ADPRS_MOUSE
ID ADPRS_MOUSE Reviewed; 370 AA.
AC Q8CG72; A3KFY3; Q80UW9; Q8R575; Q921U6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ADP-ribosylhydrolase ARH3;
DE AltName: Full=ADP-ribose glycohydrolase ARH3 {ECO:0000305};
DE AltName: Full=ADP-ribosylhydrolase 3 {ECO:0000303|PubMed:24191052};
DE AltName: Full=O-acetyl-ADP-ribose deacetylase ARH3 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q9NX46};
DE AltName: Full=Poly(ADP-ribose) glycohydrolase ARH3 {ECO:0000305};
DE EC=3.2.1.143 {ECO:0000269|PubMed:24191052};
DE AltName: Full=[Protein ADP-ribosylarginine] hydrolase-like protein 2 {ECO:0000305};
DE AltName: Full=[Protein ADP-ribosylserine] hydrolase;
DE EC=3.2.2.-;
GN Name=Adprs;
GN Synonyms=Adprhl2 {ECO:0000312|MGI:MGI:2140364},
GN Arh3 {ECO:0000303|PubMed:24191052};
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 1).
RC STRAIN=C57BL/6J;
RX PubMed=12070318; DOI=10.1110/ps.0200602;
RA Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P.,
RA Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
RT "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the
RT mouse.";
RL Protein Sci. 11:1657-1670(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Liver, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16278211; DOI=10.1074/jbc.m510290200;
RA Oka S., Kato J., Moss J.;
RT "Identification and characterization of a mammalian 39-kDa poly(ADP-ribose)
RT glycohydrolase.";
RL J. Biol. Chem. 281:705-713(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=24191052; DOI=10.1073/pnas.1312783110;
RA Mashimo M., Kato J., Moss J.;
RT "ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation
RT and cell death during oxidative stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18964-18969(2013).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30830864; DOI=10.1172/jci.insight.124519;
RA Mashimo M., Bu X., Aoyama K., Kato J., Ishiwata-Endo H., Stevens L.A.,
RA Kasamatsu A., Wolfe L.A., Toro C., Adams D., Markello T., Gahl W.A.,
RA Moss J.;
RT "PARP1 inhibition alleviates injury in ARH3-deficient mice and human
RT cells.";
RL JCI Insight 4:0-0(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-369, SUBUNIT, COFACTOR, AND
RP MAGNESIUM-BINDING SITES.
RX PubMed=18323597; DOI=10.1107/s1744309108001413;
RA Mueller-Dieckmann C., Kernstock S., Mueller-Dieckmann J., Weiss M.S.,
RA Koch-Nolte F.;
RT "Structure of mouse ADP-ribosylhydrolase 3 (mARH3).";
RL Acta Crystallogr. F 64:156-162(2008).
CC -!- FUNCTION: ADP-ribosylhydrolase that preferentially hydrolyzes the
CC scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-
CC ribose and acts on different substrates, such as proteins ADP-
CC ribosylated on serine and threonine, free poly(ADP-ribose) and O-
CC acetyl-ADP-D-ribose (By similarity). Specifically acts as a serine
CC mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose
CC attached to serine residues on proteins, thereby playing a key role in
CC DNA damage response (By similarity). Serine ADP-ribosylation of
CC proteins constitutes the primary form of ADP-ribosylation of proteins
CC in response to DNA damage (By similarity). Does not hydrolyze ADP-
CC ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By
CC similarity). Also able to degrade protein free poly(ADP-ribose), which
CC is synthesized in response to DNA damage: free poly(ADP-ribose) acts as
CC a potent cell death signal and its degradation by ADPRHL2 protects
CC cells from poly(ADP-ribose)-dependent cell death, a process named
CC parthanatos (PubMed:24191052, PubMed:30830864). Also hydrolyzes free
CC poly(ADP-ribose) in mitochondria (By similarity). Specifically digests
CC O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed
CC by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-
CC ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-
CC ADP-D-ribose isomers (By similarity). {ECO:0000250|UniProtKB:Q9NX46,
CC ECO:0000269|PubMed:24191052, ECO:0000269|PubMed:30830864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-
CC alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-
CC COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143;
CC Evidence={ECO:0000269|PubMed:24191052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1''-O-acetyl-ADP-alpha-D-ribose + H2O = acetate + ADP-D-ribose
CC + H(+); Xref=Rhea:RHEA:58112, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57967, ChEBI:CHEBI:142511;
CC Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-(ADP-D-ribosyl)-L-seryl-[protein] = ADP-D-ribose + L-
CC seryl-[protein]; Xref=Rhea:RHEA:58256, Rhea:RHEA-COMP:9863,
CC Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:142556;
CC Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC Evidence={ECO:0000250|UniProtKB:Q9NX46};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18323597};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:18323597};
CC -!- ACTIVITY REGULATION: The protein undergoes a dramatic conformational
CC switch from closed to open states upon substrate-binding, which enables
CC specific substrate recognition for the 1''-O-linkage. The glutamate
CC flap (Glu-47) blocks substrate entrance to Mg(2+) in the unliganded
CC closed state. In presence of substrate, Glu-47 is ejected from the
CC active site: this closed-to-open transition significantly widens the
CC substrate-binding channel and precisely positions the scissile 1''-O-
CC linkage for cleavage while securing tightly 2'- and 3'-hydroxyls of
CC ADP-ribose. {ECO:0000250|UniProtKB:Q9NX46}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18323597}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16278211,
CC ECO:0000269|PubMed:24191052}. Cytoplasm {ECO:0000269|PubMed:16278211}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NX46}. Mitochondrion matrix
CC {ECO:0000269|PubMed:24191052}. Note=Recruited to DNA lesion regions
CC following DNA damage; ADP-D-ribose-recognition is required for
CC recruitment to DNA damage sites. {ECO:0000250|UniProtKB:Q9NX46}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CG72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CG72-2; Sequence=VSP_023037;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16278211}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are phenotypically normal and
CC fertile (PubMed:30830864). 1 hour induced brain ischemia results in
CC 100% fatality within 24 hours (PubMed:30830864). 30 minutes of induced
CC brain ischemia results in an increase in infarct size in the cortex,
CC hippocampus, and striatum (PubMed:30830864). Increased number of
CC cortical neurons with nucleus-accumulated poly(ADP-ribose) and higher
CC abundance of poly(ADP-ribose) in general (PubMed:30830864).
CC {ECO:0000269|PubMed:30830864}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; AJ427296; CAD20317.1; -; mRNA.
DR EMBL; AK143583; BAE25451.1; -; mRNA.
DR EMBL; AK147034; BAE27626.1; -; mRNA.
DR EMBL; AK169070; BAE40857.1; -; mRNA.
DR EMBL; AK171780; BAE42660.1; -; mRNA.
DR EMBL; AL606976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010639; AAH10639.1; -; mRNA.
DR EMBL; BC023177; AAH23177.2; -; mRNA.
DR EMBL; BC045203; AAH45203.1; -; mRNA.
DR CCDS; CCDS18650.1; -. [Q8CG72-1]
DR RefSeq; NP_598644.1; NM_133883.2. [Q8CG72-1]
DR PDB; 2QTY; X-ray; 1.80 A; A/B=25-369.
DR PDBsum; 2QTY; -.
DR AlphaFoldDB; Q8CG72; -.
DR SMR; Q8CG72; -.
DR STRING; 10090.ENSMUSP00000099677; -.
DR PhosphoSitePlus; Q8CG72; -.
DR EPD; Q8CG72; -.
DR MaxQB; Q8CG72; -.
DR PaxDb; Q8CG72; -.
DR PeptideAtlas; Q8CG72; -.
DR PRIDE; Q8CG72; -.
DR ProteomicsDB; 283219; -. [Q8CG72-1]
DR ProteomicsDB; 283220; -. [Q8CG72-2]
DR Antibodypedia; 17409; 113 antibodies from 22 providers.
DR DNASU; 100206; -.
DR Ensembl; ENSMUST00000102617; ENSMUSP00000099677; ENSMUSG00000042558. [Q8CG72-1]
DR GeneID; 100206; -.
DR KEGG; mmu:100206; -.
DR UCSC; uc008ute.1; mouse. [Q8CG72-1]
DR CTD; 54936; -.
DR MGI; MGI:2140364; Adprs.
DR VEuPathDB; HostDB:ENSMUSG00000042558; -.
DR eggNOG; ENOG502QUER; Eukaryota.
DR GeneTree; ENSGT00390000015369; -.
DR HOGENOM; CLU_024566_6_0_1; -.
DR InParanoid; Q8CG72; -.
DR OMA; IPPSWEQ; -.
DR OrthoDB; 988788at2759; -.
DR PhylomeDB; Q8CG72; -.
DR TreeFam; TF324754; -.
DR BRENDA; 3.2.1.143; 3474.
DR Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
DR BioGRID-ORCS; 100206; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Adprhl2; mouse.
DR EvolutionaryTrace; Q8CG72; -.
DR PRO; PR:Q8CG72; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CG72; protein.
DR Bgee; ENSMUSG00000042558; Expressed in lip and 242 other tissues.
DR Genevisible; Q8CG72; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0140292; F:ADP-ribosylserine hydrolase activity; IMP:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; ISS:UniProtKB.
DR GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:UniProtKB.
DR GO; GO:0071451; P:cellular response to superoxide; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IDA:UniProtKB.
DR GO; GO:0140290; P:peptidyl-serine ADP-deribosylation; IDA:UniProtKB.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm; DNA damage;
KW DNA repair; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="ADP-ribosylhydrolase ARH3"
FT /id="PRO_0000277614"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 152..158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18323597"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18323597"
FT SITE 47
FT /note="Glutamate flap"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX46"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023037"
FT CONFLICT 77
FT /note="E -> Q (in Ref. 4; AAH23177)"
FT /evidence="ECO:0000305"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:2QTY"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:2QTY"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:2QTY"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:2QTY"
FT HELIX 352..366
FT /evidence="ECO:0007829|PDB:2QTY"
SQ SEQUENCE 370 AA; 39414 MW; 3251113C67432A8D CRC64;
MAVAAAAAAT AMSAAGGGGA SAARSISRFR GCLAGALLGD CVGAVYEAHD TVSLASVLSH
VESLEPDPGT PGSARTETLY YTDDTAMTRA LVQSLLAKEA FDEVDMAHRF AQEYKKDPDR
GYGAGVITVF KKLLNPKCRD VYEPARAQFN GKGSYGNGGA MRVAGISLAY SSVQDVQKFA
RLSAQLTHAS SLGYNGAILQ ALAVHLALQG VSSSEHFLEQ LLGHMEELEG DAQSVLDAKE
LGMEERPYSS RLKKVGELLD QDVVSREEVV SELGNGIAAF ESVPTAIYCF LRCMEPHPEI
PSTFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMEQ VPESWQQSCE GFEETDVLAQ
SLHRVFQESS
