GENTAUR Molecular Products.

 SAP3_HUMAN              Reviewed;         193 AA.
 P17900; B2R699; D3DQH6; Q14426; Q14428; Q6LBL5;
 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
 13-NOV-2007, sequence version 4.
 13-FEB-2019, entry version 187.
 RecName: Full=Ganglioside GM2 activator;
 AltName: Full=Cerebroside sulfate activator protein;
 AltName: Full=GM2-AP;
 AltName: Full=Sphingolipid activator protein 3;
          Short=SAP-3;
 Contains:
   RecName: Full=Ganglioside GM2 activator isoform short;
 Flags: Precursor;
 Name=GM2A;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-59 AND VAL-69.
 PubMed=2059210; DOI=10.1016/0006-291X(91)90671-S;
 Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.;
 "Isolation and expression of a full-length cDNA encoding the human G-
 M2 activator protein.";
 Biochem. Biophys. Res. Commun. 177:1217-1223(1991).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
 PubMed=1915857; DOI=10.1016/0014-5793(91)81084-L;
 Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K.,
 Sandhoff K.;
 "Characterization of full-length cDNAs and the gene coding for the
 human GM2 activator protein.";
 FEBS Lett. 289:260-264(1991).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Placenta;
 PubMed=1554364; DOI=10.1042/bj2820807;
 Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.;
 "Evidence for two cDNAs encoding human GM2-activator protein.";
 Biochem. J. 282:807-813(1992).
 [4]
 NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
 PubMed=1427911; DOI=10.1016/S0888-7543(05)80190-9;
 Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.;
 "Identification of a processed pseudogene related to the functional
 gene encoding the GM2 activator protein: localization of the
 pseudogene to human chromosome 3 and the functional gene to human
 chromosome 5.";
 Genomics 14:796-798(1992).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-19 AND
 VAL-69.
 TISSUE=Substantia nigra;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15372022; DOI=10.1038/nature02919;
 Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
 Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
 She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
 Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
 Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
 Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
 Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
 Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
 Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
 Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
 Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
 Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
 Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
 Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
 "The DNA sequence and comparative analysis of human chromosome 5.";
 Nature 431:268-274(2004).
 [7]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-19; VAL-59 AND
 VAL-69.
 PubMed=10364519; DOI=10.1086/302463;
 Chen B., Rigat B., Curry C., Mahuran D.J.;
 "Structure of the GM2A gene: identification of an exon 2 nonsense
 mutation and a naturally occurring transcript with an in-frame
 deletion of exon 2.";
 Am. J. Hum. Genet. 65:77-87(1999).
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-59 AND
 VAL-69.
 TISSUE=Uterus;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [10]
 NUCLEOTIDE SEQUENCE [MRNA] OF 15-193, AND VARIANTS THR-19; VAL-59 AND
 VAL-69.
 PubMed=2753159; DOI=10.1016/0014-5793(89)81454-1;
 Schroeder M., Klima H., Nakano T., Kwon H., Quintern L.E.,
 Gaertner S., Suzuki K., Sandhoff K.;
 "Isolation of a cDNA encoding the human GM2 activator protein.";
 FEBS Lett. 251:197-200(1989).
 [11]
 PROTEIN SEQUENCE OF 32-193.
 TISSUE=Kidney;
 PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x;
 Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.;
 "The complete amino-acid sequences of human ganglioside GM2 activator
 protein and cerebroside sulfate activator protein.";
 Eur. J. Biochem. 192:709-714(1990).
 [12]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=25944712; DOI=10.1002/pmic.201400617;
 Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
 Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
 "N-terminome analysis of the human mitochondrial proteome.";
 Proteomics 15:2519-2524(2015).
 [13]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
 PubMed=11090283; DOI=10.1006/jmbi.2000.4225;
 Wright C.S., Li S.-C., Rastinejad F.;
 "Crystal structure of human GM2-activator protein with a novel beta-
 cup topology.";
 J. Mol. Biol. 304:411-422(2000).
 [14]
 VARIANT GM2GAB ARG-138.
 PubMed=1915858; DOI=10.1016/0014-5793(91)81211-P;
 Schroeder M., Schnabel D., Suzuki K., Sandhoff K.;
 "A mutation in the gene of a glycolipid-binding protein (GM2
 activator) that causes GM2-gangliosidosis variant AB.";
 FEBS Lett. 290:1-3(1991).
 [15]
 VARIANT GM2GAB PRO-169.
 PubMed=8244332; DOI=10.1007/BF00216446;
 Schroder M., Schnabel D., Hurwitz R., Young E., Suzuki K.,
 Sandhoff K.;
 "Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation
 and expression in BHK cells.";
 Hum. Genet. 92:437-440(1993).
 [16]
 VARIANT GM2GAB LYS-88 DEL.
 PubMed=8900233;
 Schepers U., Glombitza G., Lemm T., Hoffmann A., Chabas A., Ozand P.,
 Sandhoff K.;
 "Molecular analysis of a GM2-activator deficiency in two patients with
 GM2-gangliosidosis AB variant.";
 Am. J. Hum. Genet. 59:1048-1056(1996).
 -!- FUNCTION: The large binding pocket can accommodate several single
     chain phospholipids and fatty acids, GM2A also exhibits some
     calcium-independent phospholipase activity (By similarity). Binds
     gangliosides and stimulates ganglioside GM2 degradation. It
     stimulates only the breakdown of ganglioside GM2 and glycolipid
     GA2 by beta-hexosaminidase A. It extracts single GM2 molecules
     from membranes and presents them in soluble form to beta-
     hexosaminidase A for cleavage of N-acetyl-D-galactosamine and
     conversion to GM3. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Lysosome.
 -!- PTM: The serines in positions 32 and 33 are absent in 80% of the
     sequenced protein.
 -!- DISEASE: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal
     recessive lysosomal storage disease marked by the accumulation of
     GM2 gangliosides in the neuronal cells. It is characterized by GM2
     gangliosides accumulation in the presence of both normal
     hexosaminidase A and B. {ECO:0000269|PubMed:1915858,
     ECO:0000269|PubMed:8244332, ECO:0000269|PubMed:8900233}. Note=The
     disease is caused by mutations affecting the gene represented in
     this entry.
 -!- SEQUENCE CAUTION:
     Sequence=CAA43408.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
     Sequence=CAA43994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
 -----------------------------------------------------------------------
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 EMBL; M76477; AAA35907.1; -; mRNA.
 EMBL; X62078; CAA43993.1; -; mRNA.
 EMBL; X62078; CAA43994.1; ALT_INIT; mRNA.
 EMBL; X61095; CAA43408.1; ALT_INIT; mRNA.
 EMBL; L01439; AAA52767.1; -; mRNA.
 EMBL; AF124719; AAD25741.1; -; Genomic_DNA.
 EMBL; AF124717; AAD25741.1; JOINED; Genomic_DNA.
 EMBL; AF124718; AAD25741.1; JOINED; Genomic_DNA.
 EMBL; AK312494; BAG35396.1; -; mRNA.
 EMBL; AC008385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471062; EAW61680.1; -; Genomic_DNA.
 EMBL; CH471062; EAW61681.1; -; Genomic_DNA.
 EMBL; BC009273; AAH09273.1; -; mRNA.
 EMBL; X16087; CAA34215.1; -; mRNA.
 CCDS; CCDS4313.1; -.
 PIR; I54178; I54178.
 PIR; S13195; S13195.
 PIR; S22411; S22411.
 RefSeq; NP_000396.2; NM_000405.4.
 UniGene; Hs.483873; -.
 PDB; 1G13; X-ray; 2.00 A; A/B/C=32-193.
 PDB; 1PU5; X-ray; 1.90 A; A/B/C=32-193.
 PDB; 1PUB; X-ray; 2.51 A; A=32-193.
 PDB; 1TJJ; X-ray; 2.00 A; A/B/C=32-193.
 PDB; 2AF9; X-ray; 2.00 A; A=32-193.
 PDB; 2AG2; X-ray; 2.00 A; A/B/C=32-193.
 PDB; 2AG4; X-ray; 1.80 A; A/B=32-193.
 PDB; 2AG9; X-ray; 2.20 A; A/B=32-193.
 PDBsum; 1G13; -.
 PDBsum; 1PU5; -.
 PDBsum; 1PUB; -.
 PDBsum; 1TJJ; -.
 PDBsum; 2AF9; -.
 PDBsum; 2AG2; -.
 PDBsum; 2AG4; -.
 PDBsum; 2AG9; -.
 ProteinModelPortal; P17900; -.
 SMR; P17900; -.
 BioGrid; 109022; 27.
 IntAct; P17900; 3.
 STRING; 9606.ENSP00000349687; -.
 DrugBank; DB04660; Choline alfoscerate.
 DrugBank; DB02325; Isopropyl Alcohol.
 DrugBank; DB03017; Lauric Acid.
 DrugBank; DB03633; Lpc-Ether.
 DrugBank; DB08231; MYRISTIC ACID.
 DrugBank; DB02261; Platelet Activating Factor.
 SwissLipids; SLP:000000476; -.
 BioMuta; GM2A; -.
 DMDM; 160331912; -.
 EPD; P17900; -.
 jPOST; P17900; -.
 MaxQB; P17900; -.
 PaxDb; P17900; -.
 PeptideAtlas; P17900; -.
 PRIDE; P17900; -.
 ProteomicsDB; 53524; -.
 DNASU; 2760; -.
 Ensembl; ENST00000357164; ENSP00000349687; ENSG00000196743.
 GeneID; 2760; -.
 KEGG; hsa:2760; -.
 UCSC; uc003ltr.5; human.
 CTD; 2760; -.
 DisGeNET; 2760; -.
 EuPathDB; HostDB:ENSG00000196743.8; -.
 GeneCards; GM2A; -.
 H-InvDB; HIX0005327; -.
 HGNC; HGNC:4367; GM2A.
 HPA; HPA008063; -.
 MalaCards; GM2A; -.
 MIM; 272750; phenotype.
 MIM; 613109; gene.
 neXtProt; NX_P17900; -.
 OpenTargets; ENSG00000196743; -.
 Orphanet; 309246; GM2 gangliosidosis, AB variant.
 PharmGKB; PA28752; -.
 eggNOG; ENOG410IX9N; Eukaryota.
 eggNOG; ENOG4111JSM; LUCA.
 GeneTree; ENSGT00390000003288; -.
 HOGENOM; HOG000031350; -.
 HOVERGEN; HBG000260; -.
 InParanoid; P17900; -.
 KO; K12383; -.
 OMA; WLSTGNY; -.
 OrthoDB; 1548356at2759; -.
 PhylomeDB; P17900; -.
 TreeFam; TF353575; -.
 Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
 Reactome; R-HSA-6798695; Neutrophil degranulation.
 ChiTaRS; GM2A; human.
 EvolutionaryTrace; P17900; -.
 GeneWiki; GM2A; -.
 GenomeRNAi; 2760; -.
 PRO; PR:P17900; -.
 Proteomes; UP000005640; Chromosome 5.
 Bgee; ENSG00000196743; Expressed in 239 organ(s), highest expression level in visceral pleura.
 ExpressionAtlas; P17900; baseline and differential.
 Genevisible; P17900; HS.
 GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
 GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
 GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
 GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005576; C:extracellular region; TAS:Reactome.
 GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
 GO; GO:0032428; F:beta-N-acetylgalactosaminidase activity; IEA:Ensembl.
 GO; GO:0005319; F:lipid transporter activity; IEA:Ensembl.
 GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
 GO; GO:0030290; F:sphingolipid activator protein activity; TAS:Reactome.
 GO; GO:0006689; P:ganglioside catabolic process; IEA:Ensembl.
 GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
 GO; GO:0007611; P:learning or memory; IEA:Ensembl.
 GO; GO:0019915; P:lipid storage; IEA:Ensembl.
 GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
 GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
 GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
 GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
 Gene3D; 2.70.220.10; -; 1.
 InterPro; IPR028996; GM2-AP.
 InterPro; IPR036846; GM2-AP_sf.
 InterPro; IPR003172; ML_dom.
 PANTHER; PTHR17357; PTHR17357; 1.
 Pfam; PF02221; E1_DerP2_DerF2; 1.
 SMART; SM00737; ML; 1.
 SUPFAM; SSF63707; SSF63707; 1.
 1: Evidence at protein level;
 3D-structure; Complete proteome; Direct protein sequencing;
 Disease mutation; Disulfide bond; Gangliosidosis; Glycoprotein;
 Hydrolase; Lipid metabolism; Lysosome; Polymorphism;
 Reference proteome; Signal; Sphingolipid metabolism.
 SIGNAL        1     23       {ECO:0000255}.
 PROPEP       24     31       {ECO:0000269|PubMed:2209618}.
                              /FTId=PRO_0000031639.
 CHAIN        32    193       Ganglioside GM2 activator.
                              /FTId=PRO_0000031640.
 CHAIN        34    193       Ganglioside GM2 activator isoform short.
                              /FTId=PRO_0000031641.
 CARBOHYD     63     63       N-linked (GlcNAc...) asparagine.
 DISULFID     39    183
 DISULFID     99    106
 DISULFID    112    138
 DISULFID    125    136
 VARIANT      19     19       A -> T (in dbSNP:rs1048719).
                              {ECO:0000269|PubMed:10364519,
                              ECO:0000269|PubMed:1427911,
                              ECO:0000269|PubMed:14702039,
                              ECO:0000269|PubMed:1915857,
                              ECO:0000269|PubMed:2753159}.
                              /FTId=VAR_013830.
 VARIANT      59     59       I -> V (in dbSNP:rs153477).
                              {ECO:0000269|PubMed:10364519,
                              ECO:0000269|PubMed:1427911,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:1915857,
                              ECO:0000269|PubMed:2059210,
                              ECO:0000269|PubMed:2753159}.
                              /FTId=VAR_036892.
 VARIANT      69     69       M -> V (in dbSNP:rs153478).
                              {ECO:0000269|PubMed:10364519,
                              ECO:0000269|PubMed:1427911,
                              ECO:0000269|PubMed:14702039,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:1915857,
                              ECO:0000269|PubMed:2059210,
                              ECO:0000269|PubMed:2753159}.
                              /FTId=VAR_036893.
 VARIANT      88     88       Missing (in GM2GAB).
                              {ECO:0000269|PubMed:8900233}.
                              /FTId=VAR_011697.
 VARIANT     138    138       C -> R (in GM2GAB; dbSNP:rs137852797).
                              {ECO:0000269|PubMed:1915858}.
                              /FTId=VAR_006947.
 VARIANT     169    169       R -> P (in GM2GAB; dbSNP:rs104893892).
                              {ECO:0000269|PubMed:8244332}.
                              /FTId=VAR_011698.
 CONFLICT     39     39       C -> R (in Ref. 5; BAG35396).
                              {ECO:0000305}.
 STRAND       35     40       {ECO:0000244|PDB:2AG4}.
 TURN         41     43       {ECO:0000244|PDB:2AG4}.
 STRAND       45     74       {ECO:0000244|PDB:2AG4}.
 STRAND       81     90       {ECO:0000244|PDB:2AG4}.
 STRAND       93     96       {ECO:0000244|PDB:2AG4}.
 STRAND      103    105       {ECO:0000244|PDB:2AG4}.
 STRAND      107    109       {ECO:0000244|PDB:1PUB}.
 HELIX       111    118       {ECO:0000244|PDB:2AG4}.
 STRAND      121    123       {ECO:0000244|PDB:1PUB}.
 HELIX       129    132       {ECO:0000244|PDB:2AG4}.
 STRAND      137    140       {ECO:0000244|PDB:2AG9}.
 STRAND      142    154       {ECO:0000244|PDB:2AG4}.
 TURN        161    163       {ECO:0000244|PDB:2AG9}.
 STRAND      164    176       {ECO:0000244|PDB:2AG4}.
 STRAND      179    192       {ECO:0000244|PDB:2AG4}.
 SEQUENCE   193 AA;  20838 MW;  4EB1119945365F7E CRC64;
 MQSLMQAPLL IALGLLLAAP AQAHLKKPSQ LSSFSWDNCD EGKDPAVIRS LTLEPDPIIV
 PGNVTLSVMG STSVPLSSPL KVDLVLEKEV AGLWIKIPCT DYIGSCTFEH FCDVLDMLIP
 TGEPCPEPLR TYGLPCHCPF KEGTYSLPKS EFVVPDLELP SWLTTGNYRI ESVLSSSGKR
 LGCIKIAASL KGI

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