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1:  NP_000919Reports  phospholipase A2,...[gi:4505847] BLink, Conserved Domains, Links
LOCUS       NP_000919                148 aa            linear   PRI 22-OCT-2008
DEFINITION  phospholipase A2, group IB [Homo sapiens].
ACCESSION   NP_000919
VERSION     NP_000919.1  GI:4505847
DBSOURCE    REFSEQ: accession NM_000928.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Kao,W.T., Yen,Y.C. and Lung,F.W.
  TITLE     The effects of beta2 adrenergic receptor gene polymorphism in lipid
            profiles
  JOURNAL   Lipids Health Dis 7, 20 (2008)
   PUBMED   18492292
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Gorovetz,M., Schwob,O., Krimsky,M., Yedgar,S. and Reich,R.
  TITLE     MMP production in human fibrosarcoma cells and their invasiveness
            are regulated by group IB secretory phospholipase A2
            receptor-mediated activation of cytosolic phospholipase A2
  JOURNAL   Front. Biosci. 13, 1917-1925 (2008)
   PUBMED   17981679
  REMARK    GeneRIF: MMP-2/9 production is regulated by sPLA2-IB acting as a
            receptor ligand to activate cPLA2
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Pan,Y.H. and Bahnson,B.J.
  TITLE     Structural basis for bile salt inhibition of pancreatic
            phospholipase A2
  JOURNAL   J. Mol. Biol. 369 (2), 439-450 (2007)
   PUBMED   17434532
  REMARK    GeneRIF: Results describe the structural basis for bile salt
            inhibition of pancreatic phospholipase A2.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Zarini,S., Gijon,M.A., Folco,G. and Murphy,R.C.
  TITLE     Effect of arachidonic acid reacylation on leukotriene biosynthesis
            in human neutrophils stimulated with granulocyte-macrophage
            colony-stimulating factor and formyl-methionyl-leucyl-phenylalanine
  JOURNAL   J. Biol. Chem. 281 (15), 10134-10142 (2006)
   PUBMED   16495221
  REMARK    GeneRIF: a critical regulatory role of arachidonate reacylation
            that limits leukotriene biosynthesis in concert with 5-lipoxygenase
            and cytosolic phospholipase A(2)alpha activation
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Egan,A., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Arita,H., Hanasaki,K., Nakano,T., Oka,S., Teraoka,H. and
            Matsumoto,K.
  TITLE     Novel proliferative effect of phospholipase A2 in Swiss 3T3 cells
            via specific binding site
  JOURNAL   J. Biol. Chem. 266 (29), 19139-19141 (1991)
   PUBMED   1918029
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Clark,M.A., Ozgur,L.E., Conway,T.M., Dispoto,J., Crooke,S.T. and
            Bomalaski,J.S.
  TITLE     Cloning of a phospholipase A2-activating protein
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (12), 5418-5422 (1991)
   PUBMED   2052621
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Seilhamer,J.J., Randall,T.L., Yamanaka,M. and Johnson,L.K.
  TITLE     Pancreatic phospholipase A2: isolation of the human gene and cDNAs
            from porcine pancreas and human lung
  JOURNAL   DNA 5 (6), 519-527 (1986)
   PUBMED   3028739
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Sternby,B. and Akerstrom,B.
  TITLE     Immunoreactive pancreatic colipase, lipase and phospholipase A2 in
            human plasma and urine from healthy individuals
  JOURNAL   Biochim. Biophys. Acta 789 (2), 164-169 (1984)
   PUBMED   6477929
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Verheij,H.M., Westerman,J., Sternby,B. and De Haas,G.H.
  TITLE     The complete primary structure of phospholipase A2 from human
            pancreas
  JOURNAL   Biochim. Biophys. Acta 747 (1-2), 93-99 (1983)
   PUBMED   6349696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M21054.1, AA844927.1, CA867923.1, BX113838.1 and BE969737.1.
            
            Summary: Phospholipase A2 (EC 3.1.1.4) catalyzes the release of
            fatty acids from glycero-3-phosphocholines. The best known
            varieties are the digestive enzymes secreted as zymogens by the
            pancreas of mammals. Sequences of pancreatic PLA2 enzymes from a
            variety of mammals have been reported. One striking feature of
            these enzymes is their close homology to venom phospholipases of
            snakes. Other forms of PLA2 have been isolated from brain, liver,
            lung, spleen, intestine, macrophages, leukocytes, erythrocytes,
            inflammatory exudates, chondrocytes, and platelets (Seilhamer et
            al., 1986 [PubMed 3028739]) .[supplied by OMIM].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the
            Entrez Gene record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23-q24.1"
     Protein         1..148
                     /product="phospholipase A2, group IB"
                     /EC_number="3.1.1.4"
                     /calculated_mol_wt=16229
     CDS             1..148
                     /gene="PLA2G1B"
                     /gene_synonym="PLA2"
                     /gene_synonym="PLA2A"
                     /gene_synonym="PPLA2"
                     /gene_synonym="MGC119834"
                     /gene_synonym="MGC119835"
                     /coded_by="NM_000928.2:37..483"
                     /db_xref="CCDS:CCDS9195.1"
                     /db_xref="GeneID:5319"
                     /db_xref="HGNC:9030"
                     /db_xref="HPRD:01396"
                     /db_xref="MIM:172410"
ORIGIN      
        1 mkllvlavll tvaaadsgis pravwqfrkm ikcvipgsdp fleynnygcy cglggsgtpv
       61 deldkccqth dncydqakkl dsckflldnp ythtysyscs gsaitcsskn keceaficnc
      121 drnaaicfsk apynkahknl dtkkycqs
//

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Last update: Wed, 05 Nov 2008 Rev. 145015