KARG_PENMO
ID KARG_PENMO Reviewed; 356 AA.
AC C7E3T4; Q8I9P7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Arginine kinase {ECO:0000303|Ref.2, ECO:0000312|EMBL:ACT34086.1};
DE Short=AK {ECO:0000250|UniProtKB:P51541};
DE EC=2.7.3.3;
DE AltName: Allergen=Pen m 2 {ECO:0000303|PubMed:12496430, ECO:0000312|EMBL:AAO15713.1};
GN Name=AK {ECO:0000312|EMBL:AAO15713.1};
OS Penaeus monodon (Giant tiger prawn).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6687;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO15713.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-9 AND 257-264, CATALYTIC
RP ACTIVITY, ALLERGEN, AND ACETYLATION AT ALA-2.
RC TISSUE=Muscle {ECO:0000312|EMBL:AAO15713.1};
RX PubMed=12496430; DOI=10.4049/jimmunol.170.1.445;
RA Yu C.J., Lin Y.F., Chiang B.L., Chow L.P.;
RT "Proteomics and immunological analysis of a novel shrimp allergen, Pen m
RT 2.";
RL J. Immunol. 170:445-453(2003).
RN [2] {ECO:0000312|EMBL:ACT34086.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wong J., Chew F.T.;
RT "Isolation and characterization of arginine kinase from Penaeus monodon.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 34-42; 152-175; 181-189; 230-264 AND 310-328, AND
RP ALLERGENICITY.
RC TISSUE=Muscle {ECO:0000269|Ref.2};
RX DOI=10.1002/rcm.4664;
RA Abdel Rahman A.M., Kamath S., Lopata A.L., Helleur R.J.;
RT "Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon)
RT and characterization of the major allergen tropomyosin using mass
RT spectrometry.";
RL Rapid Commun. Mass Spectrom. 24:2462-2470(2010).
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:0000269|PubMed:12496430};
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:12496430, ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; AF479772; AAO15713.1; -; mRNA.
DR EMBL; GQ246164; ACT34086.1; -; mRNA.
DR AlphaFoldDB; C7E3T4; -.
DR SMR; C7E3T4; -.
DR Allergome; 3411; Pen m 2.0101.
DR Allergome; 792; Pen m 2.
DR iPTMnet; C7E3T4; -.
DR GO; GO:0004054; F:arginine kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IDA: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 Acetylation; Allergen; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12496430"
FT CHAIN 2..356
FT /note="Arginine kinase"
FT /evidence="ECO:0000269|PubMed:12496430"
FT /id="PRO_0000398786"
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:P51541"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51541"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51541"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51541,
FT ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12496430"
FT CONFLICT 279
FT /note="V -> A (in Ref. 1; AAO15713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40141 MW; 9BA42BB9342D4903 CRC64;
MADAAVIEKL EAGFKKLEAA TDCKSLLKKY LSKAVFDQLK EKKTSLGATL LDVIQSGVEN
LDSGVGIYAP DAEAYTLFSP LFDPIIEDYH VGFKQTDKHP NKDFGDVNTF VNVDPEGKYV
ISTRVRCGRS MEGYPFNPCL TEAQYKEMEA KVSSTLSSLE GELKGTYYPL TGMSKEVQQK
LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WVNEEDHLRI ISMQMGGDLG
QVFRRLTSAV NEIEKRIPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AGKYNLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KMEKEM
