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 02-SEP-2026, entry version 223. 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 FUNCTION. 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 FUNCTION, AND ACTIVITY REGULATION. RX PubMed=30988135; DOI=10.1194/jlr.m092551; RA Anheuser S., Breiden B., Sandhoff K.; RT "Membrane lipids and their degradation compounds control GM2 catabolism at RT intralysosomal luminal vesicles."; RL J. Lipid Res. 60:1099-1111(2019). RN [15] 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 [16] 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 [17] 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 [18] RP VARIANT GM2GAB LYS-88 DEL, FUNCTION, AND SUBCELLULAR LOCATION. 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: Lipid-binding and transfer protein essential for lysosomal CC degradation of ganglioside GM2. Extracts single GM2 molecules from CC intralysosomal luminal vesicle (ILV) membranes and presents them in CC soluble form to beta-hexosaminidase A (HEXA) for cleavage of N-acetyl- CC D-galactosamine and conversion to GM3 (PubMed:30988135, CC PubMed:8900233). Forms a stoichiometric GM2-GM2A complex that serves as CC the substrate for HEXA (PubMed:30988135, PubMed:8900233). Also CC stimulates the breakdown of glycolipid GA2 by HEXA (By similarity). CC Possesses dual function: membrane lipid mobilization/solubilization and CC lipid substrate presentation to hydrolases (PubMed:30988135). The large CC binding pocket can accommodate several single-chain phospholipids and CC fatty acids (By similarity). Exhibits some calcium-independent CC phospholipase activity (By similarity). Participates in cholesterol CC transfer (PubMed:17552909). {ECO:0000250|UniProtKB:Q60648, CC ECO:0000269|PubMed:17552909, ECO:0000269|PubMed:30988135, CC ECO:0000269|PubMed:8900233}. CC -!- ACTIVITY REGULATION: Activity is inhibited by cholesterol, CC sphingomyelin, sphingosine, and sphinganine. Activity is stimulated by CC ceramide, diacylglycerol, fatty acids, lysophosphatidylcholine, and CC anionic lipids such as BMP (bis(monoacylglycero)phosphate). CC {ECO:0000269|PubMed:30988135}. CC -!- INTERACTION: CC P17900; P62736: ACTA2; NbExp=2; IntAct=EBI-3046641, EBI-698810; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:8900233}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_000405.5. 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 AlphaFoldDB; P17900; -. DR SMR; P17900; -. DR BioGRID; 109022; 110. DR FunCoup; P17900; 595. DR IntAct; P17900; 68. 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 GlyCosmos; P17900; 1 site, No reported glycans. DR GlyGen; P17900; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P17900; -. DR PhosphoSitePlus; P17900; -. DR BioMuta; GM2A; -. DR DMDM; 160331912; -. DR jPOST; P17900; -. DR MassIVE; P17900; -. DR PaxDb; 9606-ENSP00000349687; -. DR PeptideAtlas; P17900; -. DR PRIDE; P17900; -. DR ProteomicsDB; 53524; -. DR Pumba; P17900; -. DR Antibodypedia; 2212; 474 antibodies from 33 providers. DR DNASU; 2760; -. DR Ensembl; ENST00000357164.4; ENSP00000349687.3; ENSG00000196743.10. 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 AGR; HGNC:4367; -. DR ClinPGx; PA28752; -. DR CTD; 2760; -. DR DisGeNET; 2760; -. DR GeneCards; GM2A; -. DR GeneReviews; GM2A; -. DR HGNC; HGNC:4367; GM2A. DR HPA; ENSG00000196743; Low tissue specificity. DR MalaCards; GM2A; -. DR MIM; 272750; phenotype. DR MIM; 613109; gene. DR OpenTargets; ENSG00000196743; -. DR Orphanet; 309246; GM2 gangliosidosis, AB variant. DR VEuPathDB; HostDB:ENSG00000196743; -. DR eggNOG; ENOG502S05S; Eukaryota. DR GeneTree; ENSGT00390000003288; -. DR HOGENOM; CLU_108261_0_0_1; -. DR InParanoid; P17900; -. DR OMA; WENCGPP; -. DR OrthoDB; 6409159at2759; -. DR PAN-GO; P17900; 4 GO annotations based on evolutionary models. DR PhylomeDB; P17900; -. DR PathwayCommons; P17900; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9840310; Glycosphingolipid catabolism. DR SignaLink; P17900; -. DR Agora; ENSG00000196743; -. DR BioGRID-ORCS; 2760; 16 hits in 1159 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 205 other cell types or tissues. DR ExpressionAtlas; P17900; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central. DR GO; GO:0160317; C:endolysosomal intralumenal vesicle membrane; IC:UOS_MCB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0032428; F:beta-N-acetylgalactosaminidase activity; IEA:Ensembl. DR GO; GO:0005319; F:lipid carrier activity; IBA:GO_Central. DR GO; GO:7770043; F:lipid chaperone activity; IDA:UOS_MCB. DR GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl. DR GO; GO:0030290; F:sphingolipid activator protein activity; TAS:Reactome. DR GO; GO:0006689; P:ganglioside catabolic process; IDA:UOS_MCB. DR GO; GO:0046479; P:glycosphingolipid catabolic process; TAS:Reactome. DR GO; GO:0006869; P:lipid transport; IBA:GO_Central. DR CDD; cd00258; GM2-AP; 1. DR FunFam; 2.70.220.10:FF:000001; GM2 ganglioside activator protein; 1. DR Gene3D; 2.70.220.10; Ganglioside GM2 activator; 1. DR InterPro; IPR028996; GM2-AP. DR InterPro; IPR036846; GM2-AP_sf. DR InterPro; IPR003172; ML_dom. DR PANTHER; PTHR17357:SF0; GANGLIOSIDE GM2 ACTIVATOR; 1. DR PANTHER; PTHR17357; GM2 GANGLIOSIDE ACTIVATOR PROTEIN; 1. DR Pfam; PF02221; E1_DerP2_DerF2; 1. DR SMART; SM00737; ML; 1. DR SUPFAM; SSF63707; Ganglioside M2 (gm2) activator; 1. DR PDBsum; 1G13; -. DR PDBsum; 1PU5; -. DR PDBsum; 1PUB; -. DR PDBsum; 1TJJ; -. DR PDBsum; 2AF9; -. DR PDBsum; 2AG2; -. DR PDBsum; 2AG4; -. DR PDBsum; 2AG9; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; KW Gangliosidosis; Glycoprotein; Hydrolase; Lipid metabolism; Lysosome; KW Proteomics identification; Reference proteome; Signal; KW 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 /evidence="ECO:0000250|UniProtKB:Q60648" FT DISULFID 99..106 FT /evidence="ECO:0000250|UniProtKB:Q60648" FT DISULFID 112..138 FT /evidence="ECO:0000250|UniProtKB:Q60648" FT DISULFID 125..136 FT /evidence="ECO:0000250|UniProtKB:Q60648" 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; dbSNP:rs1753894328)" 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 HELIX 97..99 FT /evidence="ECO:0007829|PDB:2AG9" 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 124..126 FT /evidence="ECO:0007829|PDB:2AG4" 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 //