CCL4_HUMAN
ID CCL4_HUMAN Reviewed; 92 AA.
AC P13236; P22617; Q13704; Q3SXL8; Q6FGI8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=C-C motif chemokine 4;
DE AltName: Full=G-26 T-lymphocyte-secreted protein;
DE AltName: Full=HC21;
DE AltName: Full=Lymphocyte activation gene 1 protein;
DE Short=LAG-1;
DE AltName: Full=MIP-1-beta(1-69);
DE AltName: Full=Macrophage inflammatory protein 1-beta;
DE Short=MIP-1-beta;
DE AltName: Full=PAT 744;
DE AltName: Full=Protein H400;
DE AltName: Full=SIS-gamma;
DE AltName: Full=Small-inducible cytokine A4;
DE AltName: Full=T-cell activation protein 2;
DE Short=ACT-2;
DE Contains:
DE RecName: Full=MIP-1-beta(3-69);
DE Flags: Precursor;
GN Name=CCL4; Synonyms=LAG1, MIP1B, SCYA4;
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=2462251; DOI=10.1073/pnas.85.24.9704;
RA Lipes M.A., Napolitano M., Jeang K.-T., Chang N.T., Leonard W.J.;
RT "Identification, cloning, and characterization of an immune activation
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9704-9708(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [MRNA].
RC TISSUE=T-cell;
RX PubMed=2521353;
RA Brown K.D., Zurawski S.M., Mosmann T.R., Zurawski G.;
RT "A family of small inducible proteins secreted by leukocytes are members of
RT a new superfamily that includes leukocyte and fibroblast-derived
RT inflammatory agents, growth factors, and indicators of various activation
RT processes.";
RL J. Immunol. 142:679-687(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Natural killer cell;
RX PubMed=2247088; DOI=10.1016/0161-5890(90)90097-j;
RA Baixeras E., Roman-Roman S., Jitsukawa S., Genevee C., Mechiche S.,
RA Viegas-Pequignot E., Hercend T., Triebel F.;
RT "Cloning and expression of a lymphocyte activation gene (LAG-1).";
RL Mol. Immunol. 27:1091-1102(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=2568930; DOI=10.1002/eji.1830190614;
RA Chang H.C., Reinherz E.L.;
RT "Isolation and characterization of a cDNA encoding a putative cytokine
RT which is induced by stimulation via the CD2 structure on human T
RT lymphocytes.";
RL Eur. J. Immunol. 19:1045-1051(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1894635; DOI=10.1016/s0021-9258(19)47404-8;
RA Napolitano M., Modi W.S., Cevario S.J., Gnarra J.R., Seuanez H.N.,
RA Leonard W.J.;
RT "The gene encoding the Act-2 cytokine. Genomic structure, HTLV-I/Tax
RT responsiveness of 5' upstream sequences, and chromosomal localization.";
RL J. Biol. Chem. 266:17531-17536(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=15843566; DOI=10.4049/jimmunol.174.9.5655;
RA Colobran R., Adreani P., Ashhab Y., Llano A., Este J.A., Dominguez O.,
RA Pujol-Borrell R., Juan M.;
RT "Multiple products derived from two CCL4 loci: high incidence of a new
RT polymorphism in HIV+ patients.";
RL J. Immunol. 174:5655-5664(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-80.
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-92, AND VARIANT THR-80.
RC TISSUE=T-cell;
RX PubMed=2809212;
RA Miller M.D., Hata S., Waal Malefyt R., Krangel M.S.;
RT "A novel polypeptide secreted by activated human T lymphocytes.";
RL J. Immunol. 143:2907-2916(1989).
RN [12]
RP RECEPTOR INTERACTION.
RX PubMed=9521068;
RX DOI=10.1002/(sici)1521-4141(199802)28:02<582::aid-immu582>3.0.co;2-a;
RA Bernardini G., Hedrick J., Sozzani S., Luini W., Spinetti G., Weiss M.,
RA Menon S., Zlotnik A., Mantovani A., Santoni A., Napolitano M.;
RT "Identification of the CC chemokines TARC and macrophage inflammatory
RT protein-1 beta as novel functional ligands for the CCR8 receptor.";
RL Eur. J. Immunol. 28:582-588(1998).
RN [13]
RP 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 [14]
RP FUNCTION.
RX PubMed=10540332;
RX DOI=10.1002/(sici)1521-4141(199910)29:10<3210::aid-immu3210>3.0.co;2-w;
RA Garlisi C.G., Xiao H., Tian F., Hedrick J.A., Billah M.M., Egan R.W.,
RA Umland S.P.;
RT "The assignment of chemokine-chemokine receptor pairs: TARC and MIP-1 beta
RT are not ligands for human CC-chemokine receptor 8.";
RL Eur. J. Immunol. 29:3210-3215(1999).
RN [15]
RP IDENTIFICATION OF MIP-1-BETA(3-69) BY MASS SPECTROMETRY, FUNCTION, AND
RP SUBUNIT.
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 [16]
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 [17]
RP STRUCTURE BY NMR.
RX PubMed=8134838; DOI=10.1126/science.8134838;
RA Lodi P.J., Garrett D.S., Kuscewski J., Tsang M.L.S., Weatherbee J.A.,
RA Leonard W.J., Gronenborn A.M., Clore G.M.;
RT "High-resolution solution structure of the beta chemokine hMIP-1 beta by
RT multidimensional NMR.";
RL Science 263:1762-1767(1994).
CC -!- FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds
CC to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-
CC cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of
CC different strains of HIV-1, HIV-2, and simian immunodeficiency virus
CC (SIV). The processed form MIP-1-beta(3-69) retains the abilities to
CC induce down-modulation of surface expression of the chemokine receptor
CC CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-
CC beta(3-69) is also a ligand for CCR1 and CCR2 isoform B.
CC {ECO:0000269|PubMed:10540332, ECO:0000269|PubMed:12070155,
CC ECO:0000269|PubMed:8525373}.
CC -!- SUBUNIT: Homodimer and heterodimer of MIP-1-alpha(4-69) and MIP-1-
CC beta(3-69). {ECO:0000269|PubMed:12070155}.
CC -!- INTERACTION:
CC P13236; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2873970, EBI-11343438;
CC P13236; P13236: CCL4; NbExp=3; IntAct=EBI-2873970, EBI-2873970;
CC P13236; P34972: CNR2; NbExp=3; IntAct=EBI-2873970, EBI-2835940;
CC P13236; P48165: GJA8; NbExp=3; IntAct=EBI-2873970, EBI-17458373;
CC P13236; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2873970, EBI-13345167;
CC P13236; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-2873970, EBI-13067820;
CC P13236; Q9P0N8: MARCHF2; NbExp=3; IntAct=EBI-2873970, EBI-10317612;
CC P13236; Q6IN84: MRM1; NbExp=3; IntAct=EBI-2873970, EBI-5454865;
CC P13236; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2873970, EBI-18159983;
CC P13236; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2873970, EBI-17595455;
CC P13236; Q9BRI3: SLC30A2; NbExp=8; IntAct=EBI-2873970, EBI-8644112;
CC P13236; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-2873970, EBI-10262251;
CC P13236; P30825: SLC7A1; NbExp=3; IntAct=EBI-2873970, EBI-4289564;
CC P13236; Q9NYW4: TAS2R5; NbExp=3; IntAct=EBI-2873970, EBI-17933167;
CC P13236; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2873970, EBI-6268651;
CC P13236; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2873970, EBI-8638294;
CC P13236; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-2873970, EBI-11724423;
CC P13236; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2873970, EBI-2548832;
CC P13236; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-2873970, EBI-13356252;
CC PRO_0000005165; P51681: CCR5; NbExp=2; IntAct=EBI-6625160, EBI-489374;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By mitogens.
CC -!- PTM: N-terminal processed form MIP-1-beta(3-69) is produced by
CC proteolytic cleavage after secretion from peripheral blood lymphocytes.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a ligand for CCR8.
CC {ECO:0000305|PubMed:9521068}.
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; J04130; AAA51576.1; -; mRNA.
DR EMBL; M25316; AAA57256.1; -; mRNA.
DR EMBL; M23502; AAA36656.1; -; mRNA.
DR EMBL; X53683; CAA37723.1; -; mRNA.
DR EMBL; X53682; CAA37722.2; ALT_SEQ; Genomic_DNA.
DR EMBL; X16166; CAA34291.1; -; mRNA.
DR EMBL; M69203; AAB00790.1; -; Genomic_DNA.
DR EMBL; M69201; AAB00790.1; JOINED; Genomic_DNA.
DR EMBL; M69202; AAB00790.1; JOINED; Genomic_DNA.
DR EMBL; AY766446; AAX07305.1; -; mRNA.
DR EMBL; AY766459; AAX07292.1; -; Genomic_DNA.
DR EMBL; CR542119; CAG46916.1; -; mRNA.
DR EMBL; AC003976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104226; AAI04227.1; -; mRNA.
DR EMBL; BC104227; AAI04228.1; -; mRNA.
DR EMBL; BC107433; AAI07434.1; -; mRNA.
DR EMBL; M57503; AAA36752.1; -; mRNA.
DR CCDS; CCDS11308.1; -.
DR PIR; JH0319; A31767.
DR RefSeq; NP_002975.1; NM_002984.3.
DR RefSeq; NP_996890.1; NM_207007.3.
DR PDB; 1HUM; NMR; -; A/B=24-92.
DR PDB; 1HUN; NMR; -; A/B=24-92.
DR PDB; 1JE4; NMR; -; A=24-92.
DR PDB; 2FFK; NMR; -; B=24-92.
DR PDB; 2FIN; NMR; -; B=24-92.
DR PDB; 2X6L; X-ray; 2.60 A; A/B/C/D/E=24-92.
DR PDB; 3TN2; X-ray; 1.60 A; A=24-91.
DR PDB; 4RAL; X-ray; 3.15 A; D/E=24-92.
DR PDBsum; 1HUM; -.
DR PDBsum; 1HUN; -.
DR PDBsum; 1JE4; -.
DR PDBsum; 2FFK; -.
DR PDBsum; 2FIN; -.
DR PDBsum; 2X6L; -.
DR PDBsum; 3TN2; -.
DR PDBsum; 4RAL; -.
DR AlphaFoldDB; P13236; -.
DR SMR; P13236; -.
DR BioGRID; 112254; 26.
DR BioGRID; 132664; 24.
DR DIP; DIP-5840N; -.
DR IntAct; P13236; 26.
DR MINT; P13236; -.
DR STRING; 9606.ENSP00000482259; -.
DR BindingDB; P13236; -.
DR BioMuta; CCL4; -.
DR DMDM; 127080; -.
DR MassIVE; P13236; -.
DR PaxDb; P13236; -.
DR PeptideAtlas; P13236; -.
DR PRIDE; P13236; -.
DR Antibodypedia; 72629; 609 antibodies from 39 providers.
DR DNASU; 6351; -.
DR Ensembl; ENST00000615863.2; ENSP00000482259.1; ENSG00000275302.2.
DR Ensembl; ENST00000617322.4; ENSP00000480345.1; ENSG00000275824.4.
DR Ensembl; ENST00000621600.4; ENSP00000478708.1; ENSG00000277943.4.
DR GeneID; 388372; -.
DR GeneID; 6351; -.
DR KEGG; hsa:388372; -.
DR KEGG; hsa:6351; -.
DR MANE-Select; ENST00000615863.2; ENSP00000482259.1; NM_002984.4; NP_002975.1.
DR UCSC; uc002hkw.3; human.
DR CTD; 388372; -.
DR CTD; 6351; -.
DR DisGeNET; 388372; -.
DR DisGeNET; 6351; -.
DR GeneCards; CCL4; -.
DR HGNC; HGNC:10630; CCL4.
DR HPA; ENSG00000275302; Tissue enhanced (bone).
DR MIM; 182284; gene.
DR neXtProt; NX_P13236; -.
DR OpenTargets; ENSG00000275302; -.
DR VEuPathDB; HostDB:ENSG00000275302; -.
DR eggNOG; ENOG502S8M4; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_0_1; -.
DR InParanoid; P13236; -.
DR OMA; SGPKKCC; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P13236; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P13236; -.
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; P13236; -.
DR SIGNOR; P13236; -.
DR BioGRID-ORCS; 388372; 8 hits in 179 CRISPR screens.
DR BioGRID-ORCS; 6351; 6 hits in 968 CRISPR screens.
DR ChiTaRS; CCL4; human.
DR EvolutionaryTrace; P13236; -.
DR GeneWiki; CCL4; -.
DR Pharos; P13236; Tbio.
DR PRO; PR:P13236; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13236; protein.
DR Bgee; ENSG00000275302; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; P13236; baseline and differential.
DR Genevisible; P13236; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0008009; F:chemokine activity; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Disulfide bond; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..92
FT /note="C-C motif chemokine 4"
FT /id="PRO_0000005164"
FT CHAIN 26..92
FT /note="MIP-1-beta(3-69)"
FT /id="PRO_0000005165"
FT DISULFID 34..58
FT /evidence="ECO:0000250"
FT DISULFID 35..74
FT /evidence="ECO:0000250"
FT VARIANT 12
FT /note="M -> V (in dbSNP:rs1049752)"
FT /id="VAR_048702"
FT VARIANT 20
FT /note="P -> L (in dbSNP:rs1130750)"
FT /id="VAR_048703"
FT VARIANT 80
FT /note="S -> T (in dbSNP:rs1719152)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2809212"
FT /id="VAR_059211"
FT CONFLICT 6
FT /note="T -> C (in Ref. 11; AAA36752)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="A -> S (in Ref. 6; AAB00790)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..45
FT /note="ARKLPR -> REASS (in Ref. 3; AAA36656)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> I (in Ref. 11; AAA36752)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> G (in Ref. 6; CAA37722/AAB00790)"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3TN2"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3TN2"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3TN2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3TN2"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3TN2"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3TN2"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2FFK"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3TN2"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:3TN2"
SQ SEQUENCE 92 AA; 10212 MW; F2EA7CF341B0E258 CRC64;
MKLCVTVLSL LMLVAAFCSP ALSAPMGSDP PTACCFSYTA RKLPRNFVVD YYETSSLCSQ
PAVVFQTKRS KQVCADPSES WVQEYVYDLE LN
