KARG0_SCYPA
ID KARG0_SCYPA Reviewed; 357 AA.
AC H6VGI3;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Arginine kinase Scy p 2.0101 {ECO:0000305};
DE Short=AK {ECO:0000303|PubMed:23911402, ECO:0000303|PubMed:25728640, ECO:0000303|PubMed:30236721};
DE EC=2.7.3.3 {ECO:0000250|UniProtKB:C9EIP1};
DE AltName: Allergen=Scy p 2.0101 {ECO:0000305};
OS Scylla paramamosain (Mud crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Portunidae; Scylla.
OX NCBI_TaxID=85552;
RN [1] {ECO:0000312|EMBL:AFA45340.1}
RP NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, TISSUE SPECIFICITY,
RP GLYCOSYLATION, ALLERGEN, AND REGION.
RC TISSUE=Muscle {ECO:0000303|PubMed:23911402};
RX PubMed=23911402; DOI=10.1016/j.molimm.2013.04.016;
RA Mao H.Y., Cao M.J., Maleki S.J., Cai Q.F., Su W.J., Yang Y., Liu G.M.;
RT "Structural characterization and IgE epitope analysis of arginine kinase
RT from Scylla paramamosain.";
RL Mol. Immunol. 56:463-470(2013).
RN [2]
RP 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, ALLERGEN, AND REGION.
RX PubMed=25728640; DOI=10.1016/j.molimm.2015.02.010;
RA Yang Y., Cao M.J., Alcocer M., Liu Q.M., Fei D.X., Mao H.Y., Liu G.M.;
RT "Mapping and characterization of antigenic epitopes of arginine kinase of
RT Scylla paramamosain.";
RL Mol. Immunol. 65:310-320(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=30236721; DOI=10.1016/j.foodchem.2018.08.003;
RA Yang Y., Liu G.Y., Yang H., Hu M.J., Cao M.J., Su W.J., Jin T., Liu G.M.;
RT "Crystal structure determination of Scylla paramamosain arginine kinase, an
RT allergen that may cause cross-reactivity among invertebrates.";
RL Food Chem. 271:597-605(2019).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000250|UniProtKB:C9EIP1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
CC Evidence={ECO:0000250|UniProtKB:C9EIP1};
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:23911402, ECO:0000269|PubMed:25728640,
CC ECO:0000269|PubMed:30236721}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23911402}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of crab-
CC allergic patients (PubMed:23911402, PubMed:25728640, PubMed:30236721).
CC Binds to IgE in 89% of the 9 patients tested allergic to crab
CC (PubMed:23911402). Causes degranulation of rat basophilic leukemia
CC (RBL) cells and release of beta-hexosaminidase from them. Allergenicity
CC is affected to different degrees by denaturants. SDS reduces
CC allergenicity at low concentrations (0.3 mM), and allergenicity is
CC almost completely abolished with 15 mM SDS. Urea concentrations of 2.0-
CC 3.0 M enhance allergenicity, whereas at concentrations higher than 4.0
CC M, the allergenicity is reduced. Slight change in allergenicity after
CC guanidinium chloride (GdnHCl) treatment, but when concentration of
CC GdnHCl reaches 1.5 M, the allergenicity is unchanged. DTT (disulfide
CC bond-reducing agent), at a concentration of 10 mM, causes a slight
CC reduction in allergenicity and it is decreased in a dose-dependent
CC manner at concentrations of 10-250 mM, but remains steady at higher
CC concentrations. 2.5 M beta-mercaptoethanol (another disulfide bond-
CC reducing agent) treatment reduces allergenicity (PubMed:25728640).
CC {ECO:0000269|PubMed:23911402, ECO:0000269|PubMed:25728640,
CC ECO:0000269|PubMed:30236721}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00843, ECO:0000255|RuleBase:RU000505,
CC ECO:0000305}.
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DR EMBL; JN828652; AFA45340.1; -; mRNA.
DR PDB; 5ZHQ; X-ray; 3.00 A; A/B=1-357.
DR PDBsum; 5ZHQ; -.
DR AlphaFoldDB; H6VGI3; -.
DR SMR; H6VGI3; -.
DR Allergome; 12149; Scy p 2.0101.
DR Allergome; 9574; Scy p 2.
DR BRENDA; 2.7.3.3; 14671.
DR GO; GO:0004054; F:arginine kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; ATP-binding; Disulfide bond; Glycoprotein;
KW IgE-binding protein; Kinase; Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT CHAIN 2..357
FT /note="Arginine kinase Scy p 2.0101"
FT /id="PRO_0000447433"
FT DOMAIN 9..91
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 119..356
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REGION 113..127
FT /note="IgE-binding and beta-hexosaminidase release from rat
FT basophilic leukemia (RBL) cells"
FT /evidence="ECO:0000269|PubMed:25728640"
FT REGION 127..155
FT /note="IgE-binding and beta-hexosaminidase release from rat
FT basophilic leukemia (RBL) cells"
FT /evidence="ECO:0000269|PubMed:23911402,
FT ECO:0000269|PubMed:25728640"
FT REGION 204..218
FT /note="IgE-binding and beta-hexosaminidase release from rat
FT basophilic leukemia (RBL) cells"
FT /evidence="ECO:0000269|PubMed:25728640"
FT REGION 211..225
FT /note="IgE-binding, but no beta-hexosaminidase release from
FT rat basophilic leukemia (RBL) cells"
FT /evidence="ECO:0000269|PubMed:23911402,
FT ECO:0000269|PubMed:25728640"
FT REGION 316..330
FT /note="IgE-binding, but no beta-hexosaminidase release from
FT rat basophilic leukemia (RBL) cells"
FT /evidence="ECO:0000269|PubMed:25728640"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT DISULFID 201..271
FT /evidence="ECO:0000305|PubMed:25728640"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT TURN 198..207
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 218..237
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5ZHQ"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:5ZHQ"
SQ SEQUENCE 357 AA; 40299 MW; 9351554A4ABEF0FA CRC64;
MADAAVIEKL EEGFKKLEAA TDCKSLLKKY LTKSVFDQLK GKKTSLGATL LDVIQSGVEN
LDSGVGVYAP DAEAYTLFAP LFDPIIEDYH KGFKQTDKHP NKDFGDVNQF VNVDPDGKFV
ISTRVRCGRS MEGYPFNPCL TEAQYKEMES KVSSTLSNLE GELKGTYYPL TGMTKDVQQK
LIDDHFLFKE GDRFLQAANA CRYWPTGRGI YHNDNKTFLV WCNEEDHLRI ISMQMGGDLG
QVYRRLVSAV NEIEKRVPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AGKYSLQVRG TRGEHTEAEG GVYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEMQ
