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UniProtKB/Swiss-Prot entry P06859

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PA21B_TRIFL
Primary accession number P06859
Secondary accession number Q92118
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on August 1, 1991 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 76)
Name and origin of the protein
Protein name Phospholipase A2 isozyme 1 [Precursor]
Synonyms EC 3.1.1.4
Phospholipase A2 isozyme I
pgPLA 1a/pgPLA 2a
Phosphatidylcholine 2-acylhydrolase
Gene name None
From
Trimeresurus flavoviridis (Habu) (Protobothrops flavoviridis) [TaxID: 88087] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=1707052 [NCBI, ExPASy, EBI, Israel, Japan]
Oda N., Ogawa T., Ohno M., Sasaki H., Sakaki Y., Kihara H.;
"Cloning and sequence analysis of cDNA for Trimeresurus flavoviridis phospholipase A2, and consequent revision of the amino acid sequence.";
J. Biochem. 108:816-821(1990).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME [THR37]PLA2).
TISSUE=Venom gland;
PubMed=1528861 [NCBI, ExPASy, EBI, Israel, Japan]
Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y., Kihara H., Ohno M.;
"Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=8327468 [NCBI, ExPASy, EBI, Israel, Japan]
Nakashima K., Ogawa T., Oda N., Hattori M., Sakaki Y., Kihara H., Ohno M.;
"Accelerated evolution of Trimeresurus flavoviridis venom gland phospholipase A2 isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 90:5964-5968(1993).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=7765285 [NCBI, ExPASy, EBI, Israel, Japan]
Nakashima K., Nobuhisa I., Ogawa T., Hattori M., Sakaki Y., Kihara H., Ohno M.;
"Polymorphisms of Trimeresurus flavoviridis venom gland phospholipase A2 isozyme genes.";
Biosci. Biotechnol. Biochem. 58:1510-1511(1994).
[5]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Amami-Oshima, and Okinawa;
Chijiwa T., Yamaguchi Y., Ogawa T., Deshimaru M., Nobuhisa I., Nakashima K., Oda-Ueda N., Shimohigashi Y., Fukumaki Y., Hattori S., Ohno M.;
"Regional evolution of Trimeresurus flavoviridis venom-gland phospholipase A2 isoenzymes.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[6]
 PROTEIN SEQUENCE OF 17-138.
TISSUE=Venom;
PubMed=3514593 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka S., Mohri N., Kihara H., Ohno M.;
"Amino acid sequence of Trimeresurus flavoviridis phospholipase A2.";
J. Biochem. 99:281-289(1986).
[7]
 PROTEIN SEQUENCE OF 17-47.
TISSUE=Venom;
DOI=10.1016/0041-0101(86)90138-8; PubMed=3564060 [NCBI, ExPASy, EBI, Israel, Japan]
Kini R.M., Kawabata S., Iwanaga S.;
"Comparison of amino terminal region of three isoenzymes of phospholipases A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from Trimeresurus flavoviridis (habu snake) venom and the complete amino acid sequence of the basic phospholipase, TFV PL-X.";
Toxicon 24:1117-1129(1986).
[8]
 ACTIVE SITES.
PubMed=2628422 [NCBI, ExPASy, EBI, Israel, Japan]
Kohzuma T., Oda N., Kihara H., Ohno M.;
"Investigation of an active site histidine-aspartate couple in Trimeresurus flavoviridis phospholipase A2.";
J. Biochem. 106:1054-1058(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D10070; BAA00962.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10720; BAA01563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10722; BAA01565.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10724; BAA01567.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB072174; BAB68547.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB072175; BAB68548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46169; A46169.
A48188; A48188.
B48188; PSTVIF.
3D structure databases
HSSP P51972; 1VAP. [HSSP ENTRY / PDB]
SMR P06859; 18-138.
ModBase P06859.
Family and domain databases
InterPro IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
Graphical view of domain structure.
Gene3D G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER PTHR11716; Phospholipase_A2; 1.
Pfam PF00068; Phospholip_A2_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00389; PHPHLIPASEA2.
ProDom PD000303; PhospholipaseA2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00085; PA2c; 1.
SMART graphical view of domain structure.
PROSITE PS00119; PA2_ASP; 1.
PS00118; PA2_HIS; 1.
BLOCKS P06859.
Phylogenomic databases
HOVERGEN P06859; -.
Other
ProtoNet P06859.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Direct protein sequencing; Hydrolase; Lipid degradation; Metal-binding; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    16  16      
CHAIN   17   138  122     Phospholipase A2 isozyme 1. PRO_0000022952
ACT_SITE   63    63         
ACT_SITE   104   104         
METAL   43    43        Calcium; via carbonyl oxygen (By similarity). 
METAL   45    45        Calcium; via carbonyl oxygen (By similarity). 
METAL   47    47        Calcium; via carbonyl oxygen (By similarity). 
METAL   64    64        Calcium (By similarity). 
DISULFID   42   131        By similarity. 
DISULFID   44    60        By similarity. 
DISULFID   59   110        By similarity. 
DISULFID   65   138        By similarity. 
DISULFID   66   103        By similarity. 
DISULFID   73    97        By similarity. 
DISULFID   91   101        By similarity. 
VARIANT   15    15  1     D -> E. 
VARIANT   53    53  1     K -> T (in isozyme [Thr37]PLA2). 
CONFLICT   85    88        NNGD -> QGN (in Ref. 6; AA sequence). 
CONFLICT   92    92        E -> G (in Ref. 6; AA sequence). 
CONFLICT   95    97        GPC -> DPCD (in Ref. 6; AA sequence). 
Sequence information
Length: 138 AA [This is the length of the unprocessed precursor] Molecular weight: 15535 Da [This is the MW of the unprocessed precursor] CRC64: FF24B8253FEA1A1A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRTLWIMAVL LVGVDGGLWQ FENMIIKVVK KSGILSYSAY GCYCGWGGRG KPKDATDRCC 

        70         80         90        100        110        120 
FVHDCCYGKV TGCNPKLGKY TYSWNNGDIV CEGDGPCKEV CECDRAAAIC FRDNLDTYDR 

       130 
NKYWRYPASN CQEDSEPC
P06859 in FASTA format

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