ACBG2_HUMAN
ID ACBG2_HUMAN Reviewed; 666 AA.
AC Q5FVE4; B3KSF2; Q6UWJ3; Q7Z5A0; Q8WW03; Q96M36; Q9BYZ3; Q9H0C4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG2 {ECO:0000305};
DE EC=6.2.1.3 {ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 2;
DE AltName: Full=Arachidonate--CoA ligase ACSBG2 {ECO:0000305};
DE EC=6.2.1.15 {ECO:0000269|PubMed:16762313};
DE AltName: Full=Bubblegum-related protein {ECO:0000303|PubMed:16762313};
DE AltName: Full=PRTD-NY3;
GN Name=ACSBG2 {ECO:0000312|HGNC:HGNC:24174};
GN Synonyms=BGR {ECO:0000303|PubMed:16762313}; ORFNames=UNQ2443/PRO5005;
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] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, VARIANT ALA-143, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=15685348; DOI=10.1111/j.1745-7262.2005.00014.x;
RA Zheng Y., Zhou Z.-M., Min X., Li J.-M., Sha J.-H.;
RT "Identification and characterization of the BGR-like gene with a potential
RT role in human testicular development/spermatogenesis.";
RL Asian J. Androl. 7:21-32(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, VARIANT ALA-143, CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=16762313; DOI=10.1016/j.abb.2006.04.013;
RA Fraisl P., Tanaka H., Forss-Petter S., Lassmann H., Nishimune Y.,
RA Berger J.;
RT "A novel mammalian bubblegum-related acyl-CoA synthetase restricted to
RT testes and possibly involved in spermatogenesis.";
RL Arch. Biochem. Biophys. 451:23-33(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-143.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-143.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Testis;
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].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-143;
RP ASP-584; ASP-586; LYS-624 AND GLN-626.
RC TISSUE=Testis;
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 [8]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS
RP OF HIS-511, AND FUNCTION.
RX PubMed=16371355; DOI=10.1074/jbc.m511558200;
RA Pei Z., Jia Z., Watkins P.A.;
RT "The second member of the human and murine 'bubblegum' family is a
RT testis- and brainstem-specific acyl-CoA synthetase.";
RL J. Biol. Chem. 281:6632-6641(2006).
CC -!- FUNCTION: Catalyzes the conversion of fatty acids such as long chain
CC and very long-chain fatty acids to their active form acyl-CoAs for both
CC synthesis of cellular lipids, and degradation via beta-oxidation. Can
CC activate diverse saturated, monosaturated and polyunsaturated fatty
CC acids (PubMed:16371355, PubMed:16762313). Has increased ability to
CC activate oleic and linoleic acid (PubMed:16371355). May play a role in
CC spermatogenesis (PubMed:15685348). {ECO:0000269|PubMed:15685348,
CC ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16762313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:16762313};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5FVE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5FVE4-2; Sequence=VSP_030719;
CC Name=3;
CC IsoId=Q5FVE4-3; Sequence=VSP_030718;
CC Name=4;
CC IsoId=Q5FVE4-4; Sequence=VSP_030717;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15685348,
CC ECO:0000269|PubMed:16371355, ECO:0000269|PubMed:16762313}.
CC -!- DEVELOPMENTAL STAGE: Weakly or not expressed in fetal testis. Highly
CC expressed in adult testis and moderately in elderly testis.
CC {ECO:0000269|PubMed:15685348}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE12157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY009107; AAG49398.1; -; mRNA.
DR EMBL; AJ577571; CAE12156.1; -; mRNA.
DR EMBL; AJ577571; CAE12157.1; ALT_INIT; mRNA.
DR EMBL; AL136854; CAB66788.1; -; mRNA.
DR EMBL; AY358766; AAQ89126.1; -; mRNA.
DR EMBL; AK057412; BAB71476.1; -; mRNA.
DR EMBL; AK093433; BAG52714.1; -; mRNA.
DR EMBL; CH471139; EAW69111.1; -; Genomic_DNA.
DR EMBL; BC022027; AAH22027.1; -; mRNA.
DR EMBL; BC090046; AAH90046.1; -; mRNA.
DR CCDS; CCDS12159.1; -. [Q5FVE4-1]
DR CCDS; CCDS74269.1; -. [Q5FVE4-3]
DR CCDS; CCDS82282.1; -. [Q5FVE4-2]
DR RefSeq; NP_001276106.1; NM_001289177.1. [Q5FVE4-1]
DR RefSeq; NP_001276107.1; NM_001289178.1. [Q5FVE4-1]
DR RefSeq; NP_001276108.1; NM_001289179.1.
DR RefSeq; NP_001276109.1; NM_001289180.1. [Q5FVE4-3]
DR RefSeq; NP_001308313.1; NM_001321384.1. [Q5FVE4-2]
DR RefSeq; NP_112186.3; NM_030924.4. [Q5FVE4-1]
DR RefSeq; XP_016882821.1; XM_017027332.1. [Q5FVE4-1]
DR AlphaFoldDB; Q5FVE4; -.
DR SMR; Q5FVE4; -.
DR BioGRID; 123551; 9.
DR IntAct; Q5FVE4; 3.
DR STRING; 9606.ENSP00000465589; -.
DR SwissLipids; SLP:000001212; -.
DR iPTMnet; Q5FVE4; -.
DR PhosphoSitePlus; Q5FVE4; -.
DR BioMuta; ACSBG2; -.
DR DMDM; 296434386; -.
DR MassIVE; Q5FVE4; -.
DR PaxDb; Q5FVE4; -.
DR PeptideAtlas; Q5FVE4; -.
DR PRIDE; Q5FVE4; -.
DR ProteomicsDB; 62803; -. [Q5FVE4-1]
DR ProteomicsDB; 62804; -. [Q5FVE4-2]
DR ProteomicsDB; 62805; -. [Q5FVE4-3]
DR ProteomicsDB; 62806; -. [Q5FVE4-4]
DR Antibodypedia; 24085; 143 antibodies from 21 providers.
DR DNASU; 81616; -.
DR Ensembl; ENST00000586696.5; ENSP00000465589.1; ENSG00000130377.14. [Q5FVE4-1]
DR Ensembl; ENST00000588304.5; ENSP00000464938.1; ENSG00000130377.14. [Q5FVE4-2]
DR Ensembl; ENST00000588485.6; ENSP00000466336.2; ENSG00000130377.14. [Q5FVE4-1]
DR Ensembl; ENST00000591403.5; ENSP00000467755.1; ENSG00000130377.14. [Q5FVE4-1]
DR GeneID; 81616; -.
DR KEGG; hsa:81616; -.
DR MANE-Select; ENST00000588485.6; ENSP00000466336.2; NM_030924.5; NP_112186.3.
DR UCSC; uc002mee.3; human. [Q5FVE4-1]
DR CTD; 81616; -.
DR DisGeNET; 81616; -.
DR GeneCards; ACSBG2; -.
DR HGNC; HGNC:24174; ACSBG2.
DR HPA; ENSG00000130377; Tissue enriched (testis).
DR MIM; 614363; gene.
DR neXtProt; NX_Q5FVE4; -.
DR OpenTargets; ENSG00000130377; -.
DR PharmGKB; PA142672649; -.
DR VEuPathDB; HostDB:ENSG00000130377; -.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000155332; -.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; Q5FVE4; -.
DR OMA; AINECCC; -.
DR PhylomeDB; Q5FVE4; -.
DR BioCyc; MetaCyc:HS05377-MON; -.
DR BRENDA; 6.2.1.3; 2681.
DR PathwayCommons; Q5FVE4; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q5FVE4; -.
DR BioGRID-ORCS; 81616; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; ACSBG2; human.
DR GeneWiki; ACSBG2; -.
DR GenomeRNAi; 81616; -.
DR Pharos; Q5FVE4; Tbio.
DR PRO; PR:Q5FVE4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q5FVE4; protein.
DR Bgee; ENSG00000130377; Expressed in sperm and 107 other tissues.
DR ExpressionAtlas; Q5FVE4; baseline and differential.
DR Genevisible; Q5FVE4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:MGI.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; TAS:Reactome.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:MGI.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane;
KW Nucleotide-binding; Reference proteome; Spermatogenesis.
FT CHAIN 1..666
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG2"
FT /id="PRO_0000315812"
FT BINDING 230..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 418..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..200
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030717"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15685348"
FT /id="VSP_030718"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_030719"
FT VARIANT 143
FT /note="V -> A (in dbSNP:rs4807840)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15685348, ECO:0000269|PubMed:16762313"
FT /id="VAR_038317"
FT VARIANT 152
FT /note="K -> R (in dbSNP:rs33937754)"
FT /id="VAR_038318"
FT VARIANT 584
FT /note="G -> D (in dbSNP:rs17851959)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038319"
FT VARIANT 586
FT /note="G -> D (in dbSNP:rs17851960)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038320"
FT VARIANT 601
FT /note="P -> R (in dbSNP:rs35609668)"
FT /id="VAR_038321"
FT VARIANT 624
FT /note="R -> K (in dbSNP:rs17856650)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038322"
FT VARIANT 626
FT /note="E -> Q (in dbSNP:rs17856651)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038323"
FT VARIANT 650
FT /note="R -> S (in dbSNP:rs35605352)"
FT /id="VAR_038324"
FT MUTAGEN 511
FT /note="H->R: Results in a shift of the pH optimum to a more
FT acidic pH without affecting substrate specificity."
FT /evidence="ECO:0000269|PubMed:16371355"
FT CONFLICT 71
FT /note="A -> P (in Ref. 4; AAQ89126)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="K -> E (in Ref. 1; AAG49398)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="I -> M (in Ref. 2; CAE12156/CAE12157 and 3;
FT CAB66788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74354 MW; 4EE300654EF17150 CRC64;
MTGTPKTQEG AKDLEVDMNK TEVTPRLWTT CRDGEVLLRL SKHGPGHETP MTIPEFFRES
VNRFGTYPAL ASKNGKKWEI LNFNQYYEAC RKAAKSLIKL GLERFHGVGI LGFNSAEWFI
TAVGAILAGG LCVGIYATNS AEVCQYVITH AKVNILLVEN DQQLQKILSI PQSSLEPLKA
IIQYRLPMKK NNNLYSWDDF MELGRSIPDT QLEQVIESQK ANQCAVLIYT SGTTGIPKGV
MLSHDNITWI AGAVTKDFKL TDKHETVVSY LPLSHIAAQM MDIWVPIKIG ALTYFAQADA
LKGTLVSTLK EVKPTVFIGV PQIWEKIHEM VKKNSAKSMG LKKKAFVWAR NIGFKVNSKK
MLGKYNTPVS YRMAKTLVFS KVKTSLGLDH CHSFISGTAP LNQETAEFFL SLDIPIGELY
GLSESSGPHT ISNQNNYRLL SCGKILTGCK NMLFQQNKDG IGEICLWGRH IFMGYLESET
ETTEAIDDEG WLHSGDLGQL DGLGFLYVTG HIKEILITAG GENVPPIPVE TLVKKKIPII
SNAMLVGDKL KFLSMLLTLK CEMNQMSGEP LDKLNFEAIN FCRGLGSQAS TVTEIVKQQD
PLVYKAIQQG INAVNQEAMN NAQRIEKWVI LEKDFSIYGG ELGPMMKLKR HFVAQKYKKQ
IDHMYH
