PLF4_HUMAN
ID PLF4_HUMAN Reviewed; 101 AA.
AC P02776; Q53X61; Q9UC64; Q9UC65;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Platelet factor 4;
DE Short=PF-4;
DE AltName: Full=C-X-C motif chemokine 4;
DE AltName: Full=Iroplact;
DE AltName: Full=Oncostatin-A;
DE Contains:
DE RecName: Full=Platelet factor 4, short form;
DE AltName: Full=Endothelial cell growth inhibitor {ECO:0000303|PubMed:7644496};
DE Flags: Precursor;
GN Name=PF4; Synonyms=CXCL4, SCYB4;
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=3098319;
RA Poncz M., Surrey S., Larocco P., Weiss M.J., Rappaport E.F., Conway T.M.,
RA Schwartz E.;
RT "Cloning and characterization of platelet factor 4 cDNA derived from a
RT human erythroleukemic cell line.";
RL Blood 69:219-223(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1695112;
RA Eisman R., Surrey S., Ramachandran B., Schwartz E., Poncz M.;
RT "Structural and functional comparison of the genes for human platelet
RT factor 4 and PF4alt.";
RL Blood 76:336-344(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11468158; DOI=10.1182/blood.v98.3.610;
RA Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M., Poncz M.,
RA McKenzie S.E., Reilly M.P.;
RT "Localization of distal regulatory domains in the megakaryocyte-specific
RT platelet basic protein/platelet factor 4 gene locus.";
RL Blood 98:610-617(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP PROTEIN SEQUENCE OF 32-101.
RX PubMed=893407; DOI=10.1016/s0021-9258(17)39951-9;
RA Hermodson M., Schmer G., Kurachi K.;
RT "Isolation, crystallization, and primary amino acid sequence of human
RT platelet factor 4.";
RL J. Biol. Chem. 252:6276-6279(1977).
RN [8]
RP PROTEIN SEQUENCE OF 32-101.
RX PubMed=267922; DOI=10.1073/pnas.74.6.2256;
RA Deuel T.F., Keim P.S., Farmer M., Heinrikson R.L.;
RT "Amino acid sequence of human platelet factor 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:2256-2258(1977).
RN [9]
RP PROTEIN SEQUENCE OF 32-101.
RX PubMed=601757; DOI=10.1016/0049-3848(77)90117-7;
RA Walz D.A., Wu V.Y., de Lamo R., Dene H., McCoy L.E.;
RT "Primary structure of human platelet factor 4.";
RL Thromb. Res. 11:893-898(1977).
RN [10]
RP PROTEIN SEQUENCE OF 32-101.
RX PubMed=6445090;
RA Morgan F.J., Begg G.S., Chesterman C.N.;
RT "Complete covalent structure of human platelet factor 4.";
RL Thromb. Haemost. 42:1652-1660(1980).
RN [11]
RP PROTEIN SEQUENCE OF 32-101, IDENTIFICATION OF PF4 SHORT FORM, FUNCTION,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Leukocyte;
RX PubMed=7644496; DOI=10.1073/pnas.92.17.7799;
RA Gupta S.K., Hassel T., Singh J.P.;
RT "A potent inhibitor of endothelial cell proliferation is generated by
RT proteolytic cleavage of the chemokine platelet factor 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7799-7803(1995).
RN [12]
RP HEPARIN-BINDING REGION.
RX PubMed=23536183; DOI=10.1074/jbc.m113.455329;
RA Kuo J.H., Chen Y.P., Liu J.S., Dubrac A., Quemener C., Prats H.,
RA Bikfalvi A., Wu W.G., Sue S.C.;
RT "Alternative C-terminal helix orientation alters chemokine function:
RT Structure of the Anti-angiogenic Chemokine, CXCL4L1.";
RL J. Biol. Chem. 288:13522-13533(2013).
RN [13]
RP INTERACTION WITH TNFAIP6.
RX PubMed=27044744; DOI=10.1074/jbc.m116.720953;
RA Dyer D.P., Salanga C.L., Johns S.C., Valdambrini E., Fuster M.M.,
RA Milner C.M., Day A.J., Handel T.M.;
RT "The Anti-inflammatory Protein TSG-6 Regulates Chemokine Function by
RT Inhibiting Chemokine/Glycosaminoglycan Interactions.";
RL J. Biol. Chem. 291:12627-12640(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=8031770; DOI=10.1021/bi00193a025;
RA Zhang X., Chen L., Bancroft D.P., Lai C.K., Maione T.E.;
RT "Crystal structure of recombinant human platelet factor 4.";
RL Biochemistry 33:8361-8366(1994).
RN [15]
RP STRUCTURE BY NMR OF 43-101, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=7547867; DOI=10.1021/bi00036a012;
RA Mayo K.H., Roongta V., Ilyina E., Milius R., Barker S., Quinlan C.,
RA La Rosa G., Daly T.J.;
RT "NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-
RT terminal chimera: a symmetric tetramer.";
RL Biochemistry 34:11399-11409(1995).
CC -!- FUNCTION: Released during platelet aggregation. Neutralizes the
CC anticoagulant effect of heparin because it binds more strongly to
CC heparin than to the chondroitin-4-sulfate chains of the carrier
CC molecule. Chemotactic for neutrophils and monocytes. Inhibits
CC endothelial cell proliferation, the short form is a more potent
CC inhibitor than the longer form. {ECO:0000269|PubMed:7644496}.
CC -!- SUBUNIT: Homotetramer (PubMed:7547867, PubMed:8031770). Interacts with
CC TNFAIP6 (via Link domain) (PubMed:27044744).
CC {ECO:0000269|PubMed:27044744, ECO:0000269|PubMed:7547867,
CC ECO:0000269|PubMed:8031770}.
CC -!- INTERACTION:
CC P02776; P02749: APOH; NbExp=2; IntAct=EBI-2565740, EBI-2114682;
CC P02776; P51671: CCL11; NbExp=2; IntAct=EBI-2565740, EBI-727357;
CC P02776; Q99616: CCL13; NbExp=2; IntAct=EBI-2565740, EBI-725342;
CC P02776; Q92583: CCL17; NbExp=2; IntAct=EBI-2565740, EBI-16640146;
CC P02776; P13500: CCL2; NbExp=2; IntAct=EBI-2565740, EBI-1034732;
CC P02776; P78556: CCL20; NbExp=2; IntAct=EBI-2565740, EBI-3913209;
CC P02776; O00585: CCL21; NbExp=2; IntAct=EBI-2565740, EBI-953695;
CC P02776; O15444: CCL25; NbExp=3; IntAct=EBI-2565740, EBI-7783341;
CC P02776; Q9Y258: CCL26; NbExp=3; IntAct=EBI-2565740, EBI-7783416;
CC P02776; Q9NRJ3: CCL28; NbExp=3; IntAct=EBI-2565740, EBI-7783254;
CC P02776; P13501: CCL5; NbExp=6; IntAct=EBI-2565740, EBI-2848366;
CC P02776; PRO_0000005175 [P13501]: CCL5; NbExp=3; IntAct=EBI-2565740, EBI-11712923;
CC P02776; P02778: CXCL10; NbExp=2; IntAct=EBI-2565740, EBI-7815386;
CC P02776; O14625: CXCL11; NbExp=2; IntAct=EBI-2565740, EBI-2871971;
CC P02776; P48061: CXCL12; NbExp=4; IntAct=EBI-2565740, EBI-3913254;
CC P02776; O95715: CXCL14; NbExp=3; IntAct=EBI-2565740, EBI-2798068;
CC P02776; Q6UXB2: CXCL17; NbExp=2; IntAct=EBI-2565740, EBI-16804198;
CC P02776; P19875: CXCL2; NbExp=3; IntAct=EBI-2565740, EBI-2114901;
CC P02776; P80162: CXCL6; NbExp=2; IntAct=EBI-2565740, EBI-9214033;
CC P02776; P10145: CXCL8; NbExp=2; IntAct=EBI-2565740, EBI-3917999;
CC P02776; Q07325: CXCL9; NbExp=3; IntAct=EBI-2565740, EBI-3911467;
CC P02776; P47992: XCL1; NbExp=2; IntAct=EBI-2565740, EBI-10209901;
CC PRO_0000005068; PRO_0000002059 [P02749]: APOH; NbExp=4; IntAct=EBI-11809981, EBI-11809989;
CC PRO_0000005068; P0DTC2: S; Xeno; NbExp=3; IntAct=EBI-11809981, EBI-25474821;
CC PRO_0000351217; P13501: CCL5; NbExp=2; IntAct=EBI-20561364, EBI-2848366;
CC PRO_0000351217; PRO_0000005175 [P13501]: CCL5; NbExp=2; IntAct=EBI-20561364, EBI-11712923;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7644496}.
CC -!- MASS SPECTROMETRY: [Platelet factor 4]: Mass=7765; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7644496};
CC -!- MASS SPECTROMETRY: [Platelet factor 4, short form]: Mass=6033;
CC Method=Electrospray; Note=Short form.;
CC Evidence={ECO:0000269|PubMed:7644496};
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL4 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL4";
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DR EMBL; M25897; AAA60066.1; -; mRNA.
DR EMBL; AF349466; AAK29643.1; -; Genomic_DNA.
DR EMBL; CR407677; CAG28605.1; -; mRNA.
DR EMBL; AC097709; AAY41003.1; -; Genomic_DNA.
DR EMBL; BC093965; AAH93965.1; -; mRNA.
DR EMBL; BC112093; AAI12094.1; -; mRNA.
DR CCDS; CCDS3562.1; -.
DR PIR; A60161; PFHU4.
DR RefSeq; NP_002610.1; NM_002619.3.
DR PDB; 1DN3; NMR; -; A=87-101.
DR PDB; 1F9Q; X-ray; 2.00 A; A/B/C/D=32-101.
DR PDB; 1F9R; X-ray; 2.00 A; A/B/C/D=32-101.
DR PDB; 1F9S; X-ray; 2.38 A; A/B/C/D=32-101.
DR PDB; 1PFM; NMR; -; A/B/C/D=39-101.
DR PDB; 1PFN; NMR; -; A/B/C/D=39-101.
DR PDB; 1RHP; X-ray; 2.40 A; A/B/C/D=32-101.
DR PDB; 4R9W; X-ray; 2.50 A; A/B=32-101.
DR PDB; 4R9Y; X-ray; 4.11 A; A/B/C/D=32-101.
DR PDB; 4RAU; X-ray; 3.74 A; C/F/I/L/O/R/U/X=32-101.
DR PDBsum; 1DN3; -.
DR PDBsum; 1F9Q; -.
DR PDBsum; 1F9R; -.
DR PDBsum; 1F9S; -.
DR PDBsum; 1PFM; -.
DR PDBsum; 1PFN; -.
DR PDBsum; 1RHP; -.
DR PDBsum; 4R9W; -.
DR PDBsum; 4R9Y; -.
DR PDBsum; 4RAU; -.
DR AlphaFoldDB; P02776; -.
DR SMR; P02776; -.
DR BioGRID; 111219; 28.
DR DIP; DIP-56941N; -.
DR IntAct; P02776; 27.
DR MINT; P02776; -.
DR STRING; 9606.ENSP00000296029; -.
DR BindingDB; P02776; -.
DR ChEMBL; CHEMBL3286075; -.
DR DrugBank; DB00055; Drotrecogin alfa.
DR DrugBank; DB01109; Heparin.
DR PhosphoSitePlus; P02776; -.
DR BioMuta; PF4; -.
DR DMDM; 130304; -.
DR OGP; P02776; -.
DR jPOST; P02776; -.
DR MassIVE; P02776; -.
DR PaxDb; P02776; -.
DR PeptideAtlas; P02776; -.
DR PRIDE; P02776; -.
DR ProteomicsDB; 51593; -.
DR TopDownProteomics; P02776; -.
DR ABCD; P02776; 2 sequenced antibodies.
DR Antibodypedia; 24586; 503 antibodies from 32 providers.
DR DNASU; 5196; -.
DR Ensembl; ENST00000296029.4; ENSP00000296029.3; ENSG00000163737.5.
DR GeneID; 5196; -.
DR KEGG; hsa:5196; -.
DR MANE-Select; ENST00000296029.4; ENSP00000296029.3; NM_002619.4; NP_002610.1.
DR UCSC; uc003hhi.4; human.
DR CTD; 5196; -.
DR DisGeNET; 5196; -.
DR GeneCards; PF4; -.
DR HGNC; HGNC:8861; PF4.
DR HPA; ENSG00000163737; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 173460; gene.
DR neXtProt; NX_P02776; -.
DR OpenTargets; ENSG00000163737; -.
DR PharmGKB; PA33203; -.
DR VEuPathDB; HostDB:ENSG00000163737; -.
DR eggNOG; ENOG502TF57; Eukaryota.
DR GeneTree; ENSGT00940000163666; -.
DR HOGENOM; CLU_143902_1_2_1; -.
DR InParanoid; P02776; -.
DR OMA; CAVPQLI; -.
DR OrthoDB; 1618797at2759; -.
DR PhylomeDB; P02776; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P02776; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR SignaLink; P02776; -.
DR BioGRID-ORCS; 5196; 20 hits in 1019 CRISPR screens.
DR EvolutionaryTrace; P02776; -.
DR GeneWiki; Platelet_factor_4; -.
DR GenomeRNAi; 5196; -.
DR Pharos; P02776; Tbio.
DR PRO; PR:P02776; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02776; protein.
DR Bgee; ENSG00000163737; Expressed in monocyte and 119 other tissues.
DR Genevisible; P02776; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
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; IDA:UniProtKB.
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:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA: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 InterPro; IPR027222; PF4.
DR PANTHER; PTHR10179; PTHR10179; 1.
DR PANTHER; PTHR10179:SF38; PTHR10179:SF38; 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; Cytokine; Direct protein sequencing;
KW Disulfide bond; Heparin-binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:267922,
FT ECO:0000269|PubMed:601757, ECO:0000269|PubMed:6445090,
FT ECO:0000269|PubMed:7644496, ECO:0000269|PubMed:893407"
FT CHAIN 32..101
FT /note="Platelet factor 4"
FT /id="PRO_0000005068"
FT CHAIN 48..101
FT /note="Platelet factor 4, short form"
FT /evidence="ECO:0000269|PubMed:7644496"
FT /id="PRO_0000351217"
FT BINDING 92..98
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06765"
FT DISULFID 41..67
FT /evidence="ECO:0000269|PubMed:6445090"
FT DISULFID 43..83
FT /evidence="ECO:0000269|PubMed:6445090"
FT CONFLICT 78
FT /note="N -> D (in Ref. 8; AA sequence and 9; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1PFN"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1F9Q"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1F9Q"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1F9Q"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1F9S"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1F9Q"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1F9Q"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1PFM"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1F9Q"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1F9Q"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1F9Q"
SQ SEQUENCE 101 AA; 10845 MW; E96C2EFE9B944D85 CRC64;
MSSAAGFCAS RPGLLFLGLL LLPLVVAFAS AEAEEDGDLQ CLCVKTTSQV RPRHITSLEV
IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S
