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IFNG_RABIT
ID   IFNG_RABIT              Reviewed;         167 AA.
AC   P30123; P79215; Q0PW35;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Interferon gamma;
DE            Short=IFN-gamma;
DE   Flags: Precursor;
GN   Name=IFNG;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B/Jas;
RA   Yuasa T., Isono T., Tambe Y.;
RT   "Rabbit interferon gamma.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymph node;
RA   Perkins H.D., Lei S., van Leeuwen B., Kerr P.J.;
RT   "Oryctolagus cuniculus gamma interferon mRNA, complete cds.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Chinese white;
RA   Qiao J., Meng Q., Cai X.;
RT   "Cloning and expression of IFN gamma gene of Chinese white rabbit.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang D., Yang G.;
RT   "Cloning and sequence analysis of IFN-gamma gene in rabbit.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 81-136.
RC   STRAIN=B/Jas;
RX   PubMed=8753862; DOI=10.1007/bf02602561;
RA   Isono T., Nagano Y., Seto A.;
RT   "Expression of the interferon-gamma and interleukin-10 genes in rabbit
RT   HTLV-I-transformed T-cell lines.";
RL   Immunogenetics 44:306-308(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=1939201; DOI=10.1016/s0021-9258(18)54706-2;
RA   Samudzi C.T., Burton L.E., Rubin J.R.;
RT   "Crystal structure of recombinant rabbit interferon-gamma at 2.7-A
RT   resolution.";
RL   J. Biol. Chem. 266:21791-21797(1991).
CC   -!- FUNCTION: Type II interferon produced by immune cells such as T-cells
CC       and NK cells that plays crucial roles in antimicrobial, antiviral, and
CC       antitumor responses by activating effector immune cells and enhancing
CC       antigen presentation. Primarily signals through the JAK-STAT pathway
CC       after interaction with its receptor IFNGR1 to affect gene regulation.
CC       Upon IFNG binding, IFNGR1 intracellular domain opens out to allow
CC       association of downstream signaling components JAK2, JAK1 and STAT1,
CC       leading to STAT1 activation, nuclear translocation and transcription of
CC       IFNG-regulated genes. Many of the induced genes are transcription
CC       factors such as IRF1 that are able to further drive regulation of a
CC       next wave of transcription. Plays a role in class I antigen
CC       presentation pathway by inducing a replacement of catalytic proteasome
CC       subunits with immunoproteasome subunits. In turn, increases the
CC       quantity, quality, and repertoire of peptides for class I MHC loading.
CC       Increases the efficiency of peptide generation also by inducing the
CC       expression of activator PA28 that associates with the proteasome and
CC       alters its proteolytic cleavage preference. Up-regulates as well MHC II
CC       complexes on the cell surface by promoting expression of several key
CC       molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By
CC       similarity). Participates in the regulation of hematopoietic stem cells
CC       during development and under homeostatic conditions by affecting their
CC       development, quiescence, and differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:P01579, ECO:0000250|UniProtKB:P01580}.
CC   -!- SUBUNIT: Homodimer. Interacts with IFNGR1 (via extracellular domain);
CC       this interaction promotes IFNGR1 dimerization.
CC       {ECO:0000250|UniProtKB:P01579}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}.
CC   -!- TISSUE SPECIFICITY: Released primarily from activated T lymphocytes.
CC   -!- SIMILARITY: Belongs to the type II (or gamma) interferon family.
CC       {ECO:0000305}.
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DR   EMBL; AB010386; BAA24439.1; -; mRNA.
DR   EMBL; AF244933; AAF64188.1; -; mRNA.
DR   EMBL; DQ680162; ABG73601.1; -; mRNA.
DR   EMBL; DQ852341; ABH10826.1; -; mRNA.
DR   EMBL; D84216; BAA20884.1; -; mRNA.
DR   RefSeq; NP_001075460.1; NM_001081991.1.
DR   PDB; 2RIG; X-ray; 2.30 A; A=24-167.
DR   PDBsum; 2RIG; -.
DR   AlphaFoldDB; P30123; -.
DR   SMR; P30123; -.
DR   STRING; 9986.ENSOCUP00000021866; -.
DR   Ensembl; ENSOCUT00000030109; ENSOCUP00000021866; ENSOCUG00000024937.
DR   GeneID; 100008602; -.
DR   KEGG; ocu:100008602; -.
DR   CTD; 3458; -.
DR   eggNOG; ENOG502SBGW; Eukaryota.
DR   GeneTree; ENSGT00390000007831; -.
DR   HOGENOM; CLU_135106_0_0_1; -.
DR   InParanoid; P30123; -.
DR   OMA; GGPIFTE; -.
DR   OrthoDB; 1382686at2759; -.
DR   TreeFam; TF336308; -.
DR   EvolutionaryTrace; P30123; -.
DR   Proteomes; UP000001811; Chromosome 4.
DR   Bgee; ENSOCUG00000024937; Expressed in blood and 2 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005133; F:interferon-gamma receptor binding; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR002069; Interferon_gamma.
DR   PANTHER; PTHR11419; PTHR11419; 1.
DR   Pfam; PF00714; IFN-gamma; 1.
DR   PIRSF; PIRSF001936; IFN-gamma; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Cytokine; Glycoprotein; Growth regulation;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..167
FT                   /note="Interferon gamma"
FT                   /id="PRO_0000016456"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P01579"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        123
FT                   /note="Missing (in Ref. 5; BAA20884)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   167 AA;  19516 MW;  96D1CAD2A5163850 CRC64;
     MSYTSYILAF QLCLILGSYG CYCQDTLTRE TEHLKAYLKA NTSDVANGGP LFLNILRNWK
     EESDNKIIQS QIVSFYFKLF DNLKDHEVIK KSMESIKEDI FVKFFNSNLT KMDDFQNLTR
     ISVDDRLVQR KAVSELSNVL NFLSPKSNLK KRKRSQTLFR GRRASKY
 
 
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