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KARG_PENVA
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   03-AUG-2022, entry version 58.
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}.
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DR   EMBL; EU346737; ABY57915.1; -; mRNA.
DR   AlphaFoldDB; B0FRF9; -.
DR   SMR; B0FRF9; -.
DR   Allergome; 3544; Lit v 2.
DR   BioCyc; MetaCyc:MON-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   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
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="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"
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
 
 
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