ID   IL1A_CAVPO              Reviewed;         204 AA.
AC   Q60480;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Interleukin-1 alpha;
DE            Short=IL-1 alpha;
DE   Flags: Precursor; Fragment;
GN   Name=IL1A;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Lung;
RA   Yuan H.T., Kelly F.J., Bingle C.D.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produced by activated macrophages, IL-1 stimulates thymocyte
CC       proliferation by inducing IL-2 release, B-cell maturation and
CC       proliferation, and fibroblast growth factor activity. IL-1 proteins are
CC       involved in the inflammatory response, being identified as endogenous
CC       pyrogens, and are reported to stimulate the release of prostaglandin
CC       and collagenase from synovial cells (By similarity). {ECO:0000250}.
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.
CC       {ECO:0000250|UniProtKB:P01583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P01583}.
CC       Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific
CC       hydrophobic segment in the precursor sequence suggests that IL-1 is
CC       released by damaged cells or is secreted by a mechanism differing from
CC       that used for other secretory proteins. The secretion is dependent on
CC       protein unfolding and facilitated by the cargo receptor TMED10; it
CC       results in protein translocation from the cytoplasm into the ERGIC
CC       (endoplasmic reticulum-Golgi intermediate compartment) followed by
CC       vesicle entry and secretion. {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   -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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DR   EMBL; U46778; AAA87591.1; -; mRNA.
DR   AlphaFoldDB; Q60480; -.
DR   SMR; Q60480; -.
DR   STRING; 10141.ENSCPOP00000016482; -.
DR   eggNOG; ENOG502T3DD; Eukaryota.
DR   InParanoid; Q60480; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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:0001819; P:positive regulation of cytokine production; IEA:UniProt.
DR   GO; GO:0046688; P:response to copper ion; ISS:UniProtKB.
DR   InterPro; IPR003295; IL-1_alpha.
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; PR01358; INTRLEUKIN1A.
DR   SUPFAM; SSF50353; SSF50353; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Cytoplasm; Glycoprotein; Inflammatory response; Mitogen;
KW   Phosphoprotein; Pyrogen; Reference proteome; Secreted.
FT   PROPEP          <1..110
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015257"
FT   CHAIN           111..>204
FT                   /note="Interleukin-1 alpha"
FT                   /id="PRO_0000015258"
FT   REGION          34..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01582"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         204
SQ   SEQUENCE   204 AA;  23333 MW;  6AA25A71D90B7E9C CRC64;
     FEDLKNCYSE NEEYASAIDH LSLNQKSFYD TNYDPLHENR VDEPVSPNPY ENSEESNFTL
     EDSSDSSAVV LTSAHGEVLK KRRLSLNQTM SNEDLEAIAN DSEEEIIEPW SVPYSFQSNL
     KFKYQRSIKK GAVITDAMHQ SLIRESNGQH LKAMHVVDRK HEVKFDIDGY VSTATRIRPV
     TLKISKTQLY VCAQEEGQPV LLKE