CXL10_HUMAN
ID CXL10_HUMAN Reviewed; 98 AA.
AC P02778; Q96QJ5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=C-X-C motif chemokine 10;
DE AltName: Full=10 kDa interferon gamma-induced protein;
DE Short=Gamma-IP10;
DE Short=IP-10;
DE AltName: Full=Small-inducible cytokine B10;
DE Contains:
DE RecName: Full=CXCL10(1-73);
DE Flags: Precursor;
GN Name=CXCL10; Synonyms=INP10, SCYB10;
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].
RX PubMed=3925348; DOI=10.1038/315672a0;
RA Luster A.D., Unkeless J.C., Ravetch J.V.;
RT "Gamma-interferon transcriptionally regulates an early-response gene
RT containing homology to platelet proteins.";
RL Nature 315:672-676(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP PROTEIN SEQUENCE OF 22-51.
RX PubMed=8423327;
RA Proost P., de Wolf-Peeters C., Conings R., Opdenakker G., Billiau A.,
RA van Damme J.;
RT "Identification of a novel granulocyte chemotactic protein (GCP-2) from
RT human tumor cells. In vitro and in vivo comparison with natural forms of
RT GRO, IP-10, and IL-8.";
RL J. Immunol. 150:1000-1010(1993).
RN [4]
RP FUNCTION.
RX PubMed=7540647; DOI=10.1084/jem.182.1.155;
RA Angiolillo A.L., Sgadari C., Taub D.D., Liao F., Farber J.M.,
RA Maheshwari S., Kleinman H.K., Reaman G.H., Tosato G.;
RT "Human interferon-inducible protein 10 is a potent inhibitor of
RT angiogenesis in vivo.";
RL J. Exp. Med. 182:155-162(1995).
RN [5]
RP FUNCTION.
RX PubMed=9064356; DOI=10.1084/jem.184.3.963;
RA Loetscher M., Gerber B., Loetscher P., Jones S.A., Piali L.,
RA Clark-Lewis I., Baggiolini M., Moser B.;
RT "Chemokine receptor specific for IP10 and mig: structure, function, and
RT expression in activated T-lymphocytes.";
RL J. Exp. Med. 184:963-969(1996).
RN [6]
RP PROTEIN SEQUENCE OF 22-29.
RC TISSUE=Keratinocyte;
RX PubMed=10233762; DOI=10.1046/j.1523-1747.1999.00581.x;
RA Tensen C.P., Flier J., van der Raaij-Helmer E.M.H.,
RA Sampat-Sardjoepersad S., van der Schors R.C., Leurs R., Scheper R.J.,
RA Boorsma D.M., Willemze R.;
RT "Human IP-9: a keratinocyte derived high affinity CXC-chemokine ligand for
RT the IP-10/Mig receptor (CXCR3).";
RL J. Invest. Dermatol. 112:716-722(1999).
RN [7]
RP PROTEIN SEQUENCE OF 22-27; 60-67 AND 79-98, MASS SPECTROMETRY, AND
RP IDENTIFICATION OF CXCL10(1-73).
RC TISSUE=Foreskin keratinocyte;
RX PubMed=11559369; DOI=10.1046/j.0014-2956.2001.02433.x;
RA Hensbergen P.J., van der Raaij-Helmer E.M.H., Dijkman R.,
RA van der Schors R.C., Werner-Felmayer G., Boorsma D.M., Scheper R.J.,
RA Willemze R., Tensen C.P.;
RT "Processing of natural and recombinant CXCR3-targeting chemokines and
RT implications for biological activity.";
RL Eur. J. Biochem. 268:4992-4999(2001).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11157474; DOI=10.1182/blood.v97.3.601;
RA Romagnani P., Annunziato F., Lazzeri E., Cosmi L., Beltrame C., Lasagni L.,
RA Galli G., Francalanci M., Manetti R., Marra F., Vanini V., Maggi E.,
RA Romagnani S.;
RT "Interferon-inducible protein 10, monokine induced by interferon gamma, and
RT interferon-inducible T-cell alpha chemoattractant are produced by thymic
RT epithelial cells and attract T-cell receptor (TCR) alphabeta+ CD8+ single-
RT positive T cells, TCRgammadelta+ T cells, and natural killer-type cells in
RT human thymus.";
RL Blood 97:601-607(2001).
RN [9]
RP FUNCTION.
RX PubMed=12750173; DOI=10.1182/blood-2002-12-3945;
RA Smit M.J., Verdijk P., van der Raaij-Helmer E.M., Navis M.,
RA Hensbergen P.J., Leurs R., Tensen C.P.;
RT "CXCR3-mediated chemotaxis of human T cells is regulated by a Gi- and
RT phospholipase C-dependent pathway and not via activation of MEK/p44/p42
RT MAPK nor Akt/PI-3 kinase.";
RL Blood 102:1959-1965(2003).
RN [10]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12663757; DOI=10.1128/jvi.77.8.4502-4515.2003;
RA Cheeran M.C., Hu S., Sheng W.S., Peterson P.K., Lokensgard J.R.;
RT "CXCL10 production from cytomegalovirus-stimulated microglia is regulated
RT by both human and viral interleukin-10.";
RL J. Virol. 77:4502-4515(2003).
RN [11]
RP CITRULLINATION AT ARG-26.
RX PubMed=18645041; DOI=10.1182/blood-2008-04-149039;
RA Loos T., Mortier A., Gouwy M., Ronsse I., Put W., Lenaerts J.P.,
RA Van Damme J., Proost P.;
RT "Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a
RT naturally occurring posttranslational modification of chemokines and new
RT dimension of immunoregulation.";
RL Blood 112:2648-2656(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH CXCR3.
RX PubMed=19151743; DOI=10.1038/aps.2008.24;
RA Gao J.M., Xiang R.L., Jiang L., Li W.H., Feng Q.P., Guo Z.J., Sun Q.,
RA Zeng Z.P., Fang F.D.;
RT "Sulfated tyrosines 27 and 29 in the N-terminus of human CXCR3 participate
RT in binding native IP-10.";
RL Acta Pharmacol. Sin. 30:193-201(2009).
RN [13]
RP SUBCELLULAR LOCATION, AND CLEAVAGE.
RX PubMed=21183794; DOI=10.1172/jci40594;
RA Casrouge A., Decalf J., Ahloulay M., Lababidi C., Mansour H.,
RA Vallet-Pichard A., Mallet V., Mottez E., Mapes J., Fontanet A., Pol S.,
RA Albert M.L.;
RT "Evidence for an antagonist form of the chemokine CXCL10 in patients
RT chronically infected with HCV.";
RL J. Clin. Invest. 121:308-317(2011).
RN [14]
RP FUNCTION.
RX PubMed=22652417; DOI=10.1016/j.cyto.2012.05.002;
RA Sidahmed A.M., Leon A.J., Bosinger S.E., Banner D., Danesh A.,
RA Cameron M.J., Kelvin D.J.;
RT "CXCL10 contributes to p38-mediated apoptosis in primary T lymphocytes in
RT vitro.";
RL Cytokine 59:433-441(2012).
RN [15]
RP STRUCTURE BY NMR OF 22-98, AND DISULFIDE BOND.
RX PubMed=12173928; DOI=10.1021/bi026020q;
RA Booth V., Keizer D.W., Kamphuis M.B., Clark-Lewis I., Sykes B.D.;
RT "The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor
RT interactions.";
RL Biochemistry 41:10418-10425(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS), DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=12737818; DOI=10.1016/s0969-2126(03)00070-4;
RA Swaminathan G.J., Holloway D.E., Colvin R.A., Campanella G.K.,
RA Papageorgiou A.C., Luster A.D., Acharya K.R.;
RT "Crystal structures of oligomeric forms of the IP-10/CXCL10 chemokine.";
RL Structure 11:521-532(2003).
CC -!- FUNCTION: Pro-inflammatory cytokine that is involved in a wide variety
CC of processes such as chemotaxis, differentiation, and activation of
CC peripheral immune cells, regulation of cell growth, apoptosis and
CC modulation of angiostatic effects (PubMed:7540647, PubMed:11157474,
CC PubMed:22652417). Plays thereby an important role during viral
CC infections by stimulating the activation and migration of immune cells
CC to the infected sites (By similarity). Mechanistically, binding of
CC CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and
CC results in downstream activation of phospholipase C-dependent pathway,
CC an increase in intracellular calcium production and actin
CC reorganization (PubMed:12750173, PubMed:19151743). In turn, recruitment
CC of activated Th1 lymphocytes occurs at sites of inflammation
CC (PubMed:12750173, PubMed:12663757). Activation of the CXCL10/CXCR3 axis
CC also plays an important role in neurons in response to brain injury for
CC activating microglia, the resident macrophage population of the central
CC nervous system, and directing them to the lesion site. This recruitment
CC is an essential element for neuronal reorganization (By similarity).
CC {ECO:0000250|UniProtKB:P17515, ECO:0000269|PubMed:11157474,
CC ECO:0000269|PubMed:12663757, ECO:0000269|PubMed:12750173,
CC ECO:0000269|PubMed:19151743, ECO:0000269|PubMed:22652417,
CC ECO:0000269|PubMed:7540647}.
CC -!- SUBUNIT: Monomer, dimer, and tetramer (PubMed:12737818). Interacts with
CC CXCR3 (via N-terminus) (PubMed:19151743). {ECO:0000269|PubMed:12737818,
CC ECO:0000269|PubMed:19151743}.
CC -!- INTERACTION:
CC P02778; P51671: CCL11; NbExp=2; IntAct=EBI-7815386, EBI-727357;
CC P02778; Q99616: CCL13; NbExp=2; IntAct=EBI-7815386, EBI-725342;
CC P02778; O00585: CCL21; NbExp=2; IntAct=EBI-7815386, EBI-953695;
CC P02778; Q9Y258: CCL26; NbExp=2; IntAct=EBI-7815386, EBI-7783416;
CC P02778; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-7815386, EBI-7783254;
CC P02778; P13501: CCL5; NbExp=2; IntAct=EBI-7815386, EBI-2848366;
CC P02778; P48061: CXCL12; NbExp=2; IntAct=EBI-7815386, EBI-3913254;
CC P02778; Q07325: CXCL9; NbExp=2; IntAct=EBI-7815386, EBI-3911467;
CC P02778; P27487: DPP4; NbExp=2; IntAct=EBI-7815386, EBI-2871277;
CC P02778; P02776: PF4; NbExp=2; IntAct=EBI-7815386, EBI-2565740;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21183794}.
CC -!- TISSUE SPECIFICITY: Mainly secreted by monocytes, endothelial cells as
CC well as fibroblasts. Expressed by epithelial cells in thymus
CC (PubMed:11157474). Microglial cells produce CXCL10 in response to viral
CC stimulation (PubMed:12663757). {ECO:0000269|PubMed:11157474,
CC ECO:0000269|PubMed:12663757}.
CC -!- INDUCTION: By IFNG/IFN-gamma. A diverse population of cell types
CC rapidly increases transcription of mRNA encoding this protein. This
CC suggests that gamma-induced protein may be a key mediator of the
CC IFNG/IFN-gamma response.
CC -!- PTM: Several proteases can mediate post-secretion cleavages. DPP4
CC cleaves CXCL10 on its N-terminal 2 amino acids leading to an antagonist
CC form of CXCL10. This dominant negative form is capable of binding CXCR3
CC but does not induce signaling. MMP9 cleaves 9 amino acids instead.
CC {ECO:0000269|PubMed:21183794}.
CC -!- MASS SPECTROMETRY: [C-X-C motif chemokine 10]: Mass=8641.8;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11559369};
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL10 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL10";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CXCL10ID40218ch4q21.html";
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DR EMBL; X02530; CAA26370.1; -; mRNA.
DR EMBL; BC010954; AAH10954.1; -; mRNA.
DR CCDS; CCDS43240.1; -.
DR PIR; A03243; TGHUGI.
DR RefSeq; NP_001556.2; NM_001565.3.
DR PDB; 1LV9; NMR; -; A=22-98.
DR PDB; 1O7Y; X-ray; 3.00 A; A/B/C/D=22-98.
DR PDB; 1O7Z; X-ray; 1.92 A; A/B=22-98.
DR PDB; 1O80; X-ray; 2.00 A; A/B=22-98.
DR PDBsum; 1LV9; -.
DR PDBsum; 1O7Y; -.
DR PDBsum; 1O7Z; -.
DR PDBsum; 1O80; -.
DR AlphaFoldDB; P02778; -.
DR SMR; P02778; -.
DR BioGRID; 109839; 20.
DR DIP; DIP-5893N; -.
DR IntAct; P02778; 19.
DR MINT; P02778; -.
DR STRING; 9606.ENSP00000305651; -.
DR BindingDB; P02778; -.
DR ChEMBL; CHEMBL3712964; -.
DR DrugBank; DB11338; Clove oil.
DR DrugBank; DB06116; Eldelumab.
DR DrugBank; DB04487; N-Methylleucine.
DR iPTMnet; P02778; -.
DR PhosphoSitePlus; P02778; -.
DR BioMuta; CXCL10; -.
DR DMDM; 21542456; -.
DR MassIVE; P02778; -.
DR MaxQB; P02778; -.
DR PaxDb; P02778; -.
DR PeptideAtlas; P02778; -.
DR PRIDE; P02778; -.
DR ProteomicsDB; 51594; -.
DR ABCD; P02778; 57 sequenced antibodies.
DR Antibodypedia; 6335; 847 antibodies from 41 providers.
DR CPTC; P02778; 2 antibodies.
DR DNASU; 3627; -.
DR Ensembl; ENST00000306602.3; ENSP00000305651.1; ENSG00000169245.6.
DR GeneID; 3627; -.
DR KEGG; hsa:3627; -.
DR MANE-Select; ENST00000306602.3; ENSP00000305651.1; NM_001565.4; NP_001556.2.
DR UCSC; uc003hjl.5; human.
DR CTD; 3627; -.
DR DisGeNET; 3627; -.
DR GeneCards; CXCL10; -.
DR HGNC; HGNC:10637; CXCL10.
DR HPA; ENSG00000169245; Tissue enhanced (lymphoid).
DR MIM; 147310; gene.
DR neXtProt; NX_P02778; -.
DR OpenTargets; ENSG00000169245; -.
DR PharmGKB; PA35568; -.
DR VEuPathDB; HostDB:ENSG00000169245; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000161759; -.
DR HOGENOM; CLU_143902_2_2_1; -.
DR InParanoid; P02778; -.
DR OMA; RNIRCRC; -.
DR OrthoDB; 1548456at2759; -.
DR PhylomeDB; P02778; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P02778; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; P02778; -.
DR SIGNOR; P02778; -.
DR BioGRID-ORCS; 3627; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; CXCL10; human.
DR EvolutionaryTrace; P02778; -.
DR GeneWiki; CXCL10; -.
DR GenomeRNAi; 3627; -.
DR Pharos; P02778; Tbio.
DR PRO; PR:P02778; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02778; protein.
DR Bgee; ENSG00000169245; Expressed in vermiform appendix and 145 other tissues.
DR Genevisible; P02778; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; TAS:ProtInc.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0048248; F:CXCR3 chemokine receptor binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IEP:ARUK-UCL.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0097398; P:cellular response to interleukin-17; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0098586; P:cellular response to virus; IEP:ARUK-UCL.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0042118; P:endothelial cell activation; IGI:CACAO.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:1901740; P:negative regulation of myoblast fusion; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:CACAO.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:2000406; P:positive regulation of T cell migration; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; TAS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; IDA:CACAO.
DR GO; GO:0010819; P:regulation of T cell chemotaxis; IDA:CACAO.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0010818; P:T cell chemotaxis; IMP:UniProtKB.
DR CDD; cd00273; Chemokine_CXC; 1.
DR InterPro; IPR001089; Chemokine_CXC.
DR InterPro; IPR018048; Chemokine_CXC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR033899; CXC_Chemokine_domain.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR10179; PTHR10179; 1.
DR Pfam; PF00048; IL8; 1.
DR PRINTS; PR00437; SMALLCYTKCXC.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Citrullination; Cytokine;
KW Direct protein sequencing; Disulfide bond; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10233762,
FT ECO:0000269|PubMed:11559369, ECO:0000269|PubMed:8423327"
FT CHAIN 22..98
FT /note="C-X-C motif chemokine 10"
FT /id="PRO_0000005101"
FT CHAIN 22..94
FT /note="CXCL10(1-73)"
FT /id="PRO_0000005102"
FT MOD_RES 26
FT /note="Citrulline; by PAD2"
FT /evidence="ECO:0000269|PubMed:18645041"
FT DISULFID 30..57
FT /evidence="ECO:0000269|PubMed:12173928,
FT ECO:0000269|PubMed:12737818, ECO:0007744|PDB:1LV9,
FT ECO:0007744|PDB:1O7Y, ECO:0007744|PDB:1O7Z,
FT ECO:0007744|PDB:1O80"
FT DISULFID 32..74
FT /evidence="ECO:0000269|PubMed:12173928,
FT ECO:0000269|PubMed:12737818, ECO:0007744|PDB:1LV9,
FT ECO:0007744|PDB:1O7Y, ECO:0007744|PDB:1O7Z,
FT ECO:0007744|PDB:1O80"
FT CONFLICT 93
FT /note="R -> M (in Ref. 1; CAA26370)"
FT /evidence="ECO:0000305"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1O7Z"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1O7Z"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1O80"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1O7Z"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1O7Z"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1O7Z"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1O7Z"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1O7Z"
SQ SEQUENCE 98 AA; 10881 MW; 44AE51967C58DDFF CRC64;
MNQTAILICC LIFLTLSGIQ GVPLSRTVRC TCISISNQPV NPRSLEKLEI IPASQFCPRV
EIIATMKKKG EKRCLNPESK AIKNLLKAVS KERSKRSP
