FABP7_HUMAN
ID FABP7_HUMAN Reviewed; 132 AA.
AC O15540; B2R4L1; O14951; Q6IAU7; Q9H047;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Fatty acid-binding protein, brain;
DE AltName: Full=Brain lipid-binding protein;
DE Short=BLBP;
DE AltName: Full=Brain-type fatty acid-binding protein;
DE Short=B-FABP;
DE AltName: Full=Fatty acid-binding protein 7;
DE AltName: Full=Mammary-derived growth inhibitor related;
GN Name=FABP7; Synonyms=BLBP, FABPB, MRG;
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] (ISOFORM 1).
RC TISSUE=Brain;
RA Schnuetgen F., Boerchers T., Xhong N., Godbout R., Sacchettini J.C.,
RA Spener F.;
RT "Human brain-type fatty acid binding protein shows high affinity for omega-
RT 3 fatty acids but not for omega-6 fatty acids.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9375786; DOI=10.1016/s0167-4781(97)00115-2;
RA Shimizu F., Watanabe T.K., Shinomiya H., Nakamura Y., Fujiwara T.;
RT "Isolation and expression of a cDNA for human brain fatty acid-binding
RT protein (B-FABP).";
RL Biochim. Biophys. Acta 1354:24-28(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=9591779; DOI=10.1038/sj.onc.1201740;
RA Godbout R., Bisgrove D.A., Shkolny D., Day R.S. III;
RT "Correlation of B-FABP and GFAP expression in malignant glioma.";
RL Oncogene 16:1955-1962(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
RA Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
RA Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shi Y.E., Ni J.;
RT "Identification and characterization of a novel human tumor suppressor gene
RT with homology to mammary derived growth inhibitor.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [12]
RP PROTEIN SEQUENCE OF 11-53; 60-79; 83-97 AND 114-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
RX PubMed=10854433; DOI=10.1074/jbc.m003001200;
RA Balendiran G.K., Schnuetgen F., Scapin G., Boerchers T., Xhong N., Lim K.,
RA Godbout R., Spener F., Sacchettini J.C.;
RT "Crystal structure and thermodynamic analysis of human brain fatty acid-
RT binding protein.";
RL J. Biol. Chem. 275:27045-27054(2000).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=12479569; DOI=10.1023/a:1020566909213;
RA Rademacher M., Zimmerman A.W., Rueterjans H., Veerkamp J.H., Luecke C.;
RT "Solution structure of fatty acid-binding protein from human brain.";
RL Mol. Cell. Biochem. 239:61-68(2002).
CC -!- FUNCTION: B-FABP could be involved in the transport of a so far unknown
CC hydrophobic ligand with potential morphogenic activity during CNS
CC development. It is required for the establishment of the radial glial
CC fiber system in developing brain, a system that is necessary for the
CC migration of immature neurons to establish cortical layers (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O15540; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10697159, EBI-10976677;
CC O15540; O15354: GPR37; NbExp=3; IntAct=EBI-10697159, EBI-15639515;
CC O15540; P28799: GRN; NbExp=3; IntAct=EBI-10697159, EBI-747754;
CC O15540; P28799-2: GRN; NbExp=3; IntAct=EBI-10697159, EBI-25860013;
CC O15540; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10697159, EBI-10975473;
CC O15540; D3DTS7: PMP22; NbExp=3; IntAct=EBI-10697159, EBI-25882629;
CC O15540; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10697159, EBI-396669;
CC O15540; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10697159, EBI-5235340;
CC O15540; O76024: WFS1; NbExp=3; IntAct=EBI-10697159, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15540-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15540-2; Sequence=VSP_055490;
CC -!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates the hydrophobic
CC ligand in its interior.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
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DR EMBL; AJ002962; CAA05773.1; -; mRNA.
DR EMBL; D88648; BAA23645.1; -; mRNA.
DR EMBL; U51338; AAB87141.1; -; mRNA.
DR EMBL; D50373; BAA23324.1; -; mRNA.
DR EMBL; U81235; AAD00507.1; -; mRNA.
DR EMBL; CR457057; CAG33338.1; -; mRNA.
DR EMBL; AK289836; BAF82525.1; -; mRNA.
DR EMBL; AK311867; BAG34808.1; -; mRNA.
DR EMBL; AL512688; CAC21646.1; -; mRNA.
DR EMBL; AL645811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48166.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48167.1; -; Genomic_DNA.
DR EMBL; BC012299; AAH12299.1; -; mRNA.
DR CCDS; CCDS5127.1; -. [O15540-1]
DR CCDS; CCDS83121.1; -. [O15540-2]
DR RefSeq; NP_001305968.1; NM_001319039.1. [O15540-2]
DR RefSeq; NP_001437.1; NM_001446.4. [O15540-1]
DR PDB; 1FDQ; X-ray; 2.10 A; A/B=2-132.
DR PDB; 1FE3; X-ray; 2.80 A; A=2-132.
DR PDB; 1JJX; NMR; -; A=2-132.
DR PDB; 5URA; X-ray; 1.85 A; A/B/C/D=1-132.
DR PDB; 6L9O; X-ray; 1.42 A; A=1-132.
DR PDB; 7E25; X-ray; 1.60 A; A=1-132.
DR PDBsum; 1FDQ; -.
DR PDBsum; 1FE3; -.
DR PDBsum; 1JJX; -.
DR PDBsum; 5URA; -.
DR PDBsum; 6L9O; -.
DR PDBsum; 7E25; -.
DR AlphaFoldDB; O15540; -.
DR BMRB; O15540; -.
DR SMR; O15540; -.
DR BioGRID; 108471; 14.
DR IntAct; O15540; 10.
DR STRING; 9606.ENSP00000357429; -.
DR BindingDB; O15540; -.
DR ChEMBL; CHEMBL3826863; -.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DR DrugBank; DB00159; Icosapent.
DR DrugBank; DB04224; Oleic Acid.
DR SwissLipids; SLP:000000498; -.
DR iPTMnet; O15540; -.
DR PhosphoSitePlus; O15540; -.
DR BioMuta; FABP7; -.
DR DOSAC-COBS-2DPAGE; O15540; -.
DR EPD; O15540; -.
DR jPOST; O15540; -.
DR MassIVE; O15540; -.
DR PaxDb; O15540; -.
DR PeptideAtlas; O15540; -.
DR PRIDE; O15540; -.
DR ProteomicsDB; 48748; -. [O15540-1]
DR ProteomicsDB; 80204; -.
DR Antibodypedia; 19513; 607 antibodies from 41 providers.
DR DNASU; 2173; -.
DR Ensembl; ENST00000356535.4; ENSP00000348931.4; ENSG00000164434.12. [O15540-2]
DR Ensembl; ENST00000368444.8; ENSP00000357429.3; ENSG00000164434.12. [O15540-1]
DR GeneID; 2173; -.
DR KEGG; hsa:2173; -.
DR MANE-Select; ENST00000368444.8; ENSP00000357429.3; NM_001446.5; NP_001437.1.
DR UCSC; uc003pzd.4; human. [O15540-1]
DR CTD; 2173; -.
DR DisGeNET; 2173; -.
DR GeneCards; FABP7; -.
DR HGNC; HGNC:3562; FABP7.
DR HPA; ENSG00000164434; Group enriched (brain, choroid plexus, retina, tongue).
DR MIM; 602965; gene.
DR neXtProt; NX_O15540; -.
DR OpenTargets; ENSG00000164434; -.
DR PharmGKB; PA27963; -.
DR VEuPathDB; HostDB:ENSG00000164434; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000156713; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; O15540; -.
DR OMA; KDDKMVM; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; O15540; -.
DR TreeFam; TF316894; -.
DR PathwayCommons; O15540; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR SignaLink; O15540; -.
DR SIGNOR; O15540; -.
DR BioGRID-ORCS; 2173; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; FABP7; human.
DR EvolutionaryTrace; O15540; -.
DR GeneWiki; FABP7; -.
DR GenomeRNAi; 2173; -.
DR Pharos; O15540; Tchem.
DR PRO; PR:O15540; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15540; protein.
DR Bgee; ENSG00000164434; Expressed in ventricular zone and 157 other tissues.
DR Genevisible; O15540; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; TAS:ProtInc.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000463; Fatty_acid-bd.
DR InterPro; IPR031259; ILBP.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11955; PTHR11955; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00178; FATTYACIDBP.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00214; FABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Lipid-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q09139"
FT CHAIN 2..132
FT /note="Fatty acid-binding protein, brain"
FT /id="PRO_0000067373"
FT BINDING 127..129
FT /ligand="a fatty acid"
FT /ligand_id="ChEBI:CHEBI:28868"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:Q09139"
FT VAR_SEQ 117..132
FT /note="TLTFGDVVAVRHYEKA -> VSNDNSPFFLVFFSSPHTSHLLPSSSLLLPFF
FT LLPSFFNNTSLARFFNYM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_055490"
FT VARIANT 61
FT /note="T -> M (in dbSNP:rs2279381)"
FT /id="VAR_049012"
FT CONFLICT 60
FT /note="N -> D (in Ref. 4; BAA23324)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="K -> R (in Ref. 6; CAG33338)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:6L9O"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6L9O"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6L9O"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1JJX"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:6L9O"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:6L9O"
SQ SEQUENCE 132 AA; 14889 MW; F1E8EE12B9474B97 CRC64;
MVEAFCATWK LTNSQNFDEY MKALGVGFAT RQVGNVTKPT VIISQEGDKV VIRTLSTFKN
TEISFQLGEE FDETTADDRN CKSVVSLDGD KLVHIQKWDG KETNFVREIK DGKMVMTLTF
GDVVAVRHYE KA
