CCL3_HUMAN
ID CCL3_HUMAN Reviewed; 92 AA.
AC P10147;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=C-C motif chemokine 3;
DE AltName: Full=G0/G1 switch regulatory protein 19-1;
DE AltName: Full=Macrophage inflammatory protein 1-alpha;
DE Short=MIP-1-alpha;
DE AltName: Full=PAT 464.1;
DE AltName: Full=SIS-beta;
DE AltName: Full=Small-inducible cytokine A3;
DE AltName: Full=Tonsillar lymphocyte LD78 alpha protein;
DE Contains:
DE RecName: Full=MIP-1-alpha(4-69);
DE AltName: Full=LD78-alpha(4-69);
DE Flags: Precursor;
GN Name=CCL3; Synonyms=G0S19-1, MIP1A, SCYA3;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=3086300; DOI=10.1093/oxfordjournals.jbchem.a135549;
RA Obaru K., Fukuda M., Maeda S., Shimada K.;
RT "A cDNA clone used to study mRNA inducible in human tonsillar lymphocytes
RT by a tumor promoter.";
RL J. Biochem. 99:885-894(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=2521882;
RA Zipfel P.F., Balke J., Irving S.G., Kelly K., Siebenlist U.;
RT "Mitogenic activation of human T cells induces two closely related genes
RT which share structural similarities with a new family of secreted
RT factors.";
RL J. Immunol. 142:1582-1590(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=2271120; DOI=10.1089/dna.1990.9.589;
RA Blum S., Forsdyke R.E., Forsdyke D.R.;
RT "Three human homologs of a murine gene encoding an inhibitor of stem cell
RT proliferation.";
RL DNA Cell Biol. 9:589-602(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=1694014; DOI=10.1128/mcb.10.7.3646-3658.1990;
RA Nakao M., Nomiyama H., Shimada K.;
RT "Structures of human genes coding for cytokine LD78 and their expression.";
RL Mol. Cell. Biol. 10:3646-3658(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Natural killer cell;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-92.
RC TISSUE=Leukocyte;
RA Jang J.S., Kim B.E.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 24-92, AND MUTAGENESIS OF ASP-49.
RX PubMed=8541527;
RA Hunter M.G., Bawden L., Brotherton D., Craig S., Cribbes S.,
RA Czaplewski L.G., Dexter T.M., Drummond A.H., Gearing A.H., Heyworth C.M.,
RA Lord B.I., Mccourt M., Varley P.G., Wood L.M., Edwards R.M., Lewis P.J.;
RT "BB-10010: an active variant of human macrophage inflammatory protein-1
RT alpha with improved pharmaceutical properties.";
RL Blood 86:4400-4408(1995).
RN [8]
RP PROTEIN SEQUENCE OF 27-40 AND 71-83, AND FUNCTION.
RX PubMed=8525373; DOI=10.1126/science.270.5243.1811;
RA Cocchi F., DeVico A.L., Garzino-Demo A., Arya S.K., Gallo R.C., Lusso P.;
RT "Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-
RT suppressive factors produced by CD8+ T cells.";
RL Science 270:1811-1815(1995).
RN [9]
RP PROTEIN SEQUENCE OF 27-51, AND IDENTIFICATION OF LD78-ALPHA(4-69).
RX PubMed=7537510; DOI=10.1089/aid.1995.11.155;
RA Bertini R., Luini W., Sozzani S., Bottazzi B., Ruggiero P., Boraschi D.,
RA Saggioro D., Chieco-Bianchi L., Proost P., van Damme J., Mantovani A.;
RT "Identification of MIP-1 alpha/LD78 as a monocyte chemoattractant released
RT by the HTLV-I-transformed cell line MT4.";
RL AIDS Res. Hum. Retroviruses 11:155-160(1995).
RN [10]
RP GAG BINDING SITES ARG-40; ARG-68 AND ARG-70, AND MUTAGENESIS OF ARG-40;
RP ARG-68 AND ARG-70.
RX PubMed=9092555; DOI=10.1074/jbc.272.15.10103;
RA Koopmann W., Krangel M.S.;
RT "Identification of a glycosaminoglycan-binding site in chemokine macrophage
RT inflammatory protein-1alpha.";
RL J. Biol. Chem. 272:10103-10109(1997).
RN [11]
RP SUBUNIT, AND INTERACTION WITH MIP-1-BETA(3-69).
RX PubMed=12070155; DOI=10.1074/jbc.m203077200;
RA Guan E., Wang J., Roderiquez G., Norcross M.A.;
RT "Natural truncation of the chemokine MIP-1beta/CCL4 affects receptor
RT specificity but not anti-HIV-1 activity.";
RL J. Biol. Chem. 277:32348-32352(2002).
RN [12]
RP REVIEW.
RX PubMed=12401480; DOI=10.1016/s1359-6101(02)00045-x;
RA Menten P., Wuyts A., Van Damme J.;
RT "Macrophage inflammatory protein-1.";
RL Cytokine Growth Factor Rev. 13:455-481(2002).
RN [13]
RP STRUCTURE BY NMR OF 24-92, AND MUTAGENESIS OF ASP-49 AND GLU-89.
RX PubMed=10347159; DOI=10.1074/jbc.274.23.16077;
RA Czaplewski L.G., McKeating J., Craven C.J., Higgins L.D., Appay V.,
RA Brown A., Dudgeon T., Howard L.A., Meyers T., Owen J., Palan S.R., Tan P.,
RA Wilson G., Woods N.R., Heyworth C.M., Lord B.I., Brotherton D.,
RA Christison R., Craig S., Cribbes S., Edwards R.M., Evans S.J., Gilbert R.,
RA Morgan P., Eliot Randle E., Schofield N., Varley P.G., Fisher J.,
RA Jonathan P., Waltho J.P., Hunter M.G.;
RT "Identification of amino acid residues critical for aggregation of human CC
RT chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and
RT RANTES. Characterization of active disaggregated chemokine variants.";
RL J. Biol. Chem. 274:16077-16084(1999).
RN [14] {ECO:0007744|PDB:3FPU}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 24-92 IN COMPLEX WITH TICK
RP EVASIN-1, AND DISULFIDE BONDS.
RX PubMed=20041127; DOI=10.1371/journal.pone.0008514;
RA Dias J.M., Losberger C., Deruaz M., Power C.A., Proudfoot A.E., Shaw J.P.;
RT "Structural basis of chemokine sequestration by a tick chemokine binding
RT protein: the crystal structure of the complex between Evasin-1 and CCL3.";
RL PLoS ONE 4:e8514-e8514(2009).
CC -!- FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds
CC to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors
CC produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-
CC dependent inhibition of different strains of HIV-1, HIV-2, and simian
CC immunodeficiency virus (SIV). {ECO:0000269|PubMed:8525373}.
CC -!- SUBUNIT: Self-associates. Also heterodimer of MIP-1-alpha(4-69) and
CC MIP-1-beta(3-69). {ECO:0000269|PubMed:12070155}.
CC -!- INTERACTION:
CC P10147; P10147: CCL3; NbExp=3; IntAct=EBI-8459634, EBI-8459634;
CC P10147; P14735: IDE; NbExp=3; IntAct=EBI-8459634, EBI-2556886;
CC P10147; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-8459634, EBI-741480;
CC P10147; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-8459634, EBI-947187;
CC P10147; Q2F862; Xeno; NbExp=2; IntAct=EBI-8459634, EBI-16161937;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By TPA or PHA (TPA = 12-O-tetradecanoyl phorbol-13 acetate
CC (tumor promoter); PHA = phytohemagglutinin (T-cell mitogen)).
CC -!- PTM: N-terminal processed form LD78-alpha(4-69) is produced by
CC proteolytic cleavage after secretion from HTLV1-transformed T-cells.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Macrophage inflammatory protein
CC entry;
CC URL="https://en.wikipedia.org/wiki/Macrophage_Inflammatory_Protein";
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DR EMBL; D00044; BAA00029.1; -; mRNA.
DR EMBL; X03754; CAA27388.1; -; mRNA.
DR EMBL; X04018; CAA27643.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M25315; AAA57255.1; -; mRNA.
DR EMBL; M23452; AAA36316.1; -; mRNA.
DR EMBL; M23178; AAA35858.1; -; Genomic_DNA.
DR EMBL; D90144; BAA14172.1; -; Genomic_DNA.
DR EMBL; BC071834; AAH71834.1; -; mRNA.
DR EMBL; AF043339; AAC03539.1; -; mRNA.
DR CCDS; CCDS11307.1; -.
DR PIR; A35673; A30574.
DR RefSeq; NP_002974.1; NM_002983.2.
DR PDB; 1B50; NMR; -; A/B=24-92.
DR PDB; 1B53; NMR; -; A/B=24-92.
DR PDB; 2X69; X-ray; 2.65 A; A/B/C/D/E=23-92.
DR PDB; 2X6G; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=23-92.
DR PDB; 3FPU; X-ray; 1.76 A; B=24-92.
DR PDB; 3H44; X-ray; 3.00 A; C/D=23-92.
DR PDB; 3KBX; X-ray; 2.65 A; A/B/C/D/E=23-92.
DR PDB; 4RA8; X-ray; 2.60 A; A/B/C/D/E=23-91.
DR PDB; 4ZKB; X-ray; 2.90 A; B=24-92.
DR PDB; 5COR; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=23-92.
DR PDB; 5D65; X-ray; 3.10 A; A/B/C/D/E=23-92.
DR PDB; 7F1Q; EM; 2.90 A; R=24-92.
DR PDB; 7F1T; X-ray; 2.60 A; A=24-92.
DR PDBsum; 1B50; -.
DR PDBsum; 1B53; -.
DR PDBsum; 2X69; -.
DR PDBsum; 2X6G; -.
DR PDBsum; 3FPU; -.
DR PDBsum; 3H44; -.
DR PDBsum; 3KBX; -.
DR PDBsum; 4RA8; -.
DR PDBsum; 4ZKB; -.
DR PDBsum; 5COR; -.
DR PDBsum; 5D65; -.
DR PDBsum; 7F1Q; -.
DR PDBsum; 7F1T; -.
DR AlphaFoldDB; P10147; -.
DR SMR; P10147; -.
DR BioGRID; 112252; 207.
DR DIP; DIP-5837N; -.
DR IntAct; P10147; 4.
DR MINT; P10147; -.
DR STRING; 9606.ENSP00000477908; -.
DR BindingDB; P10147; -.
DR DrugBank; DB05364; ROX-888.
DR BioMuta; CCL3; -.
DR DMDM; 127078; -.
DR MassIVE; P10147; -.
DR PaxDb; P10147; -.
DR PeptideAtlas; P10147; -.
DR PRIDE; P10147; -.
DR ABCD; P10147; 17 sequenced antibodies.
DR Antibodypedia; 72661; 966 antibodies from 43 providers.
DR DNASU; 6348; -.
DR Ensembl; ENST00000613396.2; ENSP00000480753.1; ENSG00000278567.2.
DR Ensembl; ENST00000613922.2; ENSP00000477908.1; ENSG00000277632.2.
DR Ensembl; ENST00000616221.2; ENSP00000483712.1; ENSG00000274221.2.
DR GeneID; 6348; -.
DR KEGG; hsa:6348; -.
DR MANE-Select; ENST00000613922.2; ENSP00000477908.1; NM_002983.3; NP_002974.1.
DR UCSC; uc002hkv.5; human.
DR CTD; 6348; -.
DR DisGeNET; 6348; -.
DR GeneCards; CCL3; -.
DR HGNC; HGNC:10627; CCL3.
DR HPA; ENSG00000277632; Tissue enhanced (bone marrow, lung, lymphoid tissue).
DR MalaCards; CCL3; -.
DR MIM; 182283; gene.
DR neXtProt; NX_P10147; -.
DR OpenTargets; ENSG00000277632; -.
DR PharmGKB; PA35559; -.
DR VEuPathDB; HostDB:ENSG00000277632; -.
DR eggNOG; ENOG502SAF0; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_0_1; -.
DR InParanoid; P10147; -.
DR OMA; QEWVQKY; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P10147; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P10147; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; P10147; -.
DR SIGNOR; P10147; -.
DR BioGRID-ORCS; 6348; 8 hits in 1000 CRISPR screens.
DR ChiTaRS; CCL3; human.
DR EvolutionaryTrace; P10147; -.
DR GeneWiki; CCL3; -.
DR GenomeRNAi; 6348; -.
DR Pharos; P10147; Tbio.
DR PRO; PR:P10147; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P10147; protein.
DR Bgee; ENSG00000277632; Expressed in bone marrow and 104 other tissues.
DR ExpressionAtlas; P10147; baseline and differential.
DR Genevisible; P10147; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0031726; F:CCR1 chemokine receptor binding; IPI:UniProtKB.
DR GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0016004; F:phospholipase activator activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0043615; P:astrocyte cell migration; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0001775; P:cell activation; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0043308; P:eosinophil degranulation; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071621; P:granulocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
DR GO; GO:0090280; P:positive regulation of calcium ion import; TAS:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; TAS:ARUK-UCL.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; TAS:ARUK-UCL.
DR GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070723; P:response to cholesterol; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0023052; P:signaling; IEP:UniProtKB.
DR GO; GO:0010818; P:T cell chemotaxis; IDA:UniProtKB.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR000827; Chemokine_CC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Inflammatory response; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8541527"
FT CHAIN 24..92
FT /note="C-C motif chemokine 3"
FT /id="PRO_0000005156"
FT CHAIN 27..92
FT /note="MIP-1-alpha(4-69)"
FT /id="PRO_0000005157"
FT SITE 40
FT /note="Involved in GAG binding"
FT SITE 68
FT /note="Involved in GAG binding"
FT SITE 70
FT /note="Involved in GAG binding"
FT DISULFID 33..57
FT /evidence="ECO:0000269|PubMed:20041127,
FT ECO:0007744|PDB:3FPU"
FT DISULFID 34..73
FT /evidence="ECO:0000269|PubMed:20041127,
FT ECO:0007744|PDB:3FPU"
FT VARIANT 78
FT /note="E -> D (in dbSNP:rs34171309)"
FT /id="VAR_048701"
FT MUTAGEN 40
FT /note="R->A: Slightly reduces heparin binding."
FT /evidence="ECO:0000269|PubMed:9092555"
FT MUTAGEN 49
FT /note="D->A: Reduces self-association; in BB-10010:
FT Improved pharmaceutical properties."
FT /evidence="ECO:0000269|PubMed:10347159,
FT ECO:0000269|PubMed:8541527"
FT MUTAGEN 68
FT /note="R->A: Strongly reduces heparin binding."
FT /evidence="ECO:0000269|PubMed:9092555"
FT MUTAGEN 70
FT /note="R->A: Reduces heparin binding."
FT /evidence="ECO:0000269|PubMed:9092555"
FT MUTAGEN 89
FT /note="E->A: Reduces self-association."
FT /evidence="ECO:0000269|PubMed:10347159"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2X6G"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7F1Q"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3FPU"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4ZKB"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:3FPU"
SQ SEQUENCE 92 AA; 10085 MW; 517865D5D6776CA8 CRC64;
MQVSTAALAV LLCTMALCNQ FSASLAADTP TACCFSYTSR QIPQNFIADY FETSSQCSKP
GVIFLTKRSR QVCADPSEEW VQKYVSDLEL SA
