ID   SIAT9_MOUSE             Reviewed;         414 AA.
AC   O88829; B2RRS1; Q3TMT6; Q3TY01; Q91YF2; Q91YF3; Q9CZ65; Q9QWF8; Q9QWF9;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=Lactosylceramide alpha-2,3-sialyltransferase;
DE            EC=2.4.3.9 {ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:12629211, ECO:0000269|PubMed:9875239};
DE   AltName: Full=CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase;
DE   AltName: Full=Ganglioside GM3 synthase;
DE   AltName: Full=ST3Gal V;
DE            Short=ST3GalV;
DE   AltName: Full=Sialyltransferase 9;
GN   Name=St3gal5; Synonyms=GM3S, Siat9;
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] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=9875239; DOI=10.1006/bbrc.1998.9768;
RA   Kono M., Takashima S., Liu H., Inoue M., Kojima N., Young-Choon L.,
RA   Hamamoto T., Tsuji S.;
RT   "Molecular cloning and characterization of fifth type of beta-galactoside
RT   alpha-2,3-sialyltransferase (ST3Gal V; GM3 synthase).";
RL   Biochem. Biophys. Res. Commun. 253:170-175(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Ishii A., Saito M.;
RT   "Mouse GM3 Synthase cDNA.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Kapitonov D., Yu R.K.;
RT   "Combinatorial PCR in homologous cloning: cloning of GM3 synthase (ST-I).";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 52-414, FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=10092602; DOI=10.1074/jbc.274.14.9271;
RA   Fukumoto S., Miyazaki H., Goto G., Urano T., Furukawa K., Furukawa K.;
RT   "Expression cloning of mouse cDNA of CMP-NeuAc: lactosylceramide alpha2,3-
RT   sialyltransferase, an enzyme that initiates the synthesis of
RT   gangliosides.";
RL   J. Biol. Chem. 274:9271-9276(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-414.
RC   STRAIN=ICR; TISSUE=Brain;
RA   Shuichi T.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12629211; DOI=10.1073/pnas.0635898100;
RA   Yamashita T., Hashiramoto A., Haluzik M., Mizukami H., Beck S., Norton A.,
RA   Kono M., Tsuji S., Daniotti J.L., Werth N., Sandhoff R., Sandhoff K.,
RA   Proia R.L.;
RT   "Enhanced insulin sensitivity in mice lacking ganglioside GM3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:3445-3449(2003).
RN   [9]
RP   FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16115873; DOI=10.1074/jbc.m507596200;
RA   Tsukamoto K., Kohda T., Mukamoto M., Takeuchi K., Ihara H., Saito M.,
RA   Kozaki S.;
RT   "Binding of Clostridium botulinum type C and D neurotoxins to ganglioside
RT   and phospholipid. Novel insights into the receptor for clostridial
RT   neurotoxins.";
RL   J. Biol. Chem. 280:35164-35171(2005).
CC   -!- FUNCTION: (Microbial infection) Gangliosides GD1b and GT1b (derived
CC       from GM3) may serve as receptors for some C.botulinum neurotoxins
CC       (minimally types BoNT/A, B, C) (PubMed:16115873).
CC       {ECO:0000305|PubMed:16115873}.
CC   -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC       NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of
CC       glycosphingolipids forming gangliosides (important molecules involved
CC       in the regulation of multiple cellular processes, including cell
CC       proliferation and differentiation, apoptosis, embryogenesis,
CC       development, and oncogenesis) (PubMed:9875239, PubMed:10092602,
CC       PubMed:12629211). Mainly involved in the biosynthesis of ganglioside
CC       GM3 but can also use different glycolipids as substrate acceptors such
CC       as D-galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1
CC       (GA1), although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-
CC       (1<->1)-Cer (LacCer) (By similarity). {ECO:0000250|UniProtKB:Q9UNP4,
CC       ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:12629211,
CC       ECO:0000269|PubMed:9875239}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-
CC         acetyl-beta-neuraminate = a ganglioside GM3 (d18:1(4E)) + CMP + H(+);
CC         Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.3.9;
CC         Evidence={ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:12629211,
CC         ECO:0000269|PubMed:9875239};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18418;
CC         Evidence={ECO:0000305|PubMed:10092602, ECO:0000305|PubMed:12629211,
CC         ECO:0000305|PubMed:9875239};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA2
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM2 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41776, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:78485, ChEBI:CHEBI:78486;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41777;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Gal-(1<->1')-Cer + CMP-N-acetyl-beta-neuraminate = CMP
CC         + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC         (1<->1')-ceramide; Xref=Rhea:RHEA:41780, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82643,
CC         ChEBI:CHEBI:143593; Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41781;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM1 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41784, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:78484;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41785;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNP4};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88829-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88829-2; Sequence=VSP_033689;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain, and then testis, heart
CC       and liver, almost all tissues showed some levels of the gene
CC       expression. {ECO:0000269|PubMed:10092602, ECO:0000269|PubMed:9875239}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, and do not show any
CC       obvious abnormality apart from an increased sensitivity to insulin
CC       (PubMed:12629211). The major brain gangliosides derived from GM3 (GM1a,
CC       GD1a, GD1b, and GT1b) are missing (PubMed:12629211).
CC       {ECO:0000269|PubMed:12629211}.
CC   -!- DISRUPTION PHENOTYPE: (Microbial infection) Cerebellar granule cells
CC       are no longer susceptible to C.botulinum neurotoxin type C (BoNT/C),
CC       and syntaxin, the BoNT/C target, is not degraded. Cells remain
CC       susceptible to neurotoxins C.botulinum neurotoxin types CD and D
CC       (BoNT/CD and BoNT/D, botD) (PubMed:16115873). Knockout mice survive 6
CC       times longer when injected intravenously with BoNT/C; the knockout has
CC       no effects on time of survival for BoNT/CD and BoNT/D
CC       (PubMed:16115873). {ECO:0000269|PubMed:16115873}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF66147.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA33491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA76467.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB28571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE34763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA75235.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA75236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC79655.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal V;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_646";
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DR   EMBL; Y15003; CAA75235.1; ALT_INIT; mRNA.
DR   EMBL; Y15003; CAA75236.1; ALT_INIT; mRNA.
DR   EMBL; AB018048; BAA33491.1; ALT_INIT; mRNA.
DR   EMBL; AF119416; AAF66147.1; ALT_INIT; mRNA.
DR   EMBL; AK012961; BAB28571.1; ALT_INIT; mRNA.
DR   EMBL; AK159000; BAE34763.1; ALT_INIT; mRNA.
DR   EMBL; AK165726; BAE38355.1; -; mRNA.
DR   EMBL; BC138557; AAI38558.1; -; mRNA.
DR   EMBL; BC138559; AAI38560.1; -; mRNA.
DR   EMBL; AB013302; BAA76467.1; ALT_INIT; mRNA.
DR   EMBL; Y18022; CAC79654.1; -; Genomic_DNA.
DR   EMBL; Y18023; CAC79655.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS20237.1; -. [O88829-1]
DR   PIR; JE0364; JE0364.
DR   RefSeq; NP_001030305.1; NM_001035228.2. [O88829-1]
DR   RefSeq; NP_035505.2; NM_011375.3.
DR   RefSeq; XP_006505880.1; XM_006505817.3.
DR   AlphaFoldDB; O88829; -.
DR   SMR; O88829; -.
DR   BioGRID; 203247; 1.
DR   ELM; O88829; -.
DR   STRING; 10090.ENSMUSP00000070414; -.
DR   SwissLipids; SLP:000000752; -.
DR   SwissLipids; SLP:000000759; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyConnect; 2454; 4 N-Linked glycans (1 site).
DR   GlyCosmos; O88829; 3 sites, 4 glycans.
DR   GlyGen; O88829; 3 sites, 4 N-linked glycans (1 site).
DR   iPTMnet; O88829; -.
DR   PhosphoSitePlus; O88829; -.
DR   SwissPalm; O88829; -.
DR   MaxQB; O88829; -.
DR   PaxDb; 10090-ENSMUSP00000070414; -.
DR   PeptideAtlas; O88829; -.
DR   ProteomicsDB; 261398; -. [O88829-1]
DR   ProteomicsDB; 261399; -. [O88829-2]
DR   Pumba; O88829; -.
DR   Antibodypedia; 31972; 174 antibodies from 25 providers.
DR   DNASU; 20454; -.
DR   Ensembl; ENSMUST00000069994.11; ENSMUSP00000070414.5; ENSMUSG00000056091.13. [O88829-1]
DR   GeneID; 20454; -.
DR   KEGG; mmu:20454; -.
DR   UCSC; uc009chy.2; mouse. [O88829-1]
DR   AGR; MGI:1339963; -.
DR   CTD; 8869; -.
DR   MGI; MGI:1339963; St3gal5.
DR   VEuPathDB; HostDB:ENSMUSG00000056091; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT00940000157929; -.
DR   InParanoid; O88829; -.
DR   OrthoDB; 5404317at2759; -.
DR   PhylomeDB; O88829; -.
DR   TreeFam; TF352819; -.
DR   BRENDA; 2.4.99.9; 3474.
DR   Reactome; R-MMU-4085001; Sialic acid metabolism.
DR   BioGRID-ORCS; 20454; 5 hits in 80 CRISPR screens.
DR   ChiTaRS; St3gal5; mouse.
DR   PRO; PR:O88829; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; O88829; Protein.
DR   Bgee; ENSMUSG00000056091; Expressed in granulocyte and 249 other cell types or tissues.
DR   ExpressionAtlas; O88829; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047291; F:lactosylceramide alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   PANTHER; PTHR13713:SF60; LACTOSYLCERAMIDE ALPHA-2,3-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR13713; SIALYLTRANSFERASE; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   Genevisible; O88829; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..414
FT                   /note="Lactosylceramide alpha-2,3-sialyltransferase"
FT                   /id="PRO_0000149303"
FT   TOPO_DOM        1..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..414
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        194..352
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..26
FT                   /note="MHTEAVGGAARRPQKLRSQAAAPACR -> MGAPGELRRCGRGAA (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9875239"
FT                   /id="VSP_033689"
FT   CONFLICT        139
FT                   /note="N -> K (in Ref. 4; BAE34763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="P -> S (in Ref. 1; CAA75235/CAA75236)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="H -> Y (in Ref. 4; BAE34763)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  47360 MW;  3BC5AEE20D7627DD CRC64;
     MHTEAVGGAA RRPQKLRSQA AAPACRAMPS EFTSAKLRSD CSRTSLQWYT RTQHKMRRPS
     LLIKDICKCT LVAFGVWLLY ILILNYTAEE CDMKRMHYVD PDRIKRAQSY AQEVLQKECR
     PRYAKTAMAL LFEDRYSINL EPFVQKVPTA SEAELKYDPP FGFRKFSSKV QSLLDMLPEH
     DFPEHLRAKA CKRCVVVGNG GILHGLELGH ALNQFDVVIR LNSAPVEGYS EHVGNKTTIR
     MTYPEGAPLS DVEYYANDLF VTVLFKSVDF KWLQAMVKNE SLPFWVRLFF WKQVAEKVPL
     QPKHFRILNP VIIKETAFDI LQYSEPQSRF WGHDKNIPTI GVIAVVLATH LCDEVSLAGF
     GYDLSQPRTP LHYFDSQCMG AMHWQVMHNV TTETKFLLKL LKEGVVEDLS GGIH
//