FABP5_MOUSE
ID FABP5_MOUSE Reviewed; 135 AA.
AC Q05816;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Fatty acid-binding protein 5 {ECO:0000305};
DE AltName: Full=Epidermal-type fatty acid-binding protein;
DE Short=E-FABP;
DE AltName: Full=Fatty acid-binding protein, epidermal;
DE AltName: Full=Keratinocyte lipid-binding protein {ECO:0000303|PubMed:8608126};
DE AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
DE Short=PA-FABP;
GN Name=Fabp5 {ECO:0000312|MGI:MGI:101790};
GN Synonyms=Fabpe, Klbp, Mal1 {ECO:0000303|PubMed:8349619};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=8349619; DOI=10.1016/s0021-9258(19)85343-7;
RA Krieg P., Feil S., Fuerstenberger G., Bowden T.G.;
RT "Tumor-specific overexpression of a novel keratinocyte lipid-binding
RT protein. Identification and characterization of a cloned sequence activated
RT during multistage carcinogenesis in mouse skin.";
RL J. Biol. Chem. 268:17362-17369(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9666100; DOI=10.1016/s0378-1119(98)00262-5;
RA Bleck B., Hohoff C., Binas B., Rustow B., Dixkens C., Hameister H.,
RA Boerchers T., Spener F.;
RT "Cloning and chromosomal localisation of the murine epidermal-type fatty
RT acid binding protein gene (Fabpe).";
RL Gene 215:123-130(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9795232; DOI=10.1016/s0378-1119(98)00446-6;
RA Hertzel A.V., Bernlohr D.A.;
RT "Cloning and chromosomal location of the murine Keratinocyte lipid-binding
RT protein gene.";
RL Gene 221:235-243(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 13-24, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP SUBUNIT, AND FUNCTION.
RX PubMed=8608126; DOI=10.1021/bi952476e;
RA Kane C.D., Coe N.R., Vanlandingham B., Krieg P., Bernlohr D.A.;
RT "Expression, purification, and ligand-binding analysis of recombinant
RT keratinocyte lipid-binding protein (MAL-1), an intracellular lipid-binding
RT found overexpressed in neoplastic skin cells.";
RL Biochemistry 35:2894-2900(1996).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12540600; DOI=10.2337/diabetes.52.2.300;
RA Maeda K., Uysal K.T., Makowski L., Goerguen C.Z., Atsumi G., Parker R.A.,
RA Bruening J., Hertzel A.V., Bernlohr D.A., Hotamisligil G.S.;
RT "Role of the fatty acid binding protein mal1 in obesity and insulin
RT resistance.";
RL Diabetes 52:300-307(2003).
RN [9]
RP FUNCTION, LIGAND-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=17512406; DOI=10.1016/j.cell.2007.02.050;
RA Schug T.T., Berry D.C., Shaw N.S., Travis S.N., Noy N.;
RT "Opposing effects of retinoic acid on cell growth result from alternate
RT activation of two different nuclear receptors.";
RL Cell 129:723-733(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=29440395; DOI=10.1074/jbc.ra118.001593;
RA Bogdan D., Falcone J., Kanjiya M.P., Park S.H., Carbonetti G.,
RA Studholme K., Gomez M., Lu Y., Elmes M.W., Smietalo N., Yan S., Ojima I.,
RA Puopolo M., Kaczocha M.;
RT "Fatty acid-binding protein 5 controls microsomal prostaglandin E synthase
RT 1 (mPGES-1) induction during inflammation.";
RL J. Biol. Chem. 293:5295-5306(2018).
RN [12]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=29531087; DOI=10.1073/pnas.1721339115;
RA Haj-Dahmane S., Shen R.Y., Elmes M.W., Studholme K., Kanjiya M.P.,
RA Bogdan D., Thanos P.K., Miyauchi J.T., Tsirka S.E., Deutsch D.G.,
RA Kaczocha M.;
RT "Fatty-acid-binding protein 5 controls retrograde endocannabinoid signaling
RT at central glutamate synapses.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3482-3487(2018).
RN [13] {ECO:0007744|PDB:4AZN, ECO:0007744|PDB:4AZO, ECO:0007744|PDB:4AZP, ECO:0007744|PDB:4AZQ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH
RP N-ARACHIDONOYLETHANOLAMIDE AND 2-ARACHIDONOYLGLYCEROL, AND SUBUNIT.
RX PubMed=24531463; DOI=10.1107/s1399004713026795;
RA Sanson B., Wang T., Sun J., Wang L., Kaczocha M., Ojima I., Deutsch D.,
RA Li H.;
RT "Crystallographic study of FABP5 as an intracellular endocannabinoid
RT transporter.";
RL Acta Crystallogr. D 70:290-298(2014).
CC -!- FUNCTION: Intracellular carrier for long-chain fatty acids and related
CC active lipids, such as endocannabinoids, that regulate the metabolism
CC and actions of the ligands they bind (PubMed:8608126, PubMed:12540600).
CC In addition to the cytosolic transport, selectively delivers specific
CC fatty acids from the cytosol to the nucleus, wherein they activate
CC nuclear receptors (By similarity). Delivers retinoic acid to the
CC nuclear receptor peroxisome proliferator-activated receptor delta;
CC which promotes proliferation and survival (PubMed:17512406). May also
CC serve as a synaptic carrier of endocannabinoid at central synapses and
CC thus controls retrograde endocannabinoid signaling (PubMed:29531087).
CC Modulates inflammation by regulating PTGES induction via NF-kappa-B
CC activation, and prostaglandin E2 (PGE2) biosynthesis during
CC inflammation (PubMed:29440395). May be involved in keratinocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q01469,
CC ECO:0000269|PubMed:12540600, ECO:0000269|PubMed:17512406,
CC ECO:0000269|PubMed:29440395, ECO:0000269|PubMed:29531087,
CC ECO:0000269|PubMed:8608126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:Q01469};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8608126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17512406,
CC ECO:0000269|PubMed:29531087}. Nucleus {ECO:0000269|PubMed:17512406}.
CC Synapse {ECO:0000269|PubMed:29531087}. Postsynaptic density
CC {ECO:0000269|PubMed:29531087}. Secreted {ECO:0000269|PubMed:29531087}.
CC Note=Localizes primarily to the cytoplasm. Upon certain ligand binding,
CC a conformation change exposes a nuclear localization motif and the
CC protein is transported into nucleus (By similarity). Secreted by
CC astrocytes, but not by neurons (PubMed:29531087).
CC {ECO:0000250|UniProtKB:Q01469, ECO:0000269|PubMed:29531087}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8349619}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display resistance to diet-induced
CC obesity, decreased adipose tissue and imporved glucose tolerance and
CC insulin sensitivity. {ECO:0000269|PubMed:12540600}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC protein (FABP) family. {ECO:0000305}.
CC -!- CAUTION: While human FABP5 can exist as a monomer as well as a domain-
CC swapped dimer, mouse is found only in the monomeric form.
CC {ECO:0000269|PubMed:24531463}.
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DR EMBL; X70100; CAA49703.1; -; mRNA.
DR EMBL; AJ223066; CAA11069.1; -; Genomic_DNA.
DR EMBL; AF061015; AAC82368.1; -; Genomic_DNA.
DR EMBL; AF061014; AAC82368.1; JOINED; Genomic_DNA.
DR EMBL; AK008782; BAB25890.1; -; mRNA.
DR EMBL; AK011551; BAB27692.1; -; mRNA.
DR EMBL; BC002008; AAH02008.1; -; mRNA.
DR CCDS; CCDS38388.1; -.
DR PIR; A47497; A47497.
DR RefSeq; NP_034764.1; NM_010634.3.
DR PDB; 4AZN; X-ray; 2.51 A; A/B=1-135.
DR PDB; 4AZO; X-ray; 2.33 A; A=1-135.
DR PDB; 4AZP; X-ray; 2.10 A; A=1-135.
DR PDB; 4AZQ; X-ray; 2.00 A; A=1-135.
DR PDBsum; 4AZN; -.
DR PDBsum; 4AZO; -.
DR PDBsum; 4AZP; -.
DR PDBsum; 4AZQ; -.
DR AlphaFoldDB; Q05816; -.
DR SMR; Q05816; -.
DR BioGRID; 200959; 4.
DR IntAct; Q05816; 1.
DR STRING; 10090.ENSMUSP00000029046; -.
DR BindingDB; Q05816; -.
DR CarbonylDB; Q05816; -.
DR iPTMnet; Q05816; -.
DR PhosphoSitePlus; Q05816; -.
DR SwissPalm; Q05816; -.
DR REPRODUCTION-2DPAGE; Q05816; -.
DR UCD-2DPAGE; Q05816; -.
DR CPTAC; non-CPTAC-3645; -.
DR EPD; Q05816; -.
DR jPOST; Q05816; -.
DR PaxDb; Q05816; -.
DR PeptideAtlas; Q05816; -.
DR PRIDE; Q05816; -.
DR ProteomicsDB; 275844; -.
DR Antibodypedia; 25313; 411 antibodies from 37 providers.
DR DNASU; 16592; -.
DR Ensembl; ENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
DR GeneID; 16592; -.
DR KEGG; mmu:16592; -.
DR UCSC; uc008opg.2; mouse.
DR CTD; 2171; -.
DR MGI; MGI:101790; Fabp5.
DR VEuPathDB; HostDB:ENSMUSG00000027533; -.
DR eggNOG; KOG4015; Eukaryota.
DR GeneTree; ENSGT00940000154530; -.
DR HOGENOM; CLU_113772_0_0_1; -.
DR InParanoid; Q05816; -.
DR OMA; MGGMAKP; -.
DR OrthoDB; 1417203at2759; -.
DR PhylomeDB; Q05816; -.
DR TreeFam; TF316894; -.
DR Reactome; R-MMU-163560; Triglyceride catabolism.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16592; 3 hits in 55 CRISPR screens.
DR ChiTaRS; Fabp5; mouse.
DR PRO; PR:Q05816; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q05816; protein.
DR Bgee; ENSMUSG00000027533; Expressed in esophagus and 142 other tissues.
DR ExpressionAtlas; Q05816; baseline and differential.
DR Genevisible; Q05816; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0001972; F:retinoic acid binding; IDA:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISO:MGI.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IMP:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IGI:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0031392; P:regulation of prostaglandin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
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; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lipid transport; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT CHAIN 2..135
FT /note="Fatty acid-binding protein 5"
FT /id="PRO_0000067378"
FT MOTIF 24..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 43
FT /ligand="1-eicosanoylglycerol"
FT /ligand_id="ChEBI:CHEBI:142495"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZQ"
FT BINDING 56
FT /ligand="1-eicosanoylglycerol"
FT /ligand_id="ChEBI:CHEBI:142495"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZQ"
FT BINDING 109
FT /ligand="1-eicosanoylglycerol"
FT /ligand_id="ChEBI:CHEBI:142495"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZQ"
FT BINDING 129..131
FT /ligand="(9Z,12Z)-octadecadienoate"
FT /ligand_id="ChEBI:CHEBI:30245"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 129..131
FT /ligand="1-eicosanoylglycerol"
FT /ligand_id="ChEBI:CHEBI:142495"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZP, ECO:0007744|PDB:4AZQ"
FT BINDING 131
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT BINDING 131
FT /ligand="N-eicosanoyl ethanolamine"
FT /ligand_id="ChEBI:CHEBI:85253"
FT /evidence="ECO:0000269|PubMed:24531463,
FT ECO:0007744|PDB:4AZP"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55053"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT DISULFID 120..127
FT /evidence="ECO:0000250|UniProtKB:Q01469"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:4AZQ"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:4AZQ"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4AZQ"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4AZQ"
SQ SEQUENCE 135 AA; 15137 MW; 6A6C8DBEBB046185 CRC64;
MASLKDLEGK WRLMESHGFE EYMKELGVGL ALRKMAAMAK PDCIITCDGN NITVKTESTV
KTTVFSCNLG EKFDETTADG RKTETVCTFQ DGALVQHQQW DGKESTITRK LKDGKMIVEC
VMNNATCTRV YEKVQ
