0N"
FT HELIX 434..456
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:7K0M"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:7K0K"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:7K0K"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:6M4O"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:7K0K"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:7CQI"
FT HELIX 518..535
FT /evidence="ECO:0007829|PDB:7K0K"
SQ SEQUENCE 562 AA; 62924 MW; 0C1AA1E233DE36F1 CRC64;
MRPEPGGCCC RRTVRANGCV ANGEVRNGYV RSSAAAAAAA AAGQIHHVTQ NGGLYKRPFN
EAFEETPMLV AVLTYVGYGV LTLFGYLRDF LRYWRIEKCH HATEREEQKD FVSLYQDFEN
FYTRNLYMRI RDNWNRPICS VPGARVDIME RQSHDYNWSF KYTGNIIKGV INMGSYNYLG
FARNTGSCQE AAAKVLEEYG AGVCSTRQEI GNLDKHEELE ELVARFLGVE AAMAYGMGFA
TNSMNIPALV GKGCLILSDE LNHASLVLGA RLSGATIRIF KHNNMQSLEK LLKDAIVYGQ
PRTRRPWKKI LILVEGIYSM EGSIVRLPEV IALKKKYKAY LYLDEAHSIG ALGPTGRGVV
EYFGLDPEDV DVMMGTFTKS FGASGGYIGG KKELIDYLRT HSHSAVYATS LSPPVVEQII
TSMKCIMGQD GTSLGKECVQ QLAENTRYFR RRLKEMGFII YGNEDSPVVP LMLYMPAKIG
AFGREMLKRN IGVVVVGFPA TPIIESRARF CLSAAHTKEI LDTALKEIDE VGDLLQLKYS
RHRLVPLLDR PFDETTYEET ED
