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IFNK_HUMAN
ID   IFNK_HUMAN              Reviewed;         207 AA.
AC   Q9P0W0; Q5T166;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Interferon kappa;
DE            Short=IFN-kappa;
DE   Flags: Precursor;
GN   Name=IFNK; ORFNames=UNQ6124/PRO20084;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-133.
RA   Cao X., Zhang W.;
RT   "Novel human interferon.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INDUCTION, TISSUE
RP   SPECIFICITY, AND VARIANT GLU-133.
RX   PubMed=11514542; DOI=10.1074/jbc.m102502200;
RA   LaFleur D.W., Nardelli B., Tsareva T., Mather D., Feng P., Semenuk M.,
RA   Taylor K., Buergin M., Chinchilla D., Roshke V., Chen G., Ruben S.M.,
RA   Pitha P.M., Coleman T.A., Moore P.A.;
RT   "Interferon-kappa, a novel type I interferon expressed in human
RT   keratinocytes.";
RL   J. Biol. Chem. 276:39765-39771(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-133.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 28-42.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12391192; DOI=10.4049/jimmunol.169.9.4822;
RA   Nardelli B., Zaritskaya L., Semenuk M., Cho Y.H., LaFleur D.W., Shah D.,
RA   Ullrich S., Girolomoni G., Albanesi C., Moore P.A.;
RT   "Regulatory effect of IFN-kappa, a novel type I IFN, on cytokine production
RT   by cells of the innate immune system.";
RL   J. Immunol. 169:4822-4830(2002).
CC   -!- FUNCTION: May play a role in the regulation of immune cell function.
CC       Cytokine that imparts cellular protection against viral infection in a
CC       species-specific manner. Activates the interferon-stimulated response
CC       element signaling pathway. It is able to directly modulate cytokine
CC       release from monocytes and dendritic cells. Binds heparin.
CC       {ECO:0000269|PubMed:11514542, ECO:0000269|PubMed:12391192}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in keratinocytes, monocytes and in
CC       resting dendritic cells. {ECO:0000269|PubMed:11514542,
CC       ECO:0000269|PubMed:12391192}.
CC   -!- INDUCTION: By viral infection, upon exposure to double-stranded RNA, or
CC       upon treatment with either interferon-gamma or interferon-beta.
CC       {ECO:0000269|PubMed:11514542}.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR   EMBL; AF146759; AAF67468.1; -; mRNA.
DR   EMBL; AF315688; AAK01623.1; -; mRNA.
DR   EMBL; AF384048; AAK63835.1; -; Genomic_DNA.
DR   EMBL; AY358855; AAQ89214.1; -; mRNA.
DR   EMBL; AL451123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS6521.1; -.
DR   RefSeq; NP_064509.2; NM_020124.2.
DR   AlphaFoldDB; Q9P0W0; -.
DR   SMR; Q9P0W0; -.
DR   BioGRID; 121205; 47.
DR   ComplexPortal; CPX-6009; Interferon kappa receptor-ligand complex.
DR   STRING; 9606.ENSP00000276943; -.
DR   iPTMnet; Q9P0W0; -.
DR   PhosphoSitePlus; Q9P0W0; -.
DR   BioMuta; IFNK; -.
DR   DMDM; 317373367; -.
DR   EPD; Q9P0W0; -.
DR   MassIVE; Q9P0W0; -.
DR   PaxDb; Q9P0W0; -.
DR   PeptideAtlas; Q9P0W0; -.
DR   PRIDE; Q9P0W0; -.
DR   ProteomicsDB; 83609; -.
DR   Antibodypedia; 25005; 91 antibodies from 18 providers.
DR   DNASU; 56832; -.
DR   Ensembl; ENST00000276943.3; ENSP00000276943.2; ENSG00000147896.4.
DR   GeneID; 56832; -.
DR   KEGG; hsa:56832; -.
DR   MANE-Select; ENST00000276943.3; ENSP00000276943.2; NM_020124.3; NP_064509.2.
DR   UCSC; uc003zqp.3; human.
DR   CTD; 56832; -.
DR   DisGeNET; 56832; -.
DR   GeneCards; IFNK; -.
DR   HGNC; HGNC:21714; IFNK.
DR   HPA; ENSG00000147896; Group enriched (brain, choroid plexus).
DR   MIM; 615326; gene.
DR   neXtProt; NX_Q9P0W0; -.
DR   OpenTargets; ENSG00000147896; -.
DR   PharmGKB; PA134970126; -.
DR   VEuPathDB; HostDB:ENSG00000147896; -.
DR   eggNOG; ENOG502SQGR; Eukaryota.
DR   GeneTree; ENSGT01000000214430; -.
DR   HOGENOM; CLU_109427_1_0_1; -.
DR   InParanoid; Q9P0W0; -.
DR   OMA; NSFPVEC; -.
DR   OrthoDB; 1358010at2759; -.
DR   PhylomeDB; Q9P0W0; -.
DR   TreeFam; TF336177; -.
DR   PathwayCommons; Q9P0W0; -.
DR   SignaLink; Q9P0W0; -.
DR   BioGRID-ORCS; 56832; 5 hits in 1024 CRISPR screens.
DR   GeneWiki; IFNK; -.
DR   GenomeRNAi; 56832; -.
DR   Pharos; Q9P0W0; Tbio.
DR   PRO; PR:Q9P0W0; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9P0W0; protein.
DR   Bgee; ENSG00000147896; Expressed in calcaneal tendon and 32 other tissues.
DR   Genevisible; Q9P0W0; HS.
DR   GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005132; F:type I interferon receptor binding; IDA:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR   GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
DR   GO; GO:0098586; P:cellular response to virus; IC:ComplexPortal.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR   GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
DR   GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; NAS:UniProtKB.
DR   GO; GO:0045089; P:positive regulation of innate immune response; TAS:UniProtKB.
DR   GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central.
DR   GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
DR   GO; GO:0060337; P:type I interferon signaling pathway; IC:ComplexPortal.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR000471; Interferon_alpha/beta/delta.
DR   PANTHER; PTHR11691; PTHR11691; 1.
DR   Pfam; PF00143; Interferon; 1.
DR   PRINTS; PR00266; INTERFERONAB.
DR   SMART; SM00076; IFabd; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00252; INTERFERON_A_B_D; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Coiled coil; Cytokine; Direct protein sequencing;
KW   Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           28..207
FT                   /note="Interferon kappa"
FT                   /id="PRO_0000016410"
FT   COILED          118..148
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..181
FT                   /evidence="ECO:0000250"
FT   VARIANT         97
FT                   /note="I -> N (in dbSNP:rs34933275)"
FT                   /id="VAR_032710"
FT   VARIANT         133
FT                   /note="K -> E (in dbSNP:rs700785)"
FT                   /evidence="ECO:0000269|PubMed:11514542,
FT                   ECO:0000269|PubMed:12975309, ECO:0000269|Ref.1"
FT                   /id="VAR_021303"
SQ   SEQUENCE   207 AA;  25218 MW;  49CF4CB5785F0E21 CRC64;
     MSTKPDMIQK CLWLEILMGI FIAGTLSLDC NLLNVHLRRV TWQNLRHLSS MSNSFPVECL
     RENIAFELPQ EFLQYTQPMK RDIKKAFYEM SLQAFNIFSQ HTFKYWKERH LKQIQIGLDQ
     QAEYLNQCLE EDKNENEDMK EMKENEMKPS EARVPQLSSL ELRRYFHRID NFLKEKKYSD
     CAWEIVRVEI RRCLYYFYKF TALFRRK
 
 
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