ID Q9TTK1_TURTR Unreviewed; 266 AA.
AC Q9TTK1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU003753, ECO:0000256|RuleBase:RU364119};
DE Includes:
DE RecName: Full=Interleukin-1 {ECO:0000256|RuleBase:RU003753};
DE Includes:
DE RecName: Full=Interleukin-1 beta {ECO:0000256|RuleBase:RU364119};
GN Name=IL1B {ECO:0000256|RuleBase:RU364119,
GN ECO:0000313|RefSeq:NP_001267581.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|EMBL:BAA87947.1};
RN [1] {ECO:0000313|EMBL:BAA87947.1}
RP NUCLEOTIDE SEQUENCE.
RA Inoue Y., Itou T., Sakai T.;
RT "Cloning and Sequencing of a Bottle-Nosed Dolphin Interleukin-1 beta.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_001267581.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the
CC major endogenous pyrogen, induces prostaglandin synthesis, neutrophil
CC influx and activation, T-cell activation and cytokine production, B-
CC cell activation and antibody production, and fibroblast proliferation
CC and collagen production. Promotes Th17 differentiation of T-cells.
CC Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-
CC helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF
CC production synergistically with TNF and IL6. Involved in transduction
CC of inflammation downstream of pyroptosis: its mature form is
CC specifically released in the extracellular milieu by passing through
CC the gasdermin-D (GSDMD) pore. {ECO:0000256|ARBA:ARBA00033717,
CC ECO:0000256|RuleBase:RU364119}.
CC -!- SUBUNIT: Monomer. In its precursor form, weakly interacts with full-
CC length MEFV; the mature cytokine does not interact at all. Interacts
CC with integrins ITGAV:ITGBV and ITGA5:ITGB1; integrin-binding is
CC required for IL1B signaling. Interacts with cargo receptor TMED10; the
CC interaction is direct and is required for the secretion of IL1B mature
CC form. Interacts with HSP90AB1; the interaction facilitates cargo
CC translocation into the ERGIC. Interacts with HSP90B1; the interaction
CC facilitates cargo translocation into the ERGIC.
CC {ECO:0000256|ARBA:ARBA00023613}.
CC -!- SUBUNIT: Monomer. Interacts with MEFV. {ECO:0000256|RuleBase:RU364119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU364119}. Secreted
CC {ECO:0000256|RuleBase:RU364119}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371, ECO:0000256|RuleBase:RU364119}.
CC Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550,
CC ECO:0000256|RuleBase:RU364119}. Note=The precursor is cytosolic. In
CC response to inflammasome-activating signals, such as ATP for NLRP3
CC inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and
CC secreted. Mature form is secreted and released in the extracellular
CC milieu by passing through the gasdermin-D (GSDMD) pore. In contrast,
CC the precursor form is not released, due to the presence of an acidic
CC region that is proteolytically removed by CASP1 during maturation. The
CC secretion is dependent on protein unfolding and facilitated by the
CC cargo receptor TMED10. {ECO:0000256|RuleBase:RU364119}.
CC -!- MISCELLANEOUS: IL1B production occurs in 2 steps, each being controlled
CC by different stimuli. First, inflammatory signals, such as LPS,
CC stimulate the synthesis and promote the accumulation of cytosolic
CC stores of pro-IL1B (priming). Then additional signals are required for
CC inflammasome assembly, leading to CASP1 activation, pro-IL1B processing
CC and eventually secretion of the active cytokine. IL1B processing and
CC secretion are temporarily associated. {ECO:0000256|RuleBase:RU364119}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000256|ARBA:ARBA00010448,
CC ECO:0000256|RuleBase:RU003753}.
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DR EMBL; AB028216; BAA87947.1; -; mRNA.
DR RefSeq; NP_001267581.1; NM_001280652.1.
DR RefSeq; XP_019786555.1; XM_019930996.1.
DR RefSeq; XP_019786556.1; XM_019930997.1.
DR STRING; 9739.ENSTTRP00000010490; -.
DR GeneID; 101318809; -.
DR OrthoDB; 4264279at2759; -.
DR Proteomes; UP000245320; Chromosome 14.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-UniRule.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR CDD; cd00100; IL1; 1.
DR Gene3D; 2.80.10.50; -; 1.
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:SF30; INTERLEUKIN-1 BETA; 1.
DR PANTHER; PTHR10078; INTERLEUKIN-1 FAMILY MEMBER; 1.
DR Pfam; PF00340; IL1; 1.
DR Pfam; PF02394; IL1_propep; 1.
DR PRINTS; PR00262; IL1HBGF.
DR PRINTS; PR00264; INTERLEUKIN1.
DR PRINTS; PR01359; INTRLEUKIN1B.
DR PRINTS; PR01357; INTRLEUKN1AB.
DR SMART; SM00125; IL1; 1.
DR SUPFAM; SSF50353; Cytokine; 1.
DR PROSITE; PS00253; INTERLEUKIN_1; 1.
PE 2: Evidence at transcript level;
KW Cytokine {ECO:0000256|ARBA:ARBA00022514, ECO:0000256|RuleBase:RU003753};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364119};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198,
KW ECO:0000256|RuleBase:RU003753};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228, ECO:0000256|RuleBase:RU364119};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246, ECO:0000256|RuleBase:RU003753};
KW Pyrogen {ECO:0000256|ARBA:ARBA00022620, ECO:0000256|RuleBase:RU003753};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Secreted {ECO:0000256|RuleBase:RU003753}.
FT DOMAIN 1..101
FT /note="Interleukin-1 propeptide"
FT /evidence="ECO:0000259|Pfam:PF02394"
SQ SEQUENCE 266 AA; 30347 MW; 95AAC10F2AA40F22 CRC64;
MATVPEPTNE VMAYYSDEND LLFEADGPKQ MKCCVQHLDL SSTGDESIHL QISHQLYNKS
FRHVVSVIVA VEKLQKIPCS QTFQDDGLRS IFSLIFEEEP VIFETYDDDL LCDAAVQSLT
CKLQDRDQKS LVLASPCVLK ALHLLARDMN REVVFCMSFV QGDESNDKIP VALGLKEKNL
YLSCVMKGDR PILQLEEVDP KTYPKWKMEK RFVFNKTEIK NSVEFESALY PNWYISTSQA
EEKPIFLGRS KGGHDITDFT MEIISP
//
