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Protein

Annexin A1

Gene

Anxa1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Promotes resolution of inflammation and wound healing (By similarity). Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation ofthe formyl peptide receptors (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca2+ and can bind up to eight Ca2+ ions (By similarity). Displays Ca2+-dependent binding to phospholipid membranes (PubMed:3020049). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca2+-dependent interaction between phagosomes and the actin cytoskeleton (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi60 – 601Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi62 – 621Calcium 1By similarity
Metal bindingi97 – 971Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi100 – 1001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi105 – 1051Calcium 2By similarity
Metal bindingi127 – 1271Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi129 – 1291Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi131 – 1311Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi132 – 1321Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi134 – 1341Calcium 4By similarity
Metal bindingi171 – 1711Calcium 3By similarity
Metal bindingi210 – 2101Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi213 – 2131Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi215 – 2151Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi253 – 2531Calcium 6By similarity
Metal bindingi255 – 2551Calcium 5By similarity
Metal bindingi256 – 2561Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi261 – 2611Calcium 6By similarity
Metal bindingi286 – 2861Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi288 – 2881Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi290 – 2901Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi328 – 3281Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi330 – 3301Calcium 7By similarity
Metal bindingi331 – 3311Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi336 – 3361Calcium 8By similarity

GO - Molecular functioni

  • annealing helicase activity Source: RGD
  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • double-stranded DNA-dependent ATPase activity Source: RGD
  • helicase activity Source: RGD
  • phospholipase A2 inhibitor activity Source: RGD
  • phospholipid binding Source: RGD
  • protein homodimerization activity Source: RGD
  • single-stranded DNA binding Source: RGD
  • structural molecule activity Source: Ensembl

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • adaptive immune response Source: UniProtKB-KW
  • alpha-beta T cell differentiation Source: Ensembl
  • arachidonic acid secretion Source: Ensembl
  • cell surface receptor signaling pathway Source: RGD
  • cellular response to glucocorticoid stimulus Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: RGD
  • DNA duplex unwinding Source: RGD
  • DNA rewinding Source: RGD
  • endocrine pancreas development Source: RGD
  • estrous cycle Source: RGD
  • gliogenesis Source: RGD
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: UniProtKB
  • granulocyte chemotaxis Source: UniProtKB
  • hepatocyte differentiation Source: RGD
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • insulin secretion Source: RGD
  • keratinocyte differentiation Source: Ensembl
  • monocyte chemotaxis Source: UniProtKB
  • myoblast migration involved in skeletal muscle regeneration Source: Ensembl
  • negative regulation of exocytosis Source: UniProtKB
  • negative regulation of interleukin-8 secretion Source: Ensembl
  • negative regulation of phospholipase A2 activity Source: RGD
  • negative regulation of protein secretion Source: RGD
  • negative regulation of T-helper 2 cell differentiation Source: UniProtKB
  • neutrophil clearance Source: Ensembl
  • peptide cross-linking Source: Ensembl
  • phagocytosis Source: UniProtKB
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of neutrophil apoptotic process Source: Ensembl
  • positive regulation of prostaglandin biosynthetic process Source: RGD
  • positive regulation of T cell proliferation Source: UniProtKB
  • positive regulation of T-helper 1 cell differentiation Source: UniProtKB
  • positive regulation of vesicle fusion Source: Ensembl
  • positive regulation of wound healing Source: UniProtKB
  • prolactin secretion Source: RGD
  • prostate gland development Source: RGD
  • regulation of cell shape Source: UniProtKB
  • regulation of hormone secretion Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of interleukin-1 production Source: UniProtKB
  • regulation of leukocyte migration Source: UniProtKB
  • response to corticosteroid Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hormone Source: RGD
  • response to interleukin-1 Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to X-ray Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Phospholipase A2 inhibitor

Keywords - Biological processi

Adaptive immunity, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-416476. G alpha (q) signalling events.
R-RNO-418594. G alpha (i) signalling events.
R-RNO-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A1
Alternative name(s):
Annexin I
Annexin-1
Calpactin II1 Publication
Calpactin-2
Chromobindin-9
Lipocortin I1 Publication
Phospholipase A2 inhibitory protein
p35
Gene namesi
Name:Anxa1
Synonyms:Anx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2118. Anxa1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cell projectioncilium By similarity
  • Basolateral cell membrane By similarity
  • Lateral cell membrane By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Apical cell membrane By similarity
  • Membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Secreted By similarity
  • Secretedextracellular space By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
  • Early endosome By similarity
  • Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
  • Secretedexosome By similarity
  • Cytoplasmic vesiclesecretory vesicle lumen By similarity
  • Cell projectionphagocytic cup By similarity

  • Note: Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (PubMed:3020049).By similarity1 Publication

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB-SubCell
  • cornified envelope Source: Ensembl
  • cytoplasm Source: RGD
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • early endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: RGD
  • extrinsic component of endosome membrane Source: UniProtKB
  • extrinsic component of external side of plasma membrane Source: UniProtKB
  • focal adhesion Source: Ensembl
  • lateral plasma membrane Source: UniProtKB
  • mast cell granule Source: RGD
  • mitochondrial membrane Source: RGD
  • motile cilium Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • phagocytic cup Source: UniProtKB-SubCell
  • plasma membrane Source: RGD
  • protein complex Source: RGD
  • sarcolemma Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 346345Annexin A1PRO_0000067464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51Phosphoserine; by TRPM7By similarity
Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Modified residuei21 – 211Phosphotyrosine; by EGFRBy similarity
Modified residuei27 – 271Phosphoserine; by PKCBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei136 – 1361PhosphothreonineBy similarity
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki214 – 214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei312 – 3121N6-acetyllysineBy similarity
Disulfide bondi324 ↔ 343By similarity
Cross-linki332 – 332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment.By similarity
Sumoylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP07150.
PRIDEiP07150.

PTM databases

iPTMnetiP07150.
PhosphoSiteiP07150.

Expressioni

Tissue specificityi

Detected in eosinophils (PubMed:12467520). Detected in lung, placenta, spleen and thymus (at protein level) (PubMed:3020049).2 Publications

Gene expression databases

GenevisibleiP07150. RN.

Interactioni

Subunit structurei

Homodimer; non-covalently linked (By similarity). Homodimer; linked by transglutamylation. Homodimers linked by transglutamylation are observed in placenta, but not in other tissues. Interacts with S100A11. Heterotetramer, formed by two molecules each of S100A11 and ANXA1 (By similarity). Interacts with DYSF (By similarity). Interacts with EGFR (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi247419. 2 interactions.
IntActiP07150. 2 interactions.
MINTiMINT-4542587.
STRINGi10116.ENSRNOP00000023664.

Structurei

3D structure databases

ProteinModelPortaliP07150.
SMRiP07150. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati51 – 11161Annexin 1Add
BLAST
Repeati123 – 18361Annexin 2Add
BLAST
Repeati207 – 26761Annexin 3Add
BLAST
Repeati282 – 34261Annexin 4Add
BLAST

Domaini

The full-length protein can bind eight Ca2+ ions via the annexin repeats. Calcium binding causes a major conformation change that modifies dimer contacts and leads to surface exposure of the N-terminal phosphorylation sites; in the absence of Ca2+, these sites are buried in the interior of the protein core. The N-terminal region becomes disordered in response to calcium-binding.By similarity
The N-terminal 26 amino acids are sufficient for its extracellular functions in the regulation of inflammation and wound healing. Acylated peptides that contain the first 26 amino acids of the mature protein can activate signaling via the formyl peptide receptors.By similarity

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP07150.
KOiK17091.
OMAiIMVSRHE.
OrthoDBiEOG74XS72.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVSEFLKQ ACYIEKQEQE YVQAVKSYKG GPGSAVSPYP SFNPSSDVAA
60 70 80 90 100
LHKAIMVKGV DEATIIDILT KRTNAQRQQI KAAYLQETGK PLDETLKKAL
110 120 130 140 150
TGHLEEVVLA MLKTPAQFDA DELRAAMKGL GTDEDTLIEI LTTRSNQQIR
160 170 180 190 200
EITRVYREEL KRDLAKDITS DTSGDFRNAL LALAKGDRCE DMSVNQDLAD
210 220 230 240 250
TDARALYEAG ERRKGTDVNV FNTILTTRSY PHLRKVFQNY RKYSQHDMNK
260 270 280 290 300
ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKTLIRIM
310 320 330 340
VSRSEIDMNE IKVFYQKKYG IPLCQAILDE TKGDYEKILV ALCGGN
Length:346
Mass (Da):38,829
Last modified:January 23, 2007 - v2
Checksum:iF046E5F410AF2CF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221P → S in AAB19866 (PubMed:1832554).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00446 mRNA. Translation: CAA68500.1.
M19967 mRNA. Translation: AAA40861.1.
S57478
, S57447, S57450, S57455, S57459, S57463, S57466, S57468, S57470, S57472, S57474, S57476 Genomic DNA. Translation: AAB19866.1.
BC061710 mRNA. Translation: AAH61710.1.
PIRiJT0303. LURT1.
RefSeqiNP_037036.1. NM_012904.2.
XP_008758517.1. XM_008760295.1.
UniGeneiRn.1792.

Genome annotation databases

EnsembliENSRNOT00000023664; ENSRNOP00000023664; ENSRNOG00000017469.
GeneIDi25380.
KEGGirno:25380.
UCSCiRGD:2118. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00446 mRNA. Translation: CAA68500.1.
M19967 mRNA. Translation: AAA40861.1.
S57478
, S57447, S57450, S57455, S57459, S57463, S57466, S57468, S57470, S57472, S57474, S57476 Genomic DNA. Translation: AAB19866.1.
BC061710 mRNA. Translation: AAH61710.1.
PIRiJT0303. LURT1.
RefSeqiNP_037036.1. NM_012904.2.
XP_008758517.1. XM_008760295.1.
UniGeneiRn.1792.

3D structure databases

ProteinModelPortaliP07150.
SMRiP07150. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247419. 2 interactions.
IntActiP07150. 2 interactions.
MINTiMINT-4542587.
STRINGi10116.ENSRNOP00000023664.

PTM databases

iPTMnetiP07150.
PhosphoSiteiP07150.

Proteomic databases

PaxDbiP07150.
PRIDEiP07150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023664; ENSRNOP00000023664; ENSRNOG00000017469.
GeneIDi25380.
KEGGirno:25380.
UCSCiRGD:2118. rat.

Organism-specific databases

CTDi301.
RGDi2118. Anxa1.

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
GeneTreeiENSGT00760000118972.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP07150.
KOiK17091.
OMAiIMVSRHE.
OrthoDBiEOG74XS72.

Enzyme and pathway databases

ReactomeiR-RNO-416476. G alpha (q) signalling events.
R-RNO-418594. G alpha (i) signalling events.
R-RNO-444473. Formyl peptide receptors bind formyl peptides and many other ligands.

Miscellaneous databases

PROiP07150.

Gene expression databases

GenevisibleiP07150. RN.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]
PANTHERiPTHR10502:SF17. PTHR10502:SF17. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00197. ANNEXINI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Lung.
  2. "Molecular cloning and expression in Escherichia coli of the cDNA coding for rat lipocortin I (calpactin II)."
    Shimizu Y., Takabayashi E., Yano S., Shimizu N., Yamada K., Gushima H.
    Gene 65:141-147(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Correlation of gene and protein structure of rat and human lipocortin I."
    Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.
    Biochemistry 30:9015-9021(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  5. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 59-71; 99-124; 129-144; 167-177; 186-204; 214-228; 251-281 AND 304-312, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fibroblast.
  6. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 99-113; 129-144 AND 215-228, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  7. "A calcium-dependent 35-kilodalton substrate for epidermal growth factor receptor/kinase isolated from normal tissue."
    De B.K., Misono K.S., Lukas T.J., Mroczkowski B., Cohen S.
    J. Biol. Chem. 261:13784-13792(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION.
  8. "Annexin 1 localisation in tissue eosinophils as detected by electron microscopy."
    Oliani S.M., Damazo A.S., Perretti M.
    Mediators Inflamm. 11:287-292(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Annexin-A1: a pivotal regulator of the innate and adaptive immune systems."
    D'Acquisto F., Perretti M., Flower R.J.
    Br. J. Pharmacol. 155:152-169(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiANXA1_RAT
AccessioniPrimary (citable) accession number: P07150
Secondary accession number(s): Q64664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Was originally identified as calcium and phospholipid binding protein that displays Ca2+-dependent binding to phospholipid membranes and can promote membrane aggregation in vitro. Was initially identified as inhibitor of phospholipase A2 activity (in vitro). Inhibition of phospholipase activity is mediated via its phospholipid binding activity that limits the access of phospholipase to its substrates.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.