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 05-JUN-2019, entry version 51. 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 CC gamma-phosphate group to L-arginine. CC {ECO:0000269|PubMed:19239924}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L- CC arginine; Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, CC 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 CC with 10 mM glucose. However, activity decreases significantly when CC glucose concentration is higher than 50 mM and almost all activity CC is lost with 200 mM glucose. Activity is significantly increased CC after treatment with 10 mM and 50 mM ATP. However, activity drops CC significantly with 200 mM ATP. Inhibited by 10-200 mM alpha- CC ketoglutarate. No change in activity after incubation with 10-200 CC mM L-citrulline, L-ornaline or glycerol. CC {ECO:0000269|PubMed:19239924}. CC -!- TISSUE SPECIFICITY: Expressed in muscle (at protein level). CC Expressed in muscle, heart, nerve, stomach and hemocytes, with the CC highest expression in muscle. Very low expression in eyestalk and CC intestine. Not expressed in hepatopancreas, gill and skin. CC {ECO:0000269|PubMed:19239924}. CC -!- INDUCTION: By LPS immunostimulation. In hemocytes, expression CC increases sharply at 3 hours, decreases slightly at 6 hours, CC increases significantly again at 24 hours and decreases at 48 CC hours after LPS injection. In muscle, expressed less than the CC control in the first 6 hours, then the expression increases CC strikingly from 6 to 24 hours and decreases at 48 hours after LPS CC injection. {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, CC ECO:0000255|RuleBase:RU000505, 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 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; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; Kinase; Nucleotide-binding; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q004B5}. FT CHAIN 2 356 Arginine kinase Lit v 2. FT {ECO:0000250|UniProtKB:Q004B5}. FT /FTId=PRO_0000447431. FT DOMAIN 9 91 Phosphagen kinase N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00842}. FT DOMAIN 119 356 Phosphagen kinase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00843}. FT NP_BIND 122 126 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00843}. FT NP_BIND 280 284 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00843}. FT NP_BIND 309 314 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00843}. FT REGION 64 68 Substrate binding. FT {ECO:0000250|UniProtKB:Q004B5}. FT BINDING 185 185 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00843}. FT BINDING 225 225 Substrate. FT {ECO:0000250|UniProtKB:Q004B5}. FT BINDING 229 229 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00843}. FT BINDING 271 271 Substrate. FT {ECO:0000250|UniProtKB:Q004B5}. FT BINDING 314 314 Substrate. FT {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 //