ID KARG_PENVA Reviewed; 356 AA. AC B0FRF9; DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 13-SEP-2023, entry version 62. DE RecName: Full=Arginine kinase Lit v 2 {ECO:0000305}; DE EC=2.7.3.3 {ECO:0000269|PubMed:19239924}; DE AltName: Full=Arginine kinase {ECO:0000303|PubMed:19239924, ECO:0000312|EMBL:ABY57915.1}; DE Short=AK {ECO:0000303|PubMed:19239924}; DE AltName: Allergen=Lit v 2 {ECO:0000305}; OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata; OC Penaeoidea; Penaeidae; Penaeus. OX NCBI_TaxID=6689; RN [1] {ECO:0000312|EMBL:ABY57915.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Muscle {ECO:0000303|PubMed:19239924}; RX PubMed=19239924; DOI=10.1016/j.fsi.2009.02.012; RA Yao C.L., Ji P.F., Kong P., Wang Z.Y., Xiang J.H.; RT "Arginine kinase from Litopenaeus vannamei: cloning, expression and RT catalytic properties."; RL Fish Shellfish Immunol. 26:553-558(2009). CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma- CC phosphate group to L-arginine. {ECO:0000269|PubMed:19239924}. 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:19239924}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941; CC Evidence={ECO:0000305|PubMed:19239924}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22942; CC Evidence={ECO:0000305|PubMed:19239924}; CC -!- ACTIVITY REGULATION: No change in activity after supplementation with CC 10 mM glucose. However, activity decreases significantly when glucose CC concentration is higher than 50 mM and almost all activity is lost with CC 200 mM glucose. Activity is significantly increased after treatment CC with 10 mM and 50 mM ATP. However, activity drops significantly with CC 200 mM ATP. Inhibited by 10-200 mM alpha-ketoglutarate. No change in CC activity after incubation with 10-200 mM L-citrulline, L-ornaline or CC glycerol. {ECO:0000269|PubMed:19239924}. CC -!- TISSUE SPECIFICITY: Expressed in muscle (at protein level). Expressed CC in muscle, heart, nerve, stomach and hemocytes, with the highest CC expression in muscle. Very low expression in eyestalk and intestine. CC Not expressed in hepatopancreas, gill and skin. CC {ECO:0000269|PubMed:19239924}. CC -!- INDUCTION: By LPS immunostimulation. In hemocytes, expression increases CC sharply at 3 hours, decreases slightly at 6 hours, increases CC significantly again at 24 hours and decreases at 48 hours after LPS CC injection. In muscle, expressed less than the control in the first 6 CC hours, then the expression increases strikingly from 6 to 24 hours and CC decreases at 48 hours after LPS injection. CC {ECO:0000269|PubMed:19239924}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE CC (Probable). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00843, ECO:0000255|RuleBase:RU000505, CC ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU346737; ABY57915.1; -; mRNA. DR AlphaFoldDB; B0FRF9; -. DR SMR; B0FRF9; -. DR Allergome; 3544; Lit v 2. DR BioCyc; MetaCyc:MONOMER-18221; -. DR BRENDA; 2.7.3.3; 4594. DR GO; GO:0004054; F:arginine kinase activity; IDA: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; IDA:UniProtKB. DR CDD; cd07932; arginine_kinase_like; 1. DR Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1. DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1. DR Pfam; PF00217; ATP-gua_Ptrans; 1. DR Pfam; PF02807; ATP-gua_PtransN; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 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; Kinase; Nucleotide-binding; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q004B5" FT CHAIN 2..356 FT /note="Arginine kinase Lit v 2" FT /evidence="ECO:0000250|UniProtKB:Q004B5" FT /id="PRO_0000447431" 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="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" 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="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" 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="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" 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="L-arginine" FT /ligand_id="ChEBI:CHEBI:32682" FT /evidence="ECO:0000250|UniProtKB:Q004B5" SQ SEQUENCE 356 AA; 40168 MW; E9C88AE671AB1BBB CRC64; MADAAVIEKL EAGFKKLEAA TDCKSLLKKY LTKEVFDKLK DKKTSLGATL LDVIQSGVEN LDSGVGIYAP DAEAYTLFAP LFDPIIEDYH VGFKQTDKHP NKDFGDVNSF VNVDPEGKFV ISTRVRCGRS MQGYPFNPCL TESQYKEMEA KVSSTLSSLE GELKGTYYPL TGMSKEVQQK LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WVNEEDHLRI ISMQMGGDLG QVFRRLTSAV NEIEKRIPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV AGKYNLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KMEKEM //