KARG_AMPFA
ID KARG_AMPFA Reviewed; 348 AA.
AC G1ESZ9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Arginine kinase Oct f 2 {ECO:0000303|PubMed:22303807};
DE Short=AK {ECO:0000303|PubMed:22303807};
DE EC=2.7.3.3 {ECO:0000250|UniProtKB:C7E3T4};
DE AltName: Allergen=Oct f 2 {ECO:0000305};
OS Amphioctopus fangsiao (Ocellated octopus) (Octopus ocellatus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Amphioctopus.
OX NCBI_TaxID=515817 {ECO:0000312|EMBL:AEK65120.1};
RN [1] {ECO:0000312|EMBL:AEK65120.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-47; 87-116; 122-133;
RP 172-185; 209-227; 301-320; 321-335 AND 336-342, IDENTIFICATION BY MASS
RP SPECTROMETRY, 3D-STRUCTURE MODELING, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000303|PubMed:22303807};
RX PubMed=22303807; DOI=10.1021/jf203779w;
RA Shen H.W., Cao M.J., Cai Q.F., Ruan M.M., Mao H.Y., Su W.J., Liu G.M.;
RT "Purification, Cloning, and Immunological Characterization of Arginine
RT Kinase, a Novel Allergen of Octopus fangsiao.";
RL J. Agric. Food Chem. 60:2190-2199(2012).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000250|UniProtKB:Q004B5}.
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:C7E3T4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable below pH 9.0. Degrades by incubation at pH 9.5 and 10.0 for 1
CC hour. {ECO:0000269|PubMed:22303807};
CC Temperature dependence:
CC Relatively stable below 30 degrees Celsius, but aggregates above 40
CC degrees Celsius. Flocculent precipitate appears by incubation at 70
CC degrees Celsius for 30 min. {ECO:0000269|PubMed:22303807};
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:22303807}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 33% of
CC the 12 patients tested allergic to octopus. IgE-binding activity can be
CC significantly reduced with thermal, acidic or alkali treatment.
CC {ECO:0000269|PubMed:22303807}.
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; JN127374; AEK65120.1; -; mRNA.
DR AlphaFoldDB; G1ESZ9; -.
DR SMR; G1ESZ9; -.
DR Allergome; 9898; Oct f 2.
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: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 Allergen; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..348
FT /note="Arginine kinase Oct f 2"
FT /id="PRO_0000447435"
FT DOMAIN 1..83
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 111..347
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 56..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 114..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT BINDING 272..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 300..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT CONFLICT 88
FT /note="H -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="I -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="NM -> SL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="E -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="C -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39239 MW; A97B448E88371E71 CRC64;
MAEELFKTLQ NAKECHSLLK KHLTKERFDK LKGLKTKFGG TLADCIRSGC KNPDSGVGIY
ASDPDAYTVF AEVLDAVIMD YHKIDKVHHP IPDFGDVNNL NIGDLDPSGN MIVSTRVRVG
RSHDSFGFPP VLKKDDRIKM EQVSVEALKS LDGELAGSYF PLANMSADVQ KQLTEDHFLF
NDSDRFLKAA SGYDDWPIGR GIYFSENKTF LCWVNEEDHL RLISMQKGGN LGEVYKRLVS
AINKMEKKLN FAKKDNMGYL TFCPSNLGTT MRASVHIKIP KLSQRSDFKS ICDKYNLQAR
GIHGEHTESV CGVYDISNKR RMGLTEYEAV TEMMRGVNEI IREETNST
