I27L1_HUMAN
ID I27L1_HUMAN Reviewed; 104 AA.
AC Q96BM0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Interferon alpha-inducible protein 27-like protein 1 {ECO:0000305};
DE AltName: Full=Interferon-stimulated gene 12c protein {ECO:0000303|PubMed:14728724};
DE Short=ISG12(c) {ECO:0000303|PubMed:14728724};
DE Short=ISG12C {ECO:0000303|PubMed:27673746};
GN Name=IFI27L1 {ECO:0000312|HGNC:HGNC:19754};
GN Synonyms=FAM14B {ECO:0000312|HGNC:HGNC:19754};
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 [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION, AND INDUCTION BY INTERFERON.
RX PubMed=14728724; DOI=10.1186/1471-2164-5-8;
RA Parker N., Porter A.C.G.;
RT "Identification of a novel gene family that includes the interferon-
RT inducible human genes 6-16 and ISG12.";
RL BMC Genomics 5:8-8(2004).
RN [3]
RP FUNCTION.
RX PubMed=27673746; DOI=10.1111/boc.201600034;
RA Gytz H., Hansen M.F., Skovbjerg S., Kristensen A.C., Hoerlyck S.,
RA Jensen M.B., Fredborg M., Markert L.D., McMillan N.A., Christensen E.I.,
RA Martensen P.M.;
RT "Apoptotic properties of the type 1 interferon induced family of human
RT mitochondrial membrane ISG12 proteins.";
RL Biol. Cell 109:94-112(2017).
RN [4]
RP INDUCTION BY INTERFERON.
RX PubMed=27777077; DOI=10.1016/j.virusres.2016.10.013;
RA Chen Y., Jiao B., Yao M., Shi X., Zheng Z., Li S., Chen L.;
RT "ISG12a inhibits HCV replication and potentiates the anti-HCV activity of
RT IFN-alpha through activation of the Jak/STAT signaling pathway independent
RT of autophagy and apoptosis.";
RL Virus Res. 227:231-239(2017).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=22609626; DOI=10.1038/nmeth.2033;
RA Klammt C., Maslennikov I., Bayrhuber M., Eichmann C., Vajpai N., Chiu E.J.,
RA Blain K.Y., Esquivies L., Kwon J.H., Balana B., Pieper U., Sali A.,
RA Slesinger P.A., Kwiatkowski W., Riek R., Choe S.;
RT "Facile backbone structure determination of human membrane proteins by NMR
RT spectroscopy.";
RL Nat. Methods 9:834-839(2012).
CC -!- FUNCTION: Plays a role in the apoptotic process and has a pro-apoptotic
CC activity. {ECO:0000269|PubMed:27673746}.
CC -!- INTERACTION:
CC Q96BM0; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-17589287, EBI-17589229;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Not up-regulated by type-I interferon.
CC {ECO:0000269|PubMed:14728724, ECO:0000269|PubMed:27777077}.
CC -!- SIMILARITY: Belongs to the IFI6/IFI27 family. {ECO:0000305}.
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DR EMBL; BC015423; AAH15423.1; -; mRNA.
DR EMBL; BN000225; CAE00392.1; -; mRNA.
DR CCDS; CCDS9919.1; -.
DR RefSeq; NP_660292.1; NM_145249.2.
DR RefSeq; NP_996832.1; NM_206949.2.
DR RefSeq; XP_011534707.1; XM_011536405.2.
DR PDB; 2LOQ; NMR; -; A=1-104.
DR PDBsum; 2LOQ; -.
DR AlphaFoldDB; Q96BM0; -.
DR BMRB; Q96BM0; -.
DR SMR; Q96BM0; -.
DR BioGRID; 125774; 64.
DR IntAct; Q96BM0; 1.
DR STRING; 9606.ENSP00000451851; -.
DR iPTMnet; Q96BM0; -.
DR PhosphoSitePlus; Q96BM0; -.
DR BioMuta; IFI27L1; -.
DR DMDM; 27805467; -.
DR PaxDb; Q96BM0; -.
DR PeptideAtlas; Q96BM0; -.
DR PRIDE; Q96BM0; -.
DR DNASU; 122509; -.
DR Ensembl; ENST00000393115.7; ENSP00000376824.3; ENSG00000165948.11.
DR Ensembl; ENST00000555523.6; ENSP00000451851.1; ENSG00000165948.11.
DR Ensembl; ENST00000611681.3; ENSP00000480235.1; ENSG00000276880.3.
DR Ensembl; ENST00000629591.2; ENSP00000485930.1; ENSG00000276880.3.
DR GeneID; 122509; -.
DR KEGG; hsa:122509; -.
DR MANE-Select; ENST00000555523.6; ENSP00000451851.1; NM_206949.3; NP_996832.1.
DR UCSC; uc001yck.4; human.
DR CTD; 122509; -.
DR GeneCards; IFI27L1; -.
DR HGNC; HGNC:19754; IFI27L1.
DR HPA; ENSG00000165948; Tissue enhanced (testis).
DR MIM; 611320; gene.
DR neXtProt; NX_Q96BM0; -.
DR OpenTargets; ENSG00000165948; -.
DR PharmGKB; PA164720846; -.
DR VEuPathDB; HostDB:ENSG00000165948; -.
DR eggNOG; ENOG502S85T; Eukaryota.
DR GeneTree; ENSGT00940000165490; -.
DR HOGENOM; CLU_142338_4_0_1; -.
DR InParanoid; Q96BM0; -.
DR OMA; GMACKAL; -.
DR OrthoDB; 1640493at2759; -.
DR PhylomeDB; Q96BM0; -.
DR TreeFam; TF340510; -.
DR PathwayCommons; Q96BM0; -.
DR SignaLink; Q96BM0; -.
DR BioGRID-ORCS; 122509; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; IFI27L1; human.
DR GenomeRNAi; 122509; -.
DR Pharos; Q96BM0; Tdark.
DR PRO; PR:Q96BM0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96BM0; protein.
DR Bgee; ENSG00000165948; Expressed in right testis and 92 other tissues.
DR ExpressionAtlas; Q96BM0; baseline and differential.
DR Genevisible; Q96BM0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
DR Gene3D; 6.10.110.10; -; 1.
DR InterPro; IPR009311; IFI6/IFI27-like.
DR InterPro; IPR038213; IFI6/IFI27-like_sf.
DR PANTHER; PTHR16932; PTHR16932; 1.
DR Pfam; PF06140; Ifi-6-16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..104
FT /note="Interferon alpha-inducible protein 27-like protein
FT 1"
FT /id="PRO_0000147371"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 35
FT /note="G -> S (in dbSNP:rs57677258)"
FT /id="VAR_062245"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:2LOQ"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2LOQ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2LOQ"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2LOQ"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2LOQ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2LOQ"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:2LOQ"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2LOQ"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2LOQ"
SQ SEQUENCE 104 AA; 9549 MW; C54AF9381B74A236 CRC64;
MGKESGWDSG RAAVAAVVGG VVAVGTVLVA LSAMGFTSVG IAASSIAAKM MSTAAIANGG
GVAAGSLVAI LQSVGAAGLS VTSKVIGGFA GTALGAWLGS PPSS
