IL1A_BUBCA
ID IL1A_BUBCA Reviewed; 268 AA.
AC Q3HWU1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Interleukin-1 alpha;
DE Short=IL-1 alpha;
DE Flags: Precursor;
GN Name=IL1A;
OS Bubalus carabanensis (Swamp type water buffalo) (Bubalus bubalis
OS carabanensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=346063;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mingala C.N., Raadan O., Konnai S., Ohashi K., Onuma M.;
RT "Comparative immunological analysis of bubaline species through cytokine
RT cloning and nucleotide sequencing.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytokine constitutively present intracellularly in nearly all
CC resting non-hematopoietic cells that plays an important role in
CC inflammation and bridges the innate and adaptive immune systems. After
CC binding to its receptor IL1R1 together with its accessory protein
CC IL1RAP, forms the high affinity interleukin-1 receptor complex.
CC Signaling involves the recruitment of adapter molecules such as MYD88,
CC IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the
CC three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell,
CC acts as an alarmin and cell death results in its liberation in the
CC extracellular space after disruption of the cell membrane to induce
CC inflammation and alert the host to injury or damage. In addition to its
CC role as a danger signal, which occurs when the cytokine is passively
CC released by cell necrosis, directly senses DNA damage and acts as
CC signal for genotoxic stress without loss of cell integrity.
CC {ECO:0000250|UniProtKB:P01583}.
CC -!- SUBUNIT: Monomer. Interacts with TMED10; the interaction mediates the
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and thereby secretion. Interacts with
CC IL1R1. Interacts with S100A13; this interaction is the first step in
CC the export of IL1A, followed by direct translocation of this complex
CC across the plasma membrane. {ECO:0000250|UniProtKB:P01583}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm
CC {ECO:0000250|UniProtKB:P01583}. Secreted
CC {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic
CC segment in the precursor sequence suggests that IL-1 is released by
CC damaged cells or is secreted by a mechanism differing from that used
CC for other secretory proteins. The secretion is dependent on protein
CC unfolding and facilitated by the cargo receptor TMED10; it results in
CC protein translocation from the cytoplasm into the ERGIC (endoplasmic
CC reticulum-Golgi intermediate compartment) followed by vesicle entry and
CC secretion. Recruited to DNA damage sites and secreted after genotoxic
CC stress. {ECO:0000250|UniProtKB:P01583}.
CC -!- DOMAIN: The similarity among the IL-1 precursors suggests that the
CC amino ends of these proteins serve some as yet undefined function.
CC {ECO:0000250}.
CC -!- PTM: Acetylated within its nuclear localization sequence, which impacts
CC subcellular localization. {ECO:0000250|UniProtKB:P01583}.
CC -!- PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner.
CC Cleavage from 31 kDa precursor to 18 kDa biologically active molecules.
CC {ECO:0000250|UniProtKB:P01583}.
CC -!- PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to
CC digestion and promotes the conversion of pre-IL1A alpha to the
CC biologically active IL1A. {ECO:0000250|UniProtKB:P01583}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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DR EMBL; DQ188096; ABA33680.1; -; mRNA.
DR AlphaFoldDB; Q3HWU1; -.
DR SMR; Q3HWU1; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0046688; P:response to copper ion; ISS:UniProtKB.
DR InterPro; IPR003295; IL-1_alpha.
DR InterPro; IPR020877; IL-1_CS.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003502; IL-1_propep.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF33; PTHR10078:SF33; 1.
DR Pfam; PF00340; IL1; 1.
DR Pfam; PF02394; IL1_propep; 1.
DR PRINTS; PR00264; INTERLEUKIN1.
DR PRINTS; PR01358; INTRLEUKIN1A.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00253; INTERLEUKIN_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytokine; Cytoplasm; Glycoprotein; Inflammatory response;
KW Mitogen; Nucleus; Phosphoprotein; Pyrogen; Secreted.
FT PROPEP 1..112
FT /id="PRO_0000254876"
FT CHAIN 113..268
FT /note="Interleukin-1 alpha"
FT /id="PRO_0000254877"
FT REGION 82..86
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250|UniProtKB:P01583"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01583"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01582"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 268 AA; 30748 MW; BD7E805827FEAB62 CRC64;
MAKVPDLFED LKNCYSENED YSSEIDHLSL NQKSFYDASY EPLREDQMDK FMSLDTSETS
KTSRLSFKEN VVMVAASGKI LKKRRLSLNQ FITDDDLEAI ANNTEEEIIK PRSAHYSFQS
NVKYNLLRVI HQECILNDAL NQSLIRDLSG PYLTAATLNN LEEAVKFDMV AYVSEEDSQL
PVTLRISKTQ LFVSAQNEDE PVLLKEMPET PKIIKDETNL LFFWEKHGSM DYFKSVAHPK
LFIATKQEKL VHMASGPPSV TDFQILEK
