位置:首页 > 蛋白库 > KARG_AMPFA
KARG_AMPFA
ID   KARG_AMPFA              Reviewed;         348 AA.
AC   G1ESZ9;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Arginine kinase Oct f 2 {ECO:0000303|PubMed:22303807};
DE            Short=AK {ECO:0000303|PubMed:22303807};
DE            EC=2.7.3.3 {ECO:0000250|UniProtKB:C7E3T4};
DE   AltName: Allergen=Oct f 2 {ECO:0000305};
OS   Amphioctopus fangsiao (Ocellated octopus) (Octopus ocellatus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Amphioctopus.
OX   NCBI_TaxID=515817 {ECO:0000312|EMBL:AEK65120.1};
RN   [1] {ECO:0000312|EMBL:AEK65120.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-47; 87-116; 122-133;
RP   172-185; 209-227; 301-320; 321-335 AND 336-342, IDENTIFICATION BY MASS
RP   SPECTROMETRY, 3D-STRUCTURE MODELING, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP   SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Muscle {ECO:0000303|PubMed:22303807};
RX   PubMed=22303807; DOI=10.1021/jf203779w;
RA   Shen H.W., Cao M.J., Cai Q.F., Ruan M.M., Mao H.Y., Su W.J., Liu G.M.;
RT   "Purification, Cloning, and Immunological Characterization of Arginine
RT   Kinase, a Novel Allergen of Octopus fangsiao.";
RL   J. Agric. Food Chem. 60:2190-2199(2012).
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:C7E3T4};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable below pH 9.0. Degrades by incubation at pH 9.5 and 10.0 for 1
CC         hour. {ECO:0000269|PubMed:22303807};
CC       Temperature dependence:
CC         Relatively stable below 30 degrees Celsius, but aggregates above 40
CC         degrees Celsius. Flocculent precipitate appears by incubation at 70
CC         degrees Celsius for 30 min. {ECO:0000269|PubMed:22303807};
CC   -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC       {ECO:0000269|PubMed:22303807}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 33% of
CC       the 12 patients tested allergic to octopus. IgE-binding activity can be
CC       significantly reduced with thermal, acidic or alkali treatment.
CC       {ECO:0000269|PubMed:22303807}.
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; JN127374; AEK65120.1; -; mRNA.
DR   AlphaFoldDB; G1ESZ9; -.
DR   SMR; G1ESZ9; -.
DR   Allergome; 9898; Oct f 2.
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; ISS: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; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..348
FT                   /note="Arginine kinase Oct f 2"
FT                   /id="PRO_0000447435"
FT   DOMAIN          1..83
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          111..347
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         56..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q004B5"
FT   BINDING         114..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q004B5"
FT   BINDING         221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q004B5"
FT   BINDING         272..276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         300..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q004B5"
FT   CONFLICT        88
FT                   /note="H -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="I -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110..111
FT                   /note="NM -> SL (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="E -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="C -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  39239 MW;  A97B448E88371E71 CRC64;
     MAEELFKTLQ NAKECHSLLK KHLTKERFDK LKGLKTKFGG TLADCIRSGC KNPDSGVGIY
     ASDPDAYTVF AEVLDAVIMD YHKIDKVHHP IPDFGDVNNL NIGDLDPSGN MIVSTRVRVG
     RSHDSFGFPP VLKKDDRIKM EQVSVEALKS LDGELAGSYF PLANMSADVQ KQLTEDHFLF
     NDSDRFLKAA SGYDDWPIGR GIYFSENKTF LCWVNEEDHL RLISMQKGGN LGEVYKRLVS
     AINKMEKKLN FAKKDNMGYL TFCPSNLGTT MRASVHIKIP KLSQRSDFKS ICDKYNLQAR
     GIHGEHTESV CGVYDISNKR RMGLTEYEAV TEMMRGVNEI IREETNST
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024