ANXA1_BOVIN
ID ANXA1_BOVIN Reviewed; 346 AA.
AC P46193; Q3ZBF5; Q58DU6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Annexin A1;
DE AltName: Full=Annexin I;
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;
DE Contains:
DE RecName: Full=Annexin Ac2-26 {ECO:0000250|UniProtKB:P04083};
GN Name=ANXA1; Synonyms=ANX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=7678738; DOI=10.1042/bj2890539;
RA Ernst J.D.;
RT "Epitope mapping of annexin I: antibodies that compete with phospholipids
RT and calcium recognize amino acids 42-99.";
RL Biochem. J. 289:539-542(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25827591; DOI=10.1186/s13567-014-0134-3;
RA Senthilkumaran C., Hewson J., Ollivett T.L., Bienzle D., Lillie B.N.,
RA Clark M., Caswell J.L.;
RT "Localization of annexins A1 and A2 in the respiratory tract of healthy
RT calves and those experimentally infected with Mannheimia haemolytica.";
RL Vet. Res. 46:6-6(2015).
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 (By similarity). 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}.
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:0000250|UniProtKB:P07150}. Cytoplasm
CC {ECO:0000269|PubMed:25827591}. Cell projection, cilium
CC {ECO:0000269|PubMed:25827591}. 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
CC {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10107}. Endosome membrane
CC {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein
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}. 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 (By similarity).
CC {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107}.
CC -!- TISSUE SPECIFICITY: Detected on surface epithelia and mucosal glands in
CC nasal cavity, trachea, bronchi and bronchioles. Detected in blood
CC vessel endothelial cells. Detected in neutrophils (at protein level).
CC {ECO:0000269|PubMed:25827591}.
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; X56649; CAA39971.1; -; mRNA.
DR EMBL; BT021501; AAX46348.1; -; mRNA.
DR EMBL; BC103375; AAI03376.1; -; mRNA.
DR PIR; S28228; S28228.
DR RefSeq; NP_786978.2; NM_175784.3.
DR AlphaFoldDB; P46193; -.
DR SMR; P46193; -.
DR IntAct; P46193; 1.
DR STRING; 9913.ENSBTAP00000021256; -.
DR ChEMBL; CHEMBL3308971; -.
DR iPTMnet; P46193; -.
DR PaxDb; P46193; -.
DR PeptideAtlas; P46193; -.
DR PRIDE; P46193; -.
DR GeneID; 327662; -.
DR KEGG; bta:327662; -.
DR CTD; 301; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P46193; -.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000009136; 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:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0031901; C:early endosome membrane; ISS: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; ISS: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:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
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; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:AgBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0031018; P:endocrine pancreas development; IBA:GO_Central.
DR GO; GO:0044849; P:estrous cycle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0070365; P:hepatocyte differentiation; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IBA:GO_Central.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IBA:GO_Central.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IBA:GO_Central.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0070459; P:prolactin secretion; IBA:GO_Central.
DR GO; GO:0030850; P:prostate gland development; IBA:GO_Central.
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:0032355; P:response to estradiol; IBA:GO_Central.
DR GO; GO:0070555; P:response to interleukin-1; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR GO; GO:0010165; P:response to X-ray; IBA:GO_Central.
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; Disulfide bond; Endosome; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Membrane;
KW Metal-binding; Nucleus; Phospholipase A2 inhibitor; Phosphoprotein;
KW Reference proteome; Repeat; 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_0000067457"
FT PEPTIDE 2..26
FT /note="Annexin Ac2-26"
FT /evidence="ECO:0000250|UniProtKB:P04083"
FT /id="PRO_0000454553"
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: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: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 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: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 58
FT /note="K -> R (in Ref. 2; AAX46348)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Y -> H (in Ref. 1; CAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> A (in Ref. 1; CAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="I -> T (in Ref. 1; CAA39971)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="T -> I (in Ref. 2; AAX46348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38952 MW; 09FA6CEF5F1AD9FB CRC64;
MAMVSEFLKQ AWFIENEEQE YIKTVKGSKG GPGSAVSPYP TFNPSSDVEA LHKAITVKGV
DEATIIEILT KRNNAQRQQI KAAYLQEKGK PLDEVLKKAL LGHLEEVVLA LLKTPAQFDA
EELRAAMKGL GTDEDTLNEI LASRTNREIR EINRVYREEL KRDLAKDIAS DTSGDYEKAL
LSLAKGDRSE ELAVNDDLAD SDARALYEAG ERRKGTDVNV FITILTTRSY PHLRRVFQKY
SKYSKHDMNK VLDLELKGDI EKCLTVIVKC ATSQPMFFAE KLHQAMKGIG TRHKTLIRIM
VSRSEIDMND IKACYQKLYG ISLCQAILDE TKGDYEKILV ALCGRD
