ANXA1_PIG
ID ANXA1_PIG Reviewed; 346 AA.
AC P19619; Q29547;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Annexin A1;
DE AltName: Full=Annexin I {ECO:0000303|PubMed:8885232};
DE AltName: Full=Annexin-1;
DE AltName: Full=Calpactin II;
DE AltName: Full=Calpactin-2;
DE AltName: Full=Chromobindin-9;
DE AltName: Full=Lipocortin I;
DE AltName: Full=Phospholipase A2 inhibitory protein;
DE AltName: Full=p35 {ECO:0000303|PubMed:3020049};
DE Contains:
DE RecName: Full=Annexin Ac2-26 {ECO:0000250|UniProtKB:P04083};
GN Name=ANXA1; Synonyms=ANX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-346, PROTEIN SEQUENCE OF 30-35 AND 214-219,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Lung;
RX PubMed=8885232; DOI=10.1091/mbc.7.9.1359;
RA Seemann J., Weber K., Osborn M., Parton R.G., Gerke V.;
RT "The association of annexin I with early endosomes is regulated by Ca2+ and
RT requires an intact N-terminal domain.";
RL Mol. Biol. Cell 7:1359-1374(1996).
RN [2]
RP PROTEIN SEQUENCE OF 13-42, PHOSPHORYLATION AT TYR-21 BY EGFR, AND TISSUE
RP SPECIFICITY.
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 [3]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-171.
RX PubMed=11058080; DOI=10.1242/jcs.113.22.3931;
RA Rescher U., Zobiack N., Gerke V.;
RT "Intact Ca(2+)-binding sites are required for targeting of annexin 1 to
RT endosomal membranes in living HeLa cells.";
RL J. Cell Sci. 113:3931-3938(2000).
RN [4]
RP INTERACTION WITH EGFR, AND SUBCELLULAR LOCATION.
RX PubMed=15581623; DOI=10.1016/j.febslet.2004.10.078;
RA Radke S., Austermann J., Russo-Marie F., Gerke V., Rescher U.;
RT "Specific association of annexin 1 with plasma membrane-resident and
RT internalized EGF receptors mediated through the protein core domain.";
RL FEBS Lett. 578:95-98(2004).
RN [5]
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 [6] {ECO:0007744|PDB:1HM6}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=11178908; DOI=10.1006/jmbi.2000.4423;
RA Rosengarth A., Gerke V., Luecke H.;
RT "X-ray structure of full-length annexin 1 and implications for membrane
RT aggregation.";
RL J. Mol. Biol. 306:489-498(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH CALCIUM, DISULFIDE
RP BONDS, DOMAIN, AND SUBUNIT.
RX PubMed=12595246; DOI=10.1016/s0022-2836(03)00027-5;
RA Rosengarth A., Luecke H.;
RT "A calcium-driven conformational switch of the N-terminal and core domains
RT of annexin A1.";
RL J. Mol. Biol. 326:1317-1325(2003).
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 (PubMed:12595246). Displays Ca(2+)-
CC dependent binding to phospholipid membranes (PubMed:8885232). 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:0000269|PubMed:12595246, ECO:0000269|PubMed:8885232}.
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm
CC {ECO:0000269|PubMed:11058080, ECO:0000269|PubMed:15581623}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:P10107}. Early endosome
CC {ECO:0000269|PubMed:11058080, ECO:0000269|PubMed:8885232}. Cell
CC membrane {ECO:0000269|PubMed:15581623, ECO:0000269|PubMed:3020049};
CC Peripheral membrane protein {ECO:0000269|PubMed:3020049}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:11058080,
CC ECO:0000269|PubMed:15581623}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P10107}. Membrane
CC {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10107}. Endosome
CC {ECO:0000250|UniProtKB:P07150}. Secreted
CC {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P04083}. Cell membrane
CC {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P04083}; Extracellular side
CC {ECO:0000250|UniProtKB:P04083}. 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 lung and spleen (at protein level).
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:0000269|PubMed:12595246}.
CC -!- PTM: Phosphorylated by EGFR (PubMed:3020049). Phosphorylated by protein
CC kinase C and TRPM7 (By similarity). Phosphorylated in response to EGF
CC treatment (PubMed:3020049). {ECO:0000250|UniProtKB:P04083,
CC ECO:0000269|PubMed:3020049}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; X95108; CAA64477.1; -; mRNA.
DR RefSeq; NP_001157470.1; NM_001163998.1.
DR PDB; 1HM6; X-ray; 1.80 A; A/B=1-346.
DR PDB; 1MCX; X-ray; 2.03 A; A=1-346.
DR PDBsum; 1HM6; -.
DR PDBsum; 1MCX; -.
DR AlphaFoldDB; P19619; -.
DR SMR; P19619; -.
DR STRING; 9823.ENSSSCP00000005658; -.
DR iPTMnet; P19619; -.
DR PaxDb; P19619; -.
DR PeptideAtlas; P19619; -.
DR PRIDE; P19619; -.
DR GeneID; 396942; -.
DR KEGG; ssc:396942; -.
DR CTD; 301; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P19619; -.
DR OrthoDB; 856254at2759; -.
DR EvolutionaryTrace; P19619; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IDA:UniProtKB.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISS:UniProtKB.
DR GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
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:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
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:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
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 DisProt; DP01963; -.
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; 3.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; 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:0000250|UniProtKB:P04083"
FT CHAIN 2..346
FT /note="Annexin A1"
FT /id="PRO_0000067462"
FT PEPTIDE 2..26
FT /note="Annexin Ac2-26"
FT /evidence="ECO:0000250|UniProtKB:P04083"
FT /id="PRO_0000454559"
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 REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:1MCX"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:1MCX"
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:0000250|UniProtKB:P04083"
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:0000269|PubMed:3020049"
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 41
FT /note="Phosphothreonine"
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 239
FT /note="N6-acetyllysine"
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:0007744|PDB:1HM6, ECO:0007744|PDB:1MCX"
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 MUTAGEN 171
FT /note="D->A: Abolishes calcium-dependent interaction with
FT membranes."
FT /evidence="ECO:0000269|PubMed:11058080"
FT CONFLICT 41
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1HM6"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:1HM6"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1HM6"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:1MCX"
FT HELIX 258..272
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:1HM6"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:1HM6"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:1HM6"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:1HM6"
SQ SEQUENCE 346 AA; 38759 MW; 925845C5DEBCBAB2 CRC64;
MAMVSEFLKQ AWFIDNEEQE YIKTVKGSKG GPGSAVSPYP TFNPSSDVEA SHKAITVKGV
DEATIIEIHT KRTNAQRQQI KAAYLQEKGK PLDEALKKAL TGHLEEVALA LLKTPAQFDA
DELRAAMKGL GTDEDTLNEI LASRTNREIR EINRVYKEEL KRDLAKDITS DTSGDYQKAL
LSLAKGDRSE DLAINDDLAD TDARALYEAG ERRKGTDLNV FITILTTRSY LHLRRVFQKY
SKYSKHDMNK VLDLELKGDI ENCLTVVVKC ATSKPMFFAE KLHQAMKGNG TRHKTLIRIM
VSRSEIDMND IKACYQKLYG ISLCQAILDE TKGDYEKILV ALCGGD
