KARG_PROCL
ID KARG_PROCL Reviewed; 357 AA.
AC H6VGI2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Arginine kinase Pro c 2.0101 {ECO:0000303|PubMed:24055770};
DE Short=AK {ECO:0000303|PubMed:24055770};
DE EC=2.7.3.3 {ECO:0000250|UniProtKB:Q004B5};
DE AltName: Allergen=Pro c 2.0101 {ECO:0000305};
OS Procambarus clarkii (Red swamp crayfish).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Cambaridae; Procambarus.
OX NCBI_TaxID=6728 {ECO:0000312|EMBL:AFA45339.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-124; 181-245; 256-264;
RP 310-328 AND 330-354, IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE
RP MODELING, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, GLYCOSYLATION,
RP AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000303|PubMed:24055770};
RX PubMed=24055770; DOI=10.1016/j.fct.2013.09.014;
RA Chen H.L., Mao H.Y., Cao M.J., Cai Q.F., Su W.J., Zhang Y.X., Liu G.M.;
RT "Purification, physicochemical and immunological characterization of
RT arginine kinase, an allergen of crayfish (Procambarus clarkii).";
RL Food Chem. Toxicol. 62:475-484(2013).
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:Q004B5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable at pH 4.0-8.0. {ECO:0000269|PubMed:24055770};
CC Temperature dependence:
CC Stable at 30-44 degrees Celsius. Forms aggregates above 44 degrees
CC Celsius. {ECO:0000269|PubMed:24055770};
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:24055770}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:24055770}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 71% of
CC the 17 patients tested allergic to crustaceans. IgE-binding activity
CC increases in the 44-70 degrees Celsius temperature range, but is lost
CC at 80 degrees Celsius and above. IgE-binding activity is reduced under
CC alkaline conditions (pH 9.0-11.0), but is increased at acidic
CC conditions (pH 1.0-3.0). Allergenicity is reduced after 1 hour pepsin-
CC digestion in vitro. A 4-hour digestion by pancreatic enzymes in vitro
CC has little effect on the allergenicity. No change in allergenicity
CC after ultrasound treatment. Reduced allergenicity after 180 s of
CC microwave treatment or after boiling. The reduction in allergenicity is
CC correlated with the treatment duration. {ECO:0000269|PubMed:24055770}.
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; JN828651; AFA45339.1; -; mRNA.
DR AlphaFoldDB; H6VGI2; -.
DR SMR; H6VGI2; -.
DR Allergome; 11413; Pro c 2.
DR Allergome; 12146; Pro c 2.0101.
DR BRENDA; 2.7.3.3; 7182.
DR GO; GO:0034618; F:arginine binding; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
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; Glycoprotein; Kinase;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT CHAIN 2..357
FT /note="Arginine kinase Pro c 2.0101"
FT /id="PRO_0000447434"
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 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 CONFLICT 206
FT /note="V -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40120 MW; 29C45E87F9A00FA6 CRC64;
MADAATIAKL EEGFKKLEAA TDCKSLLKKY LSKSIFDSLK AKKTGLGATL LDVIQSGVEN
LDSGVGIYAP DAEAYSLFAP LFDPIIEDYH KGFKQTDKHP NKDFGDVNQF VNVDPDGKFV
ISTRVRCGRS LEGYPFNPCL TEAQYKEMEE KVSSTLSGLE GELKGTYYPL AGMTKEVQQK
LIDDHFLFKE GDRFLQAANA CRYWPVGRGI YHNDNKTFLV WCNEEDHLRI ISMQMGGDLG
QVYRRLVSAV NDIEKRVPFS HHDRLGFLTF CPTNLGTTIR ASVHIKLPKL AANREKLEEV
AARYSLQVRG TRGEHTEAEG GVYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEMA
