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ANXA1_RAT
ID   ANXA1_RAT               Reviewed;         346 AA.
AC   P07150; Q64664;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Annexin A1;
DE   AltName: Full=Annexin I;
DE   AltName: Full=Annexin-1;
DE   AltName: Full=Calpactin II {ECO:0000303|PubMed:2969352};
DE   AltName: Full=Calpactin-2;
DE   AltName: Full=Chromobindin-9;
DE   AltName: Full=Lipocortin I {ECO:0000303|PubMed:2958780};
DE   AltName: Full=Phospholipase A2 inhibitory protein;
DE   AltName: Full=p35;
DE   Contains:
DE     RecName: Full=Annexin Ac2-26 {ECO:0000250|UniProtKB:P04083};
GN   Name=Anxa1; Synonyms=Anx1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Lung;
RX   PubMed=2958780; DOI=10.1093/nar/15.18.7637;
RA   Tamaki M., Nakamura E., Nishikubo C., Sakata T., Shin M., Teraoka H.;
RT   "Rat lipocortin I cDNA.";
RL   Nucleic Acids Res. 15:7637-7637(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2969352; DOI=10.1016/0378-1119(88)90427-1;
RA   Shimizu Y., Takabayashi E., Yano S., Shimizu N., Yamada K., Gushima H.;
RT   "Molecular cloning and expression in Escherichia coli of the cDNA coding
RT   for rat lipocortin I (calpactin II).";
RL   Gene 65:141-147(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1832554; DOI=10.1021/bi00101a015;
RA   Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P.;
RT   "Correlation of gene and protein structure of rat and human lipocortin I.";
RL   Biochemistry 30:9015-9021(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-9; 59-71; 99-124; 129-144; 167-177; 186-204; 214-228;
RP   251-281 AND 304-312, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fibroblast;
RA   Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL   Submitted (JUN-2009) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 99-113; 129-144 AND 215-228, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [7]
RP   TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=3020049; DOI=10.1016/s0021-9258(18)67088-7;
RA   De B.K., Misono K.S., Lukas T.J., Mroczkowski B., Cohen S.;
RT   "A calcium-dependent 35-kilodalton substrate for epidermal growth factor
RT   receptor/kinase isolated from normal tissue.";
RL   J. Biol. Chem. 261:13784-13792(1986).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12467520; DOI=10.1080/09629350210000015683;
RA   Oliani S.M., Damazo A.S., Perretti M.;
RT   "Annexin 1 localisation in tissue eosinophils as detected by electron
RT   microscopy.";
RL   Mediators Inflamm. 11:287-292(2002).
RN   [9]
RP   REVIEW.
RX   PubMed=18641677; DOI=10.1038/bjp.2008.252;
RA   D'Acquisto F., Perretti M., Flower R.J.;
RT   "Annexin-A1: a pivotal regulator of the innate and adaptive immune
RT   systems.";
RL   Br. J. Pharmacol. 155:152-169(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Plays important roles in the innate immune response as
CC       effector of glucocorticoid-mediated responses and regulator of the
CC       inflammatory process. Has anti-inflammatory activity. Plays a role in
CC       glucocorticoid-mediated down-regulation of the early phase of the
CC       inflammatory response. Contributes to the adaptive immune response by
CC       enhancing signaling cascades that are triggered by T-cell activation,
CC       regulates differentiation and proliferation of activated T-cells.
CC       Promotes the differentiation of T-cells into Th1 cells and negatively
CC       regulates differentiation into Th2 cells (By similarity). Has no effect
CC       on unstimulated T-cells. Negatively regulates hormone exocytosis via
CC       activation of the formyl peptide receptors and reorganization of the
CC       actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and
CC       can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-
CC       dependent binding to phospholipid membranes (PubMed:3020049). Plays a
CC       role in the formation of phagocytic cups and phagosomes. Plays a role
CC       in phagocytosis by mediating the Ca(2+)-dependent interaction between
CC       phagosomes and the actin cytoskeleton (By similarity).
CC       {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107,
CC       ECO:0000250|UniProtKB:P19619, ECO:0000269|PubMed:3020049}.
CC   -!- FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating
CC       the formyl peptide receptors and downstream signaling cascades.
CC       Promotes chemotaxis of granulocytes and monocytes via activation of the
CC       formyl peptide receptors. Promotes rearrangement of the actin
CC       cytoskeleton, cell polarization and cell migration. Promotes resolution
CC       of inflammation and wound healing. Acts via neutrophil N-formyl peptide
CC       receptors to enhance the release of CXCL2.
CC       {ECO:0000250|UniProtKB:P04083}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked (By similarity). Homodimer;
CC       linked by transglutamylation. Homodimers linked by transglutamylation
CC       are observed in placenta, but not in other tissues. Interacts with
CC       S100A11. Heterotetramer, formed by two molecules each of S100A11 and
CC       ANXA1 (By similarity). Interacts with DYSF (By similarity). Interacts
CC       with EGFR (By similarity). {ECO:0000250|UniProtKB:P04083,
CC       ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12467520}. Cytoplasm
CC       {ECO:0000269|PubMed:12467520}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane
CC       {ECO:0000250|UniProtKB:P10107}. Cell membrane
CC       {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P10107}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000269|PubMed:3020049};
CC       Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Endosome
CC       membrane {ECO:0000269|PubMed:3020049}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:3020049}. Secreted {ECO:0000250|UniProtKB:P10107}.
CC       Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell
CC       membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P04083}; Extracellular side
CC       {ECO:0000250|UniProtKB:P04083}. Early endosome
CC       {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P19619}. Secreted, extracellular exosome
CC       {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle
CC       lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup
CC       {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at
CC       phagocytic cups. Secreted, at least in part via exosomes and other
CC       secretory vesicles. Detected in exosomes and other extracellular
CC       vesicles. Secretion is increased in response to wounding and
CC       inflammation (By similarity). Alternatively, the secretion is dependent
CC       on protein unfolding and facilitated by the cargo receptor TMED10; it
CC       results in the protein translocation from the cytoplasm into ERGIC
CC       (endoplasmic reticulum-Golgi intermediate compartment) followed by
CC       vesicle entry and secretion (By similarity). Detected in gelatinase
CC       granules in resting neutrophils. Neutrophil adhesion to endothelial
CC       cells stimulates secretion via gelatinase granules, but foreign
CC       particle phagocytosis has no effect. Displays calcium-dependent binding
CC       to phospholipid membranes (PubMed:3020049).
CC       {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107,
CC       ECO:0000269|PubMed:3020049}.
CC   -!- TISSUE SPECIFICITY: Detected in eosinophils (PubMed:12467520). Detected
CC       in lung, placenta, spleen and thymus (at protein level)
CC       (PubMed:3020049). {ECO:0000269|PubMed:12467520,
CC       ECO:0000269|PubMed:3020049}.
CC   -!- DOMAIN: The full-length protein can bind eight Ca(2+) ions via the
CC       annexin repeats. Calcium binding causes a major conformation change
CC       that modifies dimer contacts and leads to surface exposure of the N-
CC       terminal phosphorylation sites; in the absence of Ca(2+), these sites
CC       are buried in the interior of the protein core. The N-terminal region
CC       becomes disordered in response to calcium-binding.
CC       {ECO:0000250|UniProtKB:P19619}.
CC   -!- PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated
CC       in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.
CC   -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.
CC   -!- PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-
CC       terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}.
CC   -!- MISCELLANEOUS: Was originally identified as calcium and phospholipid
CC       binding protein that displays Ca(2+)-dependent binding to phospholipid
CC       membranes and can promote membrane aggregation in vitro. Was initially
CC       identified as inhibitor of phospholipase A2 activity (in vitro).
CC       Inhibition of phospholipase activity is mediated via its phospholipid
CC       binding activity that limits the access of phospholipase to its
CC       substrates. {ECO:0000250|UniProtKB:P10107}.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; Y00446; CAA68500.1; -; mRNA.
DR   EMBL; M19967; AAA40861.1; -; mRNA.
DR   EMBL; S57478; AAB19866.1; -; Genomic_DNA.
DR   EMBL; S57447; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57450; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57455; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57459; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57463; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57466; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57468; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57470; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57472; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57474; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; S57476; AAB19866.1; JOINED; Genomic_DNA.
DR   EMBL; BC061710; AAH61710.1; -; mRNA.
DR   PIR; JT0303; LURT1.
DR   RefSeq; NP_037036.1; NM_012904.2.
DR   RefSeq; XP_008758517.1; XM_008760295.2.
DR   AlphaFoldDB; P07150; -.
DR   SMR; P07150; -.
DR   BioGRID; 247419; 5.
DR   IntAct; P07150; 2.
DR   STRING; 10116.ENSRNOP00000023664; -.
DR   iPTMnet; P07150; -.
DR   PhosphoSitePlus; P07150; -.
DR   jPOST; P07150; -.
DR   PaxDb; P07150; -.
DR   PRIDE; P07150; -.
DR   Ensembl; ENSRNOT00000096060; ENSRNOP00000090466; ENSRNOG00000017469.
DR   GeneID; 25380; -.
DR   KEGG; rno:25380; -.
DR   UCSC; RGD:2118; rat.
DR   CTD; 301; -.
DR   RGD; 2118; Anxa1.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000155221; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; P07150; -.
DR   OMA; AKADRCE; -.
DR   OrthoDB; 856254at2759; -.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR   PRO; PR:P07150; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017469; Expressed in lung and 19 other tissues.
DR   Genevisible; P07150; RN.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR   GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR   GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042629; C:mast cell granule; IDA:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR   GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR   GO; GO:0097060; C:synaptic membrane; IDA:SynGO.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR   GO; GO:1990814; F:DNA/DNA annealing activity; IDA:RGD.
DR   GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:RGD.
DR   GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0046632; P:alpha-beta T cell differentiation; ISO:RGD.
DR   GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:BHF-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:RGD.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:RGD.
DR   GO; GO:0031018; P:endocrine pancreas development; IEP:RGD.
DR   GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISS:UniProtKB.
DR   GO; GO:0042063; P:gliogenesis; IEP:RGD.
DR   GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; IDA:RGD.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR   GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISO:RGD.
DR   GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
DR   GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:RGD.
DR   GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:RGD.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IMP:RGD.
DR   GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
DR   GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR   GO; GO:0097350; P:neutrophil clearance; ISO:RGD.
DR   GO; GO:0001780; P:neutrophil homeostasis; ISO:RGD.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR   GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
DR   GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; ISO:RGD.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; ISS:UniProtKB.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:RGD.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR   GO; GO:0070459; P:prolactin secretion; IMP:RGD.
DR   GO; GO:0030850; P:prostate gland development; IEP:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0032652; P:regulation of interleukin-1 production; ISS:UniProtKB.
DR   GO; GO:0002685; P:regulation of leukocyte migration; ISS:UniProtKB.
DR   GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0009725; P:response to hormone; IEP:RGD.
DR   GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0010165; P:response to X-ray; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   Gene3D; 1.10.220.10; -; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR002388; ANX1.
DR   PANTHER; PTHR10502:SF17; PTHR10502:SF17; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00197; ANNEXINI.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Adaptive immunity; Annexin; Calcium;
KW   Calcium/phospholipid-binding; Cell membrane; Cell projection; Cilium;
KW   Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   Endosome; Immunity; Inflammatory response; Innate immunity;
KW   Isopeptide bond; Membrane; Metal-binding; Nucleus;
KW   Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat;
KW   Secreted; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           2..346
FT                   /note="Annexin A1"
FT                   /id="PRO_0000067464"
FT   PEPTIDE         2..26
FT                   /note="Annexin Ac2-26"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT                   /id="PRO_0000454562"
FT   REPEAT          42..113
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          114..185
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          197..269
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          273..344
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         129
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         171
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         261
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         286
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         290
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         328
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         331
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   SITE            26..27
FT                   /note="Cleavage; by CTSG"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.5"
FT   MOD_RES         5
FT                   /note="Phosphoserine; by TRPM7"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         21
FT                   /note="Phosphotyrosine; by EGFR"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         27
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         58
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10107"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   MOD_RES         312
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   DISULFID        324..343
FT                   /evidence="ECO:0000250|UniProtKB:P19619"
FT   CROSSLNK        19
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-?)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        214
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   CROSSLNK        214
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   CROSSLNK        257
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P10107"
FT   CROSSLNK        332
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P04083"
FT   CONFLICT        322
FT                   /note="P -> S (in Ref. 3; AAB19866)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  38829 MW;  F046E5F410AF2CF5 CRC64;
     MAMVSEFLKQ ACYIEKQEQE YVQAVKSYKG GPGSAVSPYP SFNPSSDVAA LHKAIMVKGV
     DEATIIDILT KRTNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA MLKTPAQFDA
     DELRAAMKGL GTDEDTLIEI LTTRSNQQIR EITRVYREEL KRDLAKDITS DTSGDFRNAL
     LALAKGDRCE DMSVNQDLAD TDARALYEAG ERRKGTDVNV FNTILTTRSY PHLRKVFQNY
     RKYSQHDMNK ALDLELKGDI EKCLTTIVKC ATSTPAFFAE KLYEAMKGAG TRHKTLIRIM
     VSRSEIDMNE IKVFYQKKYG IPLCQAILDE TKGDYEKILV ALCGGN
 
 
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