SAP3_HUMAN
ID SAP3_HUMAN Reviewed; 193 AA.
AC P17900; B2R699; D3DQH6; Q14426; Q14428; Q6LBL5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Ganglioside GM2 activator {ECO:0000305};
DE AltName: Full=Cerebroside sulfate activator protein;
DE AltName: Full=GM2-AP;
DE AltName: Full=Sphingolipid activator protein 3;
DE Short=SAP-3;
DE Contains:
DE RecName: Full=Ganglioside GM2 activator isoform short;
DE Flags: Precursor;
GN Name=GM2A {ECO:0000312|HGNC:HGNC:4367};
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], AND VARIANTS VAL-59 AND VAL-69.
RX PubMed=2059210; DOI=10.1016/0006-291x(91)90671-s;
RA Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.;
RT "Isolation and expression of a full-length cDNA encoding the human G-M2
RT activator protein.";
RL Biochem. Biophys. Res. Commun. 177:1217-1223(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
RX PubMed=1915857; DOI=10.1016/0014-5793(91)81084-l;
RA Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K.,
RA Sandhoff K.;
RT "Characterization of full-length cDNAs and the gene coding for the human
RT GM2 activator protein.";
RL FEBS Lett. 289:260-264(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=1554364; DOI=10.1042/bj2820807;
RA Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.;
RT "Evidence for two cDNAs encoding human GM2-activator protein.";
RL Biochem. J. 282:807-813(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
RX PubMed=1427911; DOI=10.1016/s0888-7543(05)80190-9;
RA Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.;
RT "Identification of a processed pseudogene related to the functional gene
RT encoding the GM2 activator protein: localization of the pseudogene to human
RT chromosome 3 and the functional gene to human chromosome 5.";
RL Genomics 14:796-798(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-19 AND VAL-69.
RC TISSUE=Substantia nigra;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
RX PubMed=10364519; DOI=10.1086/302463;
RA Chen B., Rigat B., Curry C., Mahuran D.J.;
RT "Structure of the GM2A gene: identification of an exon 2 nonsense mutation
RT and a naturally occurring transcript with an in-frame deletion of exon 2.";
RL Am. J. Hum. Genet. 65:77-87(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-59 AND VAL-69.
RC TISSUE=Uterus;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-193, AND VARIANTS THR-19; VAL-59 AND
RP VAL-69.
RX PubMed=2753159; DOI=10.1016/0014-5793(89)81454-1;
RA Schroeder M., Klima H., Nakano T., Kwon H., Quintern L.E., Gaertner S.,
RA Suzuki K., Sandhoff K.;
RT "Isolation of a cDNA encoding the human GM2 activator protein.";
RL FEBS Lett. 251:197-200(1989).
RN [11]
RP PROTEIN SEQUENCE OF 32-193.
RC TISSUE=Kidney;
RX PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x;
RA Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.;
RT "The complete amino-acid sequences of human ganglioside GM2 activator
RT protein and cerebroside sulfate activator protein.";
RL Eur. J. Biochem. 192:709-714(1990).
RN [12]
RP CATALYTIC ACTIVITY.
RX PubMed=17552909; DOI=10.1515/bc.2007.063;
RA Babalola J.O., Wendeler M., Breiden B., Arenz C., Schwarzmann G.,
RA Locatelli-Hoops S., Sandhoff K.;
RT "Development of an assay for the intermembrane transfer of cholesterol by
RT Niemann-Pick C2 protein.";
RL Biol. Chem. 388:617-626(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11090283; DOI=10.1006/jmbi.2000.4225;
RA Wright C.S., Li S.-C., Rastinejad F.;
RT "Crystal structure of human GM2-activator protein with a novel beta-cup
RT topology.";
RL J. Mol. Biol. 304:411-422(2000).
RN [15]
RP VARIANT GM2GAB ARG-138.
RX PubMed=1915858; DOI=10.1016/0014-5793(91)81211-p;
RA Schroeder M., Schnabel D., Suzuki K., Sandhoff K.;
RT "A mutation in the gene of a glycolipid-binding protein (GM2 activator)
RT that causes GM2-gangliosidosis variant AB.";
RL FEBS Lett. 290:1-3(1991).
RN [16]
RP VARIANT GM2GAB PRO-169.
RX PubMed=8244332; DOI=10.1007/bf00216446;
RA Schroder M., Schnabel D., Hurwitz R., Young E., Suzuki K., Sandhoff K.;
RT "Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and
RT expression in BHK cells.";
RL Hum. Genet. 92:437-440(1993).
RN [17]
RP VARIANT GM2GAB LYS-88 DEL.
RX PubMed=8900233;
RA Schepers U., Glombitza G., Lemm T., Hoffmann A., Chabas A., Ozand P.,
RA Sandhoff K.;
RT "Molecular analysis of a GM2-activator deficiency in two patients with GM2-
RT gangliosidosis AB variant.";
RL Am. J. Hum. Genet. 59:1048-1056(1996).
CC -!- FUNCTION: The large binding pocket can accommodate several single chain
CC phospholipids and fatty acids, GM2A also exhibits some calcium-
CC independent phospholipase activity (By similarity). Binds gangliosides
CC and stimulates ganglioside GM2 degradation. It stimulates only the
CC breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase
CC A. It extracts single GM2 molecules from membranes and presents them in
CC soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-
CC galactosamine and conversion to GM3 (By similarity). Has cholesterol
CC transfer activity (PubMed:17552909). {ECO:0000250|UniProtKB:Q60648,
CC ECO:0000269|PubMed:17552909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:17552909};
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- PTM: The serines in positions 32 and 33 are absent in 80% of the
CC sequenced protein.
CC -!- DISEASE: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal
CC recessive lysosomal storage disease marked by the accumulation of GM2
CC gangliosides in the neuronal cells. It is characterized by GM2
CC gangliosides accumulation in the presence of both normal hexosaminidase
CC A and B. {ECO:0000269|PubMed:1915858, ECO:0000269|PubMed:8244332,
CC ECO:0000269|PubMed:8900233}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43408.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA43994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M76477; AAA35907.1; -; mRNA.
DR EMBL; X62078; CAA43993.1; -; mRNA.
DR EMBL; X62078; CAA43994.1; ALT_INIT; mRNA.
DR EMBL; X61095; CAA43408.1; ALT_INIT; mRNA.
DR EMBL; L01439; AAA52767.1; -; mRNA.
DR EMBL; AF124719; AAD25741.1; -; Genomic_DNA.
DR EMBL; AF124717; AAD25741.1; JOINED; Genomic_DNA.
DR EMBL; AF124718; AAD25741.1; JOINED; Genomic_DNA.
DR EMBL; AK312494; BAG35396.1; -; mRNA.
DR EMBL; AC008385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61680.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61681.1; -; Genomic_DNA.
DR EMBL; BC009273; AAH09273.1; -; mRNA.
DR EMBL; X16087; CAA34215.1; -; mRNA.
DR CCDS; CCDS4313.1; -.
DR PIR; I54178; I54178.
DR PIR; S13195; S13195.
DR PIR; S22411; S22411.
DR RefSeq; NP_000396.2; NM_000405.4.
DR PDB; 1G13; X-ray; 2.00 A; A/B/C=32-193.
DR PDB; 1PU5; X-ray; 1.90 A; A/B/C=32-193.
DR PDB; 1PUB; X-ray; 2.51 A; A=32-193.
DR PDB; 1TJJ; X-ray; 2.00 A; A/B/C=32-193.
DR PDB; 2AF9; X-ray; 2.00 A; A=32-193.
DR PDB; 2AG2; X-ray; 2.00 A; A/B/C=32-193.
DR PDB; 2AG4; X-ray; 1.80 A; A/B=32-193.
DR PDB; 2AG9; X-ray; 2.20 A; A/B=32-193.
DR PDBsum; 1G13; -.
DR PDBsum; 1PU5; -.
DR PDBsum; 1PUB; -.
DR PDBsum; 1TJJ; -.
DR PDBsum; 2AF9; -.
DR PDBsum; 2AG2; -.
DR PDBsum; 2AG4; -.
DR PDBsum; 2AG9; -.
DR AlphaFoldDB; P17900; -.
DR SMR; P17900; -.
DR BioGRID; 109022; 101.
DR IntAct; P17900; 22.
DR MINT; P17900; -.
DR STRING; 9606.ENSP00000349687; -.
DR DrugBank; DB04660; Choline alfoscerate.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB03633; Lpc-Ether.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB02261; Platelet Activating Factor.
DR SwissLipids; SLP:000000476; -.
DR GlyGen; P17900; 1 site.
DR iPTMnet; P17900; -.
DR PhosphoSitePlus; P17900; -.
DR BioMuta; GM2A; -.
DR DMDM; 160331912; -.
DR EPD; P17900; -.
DR jPOST; P17900; -.
DR MassIVE; P17900; -.
DR MaxQB; P17900; -.
DR PaxDb; P17900; -.
DR PeptideAtlas; P17900; -.
DR PRIDE; P17900; -.
DR ProteomicsDB; 53524; -.
DR Antibodypedia; 2212; 490 antibodies from 33 providers.
DR DNASU; 2760; -.
DR Ensembl; ENST00000357164.4; ENSP00000349687.3; ENSG00000196743.9.
DR GeneID; 2760; -.
DR KEGG; hsa:2760; -.
DR MANE-Select; ENST00000357164.4; ENSP00000349687.3; NM_000405.5; NP_000396.2.
DR UCSC; uc003ltr.5; human.
DR CTD; 2760; -.
DR DisGeNET; 2760; -.
DR GeneCards; GM2A; -.
DR HGNC; HGNC:4367; GM2A.
DR HPA; ENSG00000196743; Low tissue specificity.
DR MalaCards; GM2A; -.
DR MIM; 272750; phenotype.
DR MIM; 613109; gene.
DR neXtProt; NX_P17900; -.
DR OpenTargets; ENSG00000196743; -.
DR Orphanet; 309246; GM2 gangliosidosis, AB variant.
DR PharmGKB; PA28752; -.
DR VEuPathDB; HostDB:ENSG00000196743; -.
DR eggNOG; ENOG502S05S; Eukaryota.
DR GeneTree; ENSGT00390000003288; -.
DR HOGENOM; CLU_108261_0_0_1; -.
DR InParanoid; P17900; -.
DR OMA; GNYRIQS; -.
DR OrthoDB; 1548356at2759; -.
DR PhylomeDB; P17900; -.
DR TreeFam; TF353575; -.
DR PathwayCommons; P17900; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P17900; -.
DR BioGRID-ORCS; 2760; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; GM2A; human.
DR EvolutionaryTrace; P17900; -.
DR GeneWiki; GM2A; -.
DR GenomeRNAi; 2760; -.
DR Pharos; P17900; Tbio.
DR PRO; PR:P17900; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P17900; protein.
DR Bgee; ENSG00000196743; Expressed in mammalian vulva and 203 other tissues.
DR ExpressionAtlas; P17900; baseline and differential.
DR Genevisible; P17900; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:Ensembl.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0030290; F:sphingolipid activator protein activity; TAS:Reactome.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0051651; P:maintenance of location in cell; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
DR Gene3D; 2.70.220.10; -; 1.
DR InterPro; IPR028996; GM2-AP.
DR InterPro; IPR036846; GM2-AP_sf.
DR InterPro; IPR003172; ML_dom.
DR PANTHER; PTHR17357; PTHR17357; 1.
DR Pfam; PF02221; E1_DerP2_DerF2; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF63707; SSF63707; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Gangliosidosis; Glycoprotein; Hydrolase; Lipid metabolism; Lysosome;
KW Reference proteome; Signal; Sphingolipid metabolism.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..31
FT /evidence="ECO:0000269|PubMed:2209618"
FT /id="PRO_0000031639"
FT CHAIN 32..193
FT /note="Ganglioside GM2 activator"
FT /id="PRO_0000031640"
FT CHAIN 34..193
FT /note="Ganglioside GM2 activator isoform short"
FT /id="PRO_0000031641"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 39..183
FT DISULFID 99..106
FT DISULFID 112..138
FT DISULFID 125..136
FT VARIANT 19
FT /note="A -> T (in dbSNP:rs1048719)"
FT /evidence="ECO:0000269|PubMed:10364519,
FT ECO:0000269|PubMed:1427911, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:1915857, ECO:0000269|PubMed:2753159"
FT /id="VAR_013830"
FT VARIANT 59
FT /note="I -> V (in dbSNP:rs153477)"
FT /evidence="ECO:0000269|PubMed:10364519,
FT ECO:0000269|PubMed:1427911, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1915857, ECO:0000269|PubMed:2059210,
FT ECO:0000269|PubMed:2753159"
FT /id="VAR_036892"
FT VARIANT 69
FT /note="M -> V (in dbSNP:rs153478)"
FT /evidence="ECO:0000269|PubMed:10364519,
FT ECO:0000269|PubMed:1427911, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1915857,
FT ECO:0000269|PubMed:2059210, ECO:0000269|PubMed:2753159"
FT /id="VAR_036893"
FT VARIANT 88
FT /note="Missing (in GM2GAB)"
FT /evidence="ECO:0000269|PubMed:8900233"
FT /id="VAR_011697"
FT VARIANT 138
FT /note="C -> R (in GM2GAB; dbSNP:rs137852797)"
FT /evidence="ECO:0000269|PubMed:1915858"
FT /id="VAR_006947"
FT VARIANT 169
FT /note="R -> P (in GM2GAB; dbSNP:rs104893892)"
FT /evidence="ECO:0000269|PubMed:8244332"
FT /id="VAR_011698"
FT CONFLICT 39
FT /note="C -> R (in Ref. 5; BAG35396)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2AG4"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 45..74
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1PUB"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1PUB"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2AG9"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:2AG4"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2AG9"
FT STRAND 164..176
FT /evidence="ECO:0007829|PDB:2AG4"
FT STRAND 179..192
FT /evidence="ECO:0007829|PDB:2AG4"
SQ 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
