PURA2_HUMAN
ID PURA2_HUMAN Reviewed; 456 AA.
AC P30520; B1AQM5; Q96EG7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Adenylosuccinate synthetase isozyme 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AMPSase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AdSS 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, acidic isozyme {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, liver isozyme {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=L-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=IMP--aspartate ligase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
GN Name=ADSS2 {ECO:0000312|HGNC:HGNC:292};
GN Synonyms=ADSS {ECO:0000255|HAMAP-Rule:MF_03127};
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=1592113; DOI=10.1016/0014-5793(92)80465-s;
RA Powell S.M., Zalkin H., Dixon J.E.;
RT "Cloning and characterization of the cDNA encoding human adenylosuccinate
RT synthetase.";
RL FEBS Lett. 303:4-10(1992).
RN [2]
RP SEQUENCE REVISION.
RA Stone R.L.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-456 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "Human adenylosuccinate synthetase isozyme 2 in complex with GDP.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000250|UniProtKB:P46664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03127};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03127};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03127};
CC -!- ACTIVITY REGULATION: Inhibited competitively by AMP and IMP and non-
CC competitively by fructose 1,6-bisphosphate.
CC {ECO:0000250|UniProtKB:P46664}.
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- INTERACTION:
CC P30520; Q8NB12: SMYD1; NbExp=4; IntAct=EBI-1042898, EBI-8463848;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}.
CC Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}. Note=Partially associated
CC with particulate fractions.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03127}.
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DR EMBL; X66503; CAA47123.1; -; Genomic_DNA.
DR EMBL; AL591594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471148; EAW77102.1; -; Genomic_DNA.
DR EMBL; BC012356; AAH12356.1; -; mRNA.
DR CCDS; CCDS1624.1; -.
DR PIR; S21166; S21166.
DR RefSeq; NP_001117.2; NM_001126.3.
DR PDB; 2V40; X-ray; 1.90 A; A=21-456.
DR PDBsum; 2V40; -.
DR AlphaFoldDB; P30520; -.
DR SMR; P30520; -.
DR BioGRID; 106668; 102.
DR IntAct; P30520; 15.
DR MINT; P30520; -.
DR STRING; 9606.ENSP00000355493; -.
DR BindingDB; P30520; -.
DR ChEMBL; CHEMBL4875; -.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB05540; Alanosine.
DR DrugBank; DB00128; Aspartic acid.
DR GlyGen; P30520; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P30520; -.
DR MetOSite; P30520; -.
DR PhosphoSitePlus; P30520; -.
DR SwissPalm; P30520; -.
DR BioMuta; ADSS; -.
DR DMDM; 21264498; -.
DR CPTAC; CPTAC-163; -.
DR CPTAC; CPTAC-164; -.
DR EPD; P30520; -.
DR jPOST; P30520; -.
DR MassIVE; P30520; -.
DR MaxQB; P30520; -.
DR PaxDb; P30520; -.
DR PeptideAtlas; P30520; -.
DR PRIDE; P30520; -.
DR ProteomicsDB; 54711; -.
DR Antibodypedia; 20829; 154 antibodies from 23 providers.
DR DNASU; 159; -.
DR Ensembl; ENST00000366535.4; ENSP00000355493.3; ENSG00000035687.10.
DR GeneID; 159; -.
DR KEGG; hsa:159; -.
DR MANE-Select; ENST00000366535.4; ENSP00000355493.3; NM_001126.5; NP_001117.2.
DR UCSC; uc001iaj.4; human.
DR CTD; 159; -.
DR DisGeNET; 159; -.
DR GeneCards; ADSS2; -.
DR HGNC; HGNC:292; ADSS2.
DR HPA; ENSG00000035687; Low tissue specificity.
DR MIM; 103060; gene.
DR neXtProt; NX_P30520; -.
DR OpenTargets; ENSG00000035687; -.
DR PharmGKB; PA24601; -.
DR VEuPathDB; HostDB:ENSG00000035687; -.
DR eggNOG; KOG1355; Eukaryota.
DR GeneTree; ENSGT00390000015553; -.
DR HOGENOM; CLU_029848_3_0_1; -.
DR InParanoid; P30520; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 1276527at2759; -.
DR PhylomeDB; P30520; -.
DR TreeFam; TF300486; -.
DR PathwayCommons; P30520; -.
DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR SignaLink; P30520; -.
DR SIGNOR; P30520; -.
DR UniPathway; UPA00075; UER00335.
DR BioGRID-ORCS; 159; 334 hits in 1071 CRISPR screens.
DR ChiTaRS; ADSS; human.
DR EvolutionaryTrace; P30520; -.
DR GenomeRNAi; 159; -.
DR Pharos; P30520; Tchem.
DR PRO; PR:P30520; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P30520; protein.
DR Bgee; ENSG00000035687; Expressed in monocyte and 199 other tissues.
DR ExpressionAtlas; P30520; baseline and differential.
DR Genevisible; P30520; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042301; F:phosphate ion binding; NAS:UniProtKB.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI.
DR GO; GO:0006167; P:AMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0002376; P:immune system process; NAS:UniProtKB.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR GO; GO:0060359; P:response to ammonium ion; IEA:Ensembl.
DR GO; GO:0014074; P:response to purine-containing compound; IEA:Ensembl.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_03127; Adenylosucc_synth_vert_acid; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027529; AdSS_2_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..456
FT /note="Adenylosuccinate synthetase isozyme 2"
FT /id="PRO_0000095130"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT ACT_SITE 68
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 39..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 40..43
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 65..68
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 162
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 176
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 255
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 270
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 330..336
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 334
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 362..364
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 444..447
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT VARIANT 179
FT /note="L -> F (in dbSNP:rs12134870)"
FT /id="VAR_051881"
FT CONFLICT 24..25
FT /note="RP -> A (in Ref. 1; CAA47123)"
FT /evidence="ECO:0000305"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 188..205
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2V40"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 290..307
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:2V40"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2V40"
FT HELIX 423..436
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:2V40"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:2V40"
SQ SEQUENCE 456 AA; 50097 MW; 23B7AAC58A238783 CRC64;
MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC
QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL
EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE
ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL
TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV QYKTLPGWNT DISNARAFKE
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF
