ID AIF1L_HUMAN Reviewed; 150 AA. AC Q9BQI0; B2RBC4; Q6ZR40; Q8NAX7; Q8WU47; Q9H9G0; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 187. DE RecName: Full=Allograft inflammatory factor 1-like; DE AltName: Full=Ionized calcium-binding adapter molecule 2; GN Name=AIF1L; Synonyms=C9orf58, IBA2; ORFNames=UNQ672/PRO1306; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Kidney, Placenta, Teratocarcinoma, and Trachea; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Placenta; 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, RP LACK OF CALCIUM-BINDING, AND SUBUNIT. RX PubMed=18699778; DOI=10.1111/j.1742-4658.2008.06605.x; RA Schulze J.O., Quedenau C., Roske Y., Adam T., Schueler H., Behlke J., RA Turnbull A.P., Sievert V., Scheich C., Mueller U., Heinemann U., RA Buessow K.; RT "Structural and functional characterization of human Iba proteins."; RL FEBS J. 275:4627-4640(2008). CC -!- FUNCTION: Actin-binding protein that promotes actin bundling. May CC neither bind calcium nor depend on calcium for function. CC {ECO:0000269|PubMed:18699778}. CC -!- SUBUNIT: Homodimer (Potential). Monomer. {ECO:0000269|PubMed:18699778, CC ECO:0000305}. CC -!- INTERACTION: CC Q9BQI0-4; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-12351549, EBI-12039345; CC Q9BQI0-4; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-12351549, EBI-372432; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:18699778}. Cell projection, ruffle membrane CC {ECO:0000269|PubMed:18699778}; Peripheral membrane protein CC {ECO:0000269|PubMed:18699778}; Cytoplasmic side CC {ECO:0000269|PubMed:18699778}. Note=Colocalizes with F-actin. Partially CC relocates to membrane ruffles in response to invading bacteria. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BQI0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BQI0-2; Sequence=VSP_017150; CC Name=3; CC IsoId=Q9BQI0-3; Sequence=VSP_017151; CC Name=4; CC IsoId=Q9BQI0-4; Sequence=VSP_017152, VSP_017153; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL136566; CAB66501.1; -; mRNA. DR EMBL; AY359067; AAQ89426.1; -; mRNA. DR EMBL; AK022845; BAB14269.1; -; mRNA. DR EMBL; AK091912; BAC03770.1; -; mRNA. DR EMBL; AK128526; BAC87480.1; -; mRNA. DR EMBL; AK314600; BAG37171.1; -; mRNA. DR EMBL; AL833896; CAD38752.1; -; mRNA. DR EMBL; AL157938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87958.1; -; Genomic_DNA. DR EMBL; BC021253; AAH21253.1; -; mRNA. DR CCDS; CCDS55348.1; -. [Q9BQI0-2] DR CCDS; CCDS55349.1; -. [Q9BQI0-4] DR CCDS; CCDS6939.1; -. [Q9BQI0-1] DR RefSeq; NP_001172024.1; NM_001185095.1. [Q9BQI0-2] DR RefSeq; NP_001172025.1; NM_001185096.1. [Q9BQI0-4] DR RefSeq; NP_113614.1; NM_031426.3. [Q9BQI0-1] DR PDB; 2JJZ; X-ray; 2.15 A; B/C/D=1-150. DR PDB; 2VTG; X-ray; 2.45 A; A=1-150. DR PDBsum; 2JJZ; -. DR PDBsum; 2VTG; -. DR AlphaFoldDB; Q9BQI0; -. DR SMR; Q9BQI0; -. DR BioGRID; 123676; 57. DR IntAct; Q9BQI0; 9. DR MINT; Q9BQI0; -. DR STRING; 9606.ENSP00000361383; -. DR iPTMnet; Q9BQI0; -. DR PhosphoSitePlus; Q9BQI0; -. DR BioMuta; AIF1L; -. DR EPD; Q9BQI0; -. DR jPOST; Q9BQI0; -. DR MassIVE; Q9BQI0; -. DR MaxQB; Q9BQI0; -. DR PeptideAtlas; Q9BQI0; -. DR ProteomicsDB; 78678; -. [Q9BQI0-1] DR ProteomicsDB; 78679; -. [Q9BQI0-2] DR ProteomicsDB; 78680; -. [Q9BQI0-3] DR ProteomicsDB; 78681; -. [Q9BQI0-4] DR Pumba; Q9BQI0; -. DR TopDownProteomics; Q9BQI0-2; -. [Q9BQI0-2] DR Antibodypedia; 31561; 22 antibodies from 9 providers. DR DNASU; 83543; -. DR Ensembl; ENST00000247291.8; ENSP00000247291.3; ENSG00000126878.13. [Q9BQI0-1] DR Ensembl; ENST00000372300.5; ENSP00000361374.1; ENSG00000126878.13. [Q9BQI0-4] DR Ensembl; ENST00000372302.5; ENSP00000361376.1; ENSG00000126878.13. [Q9BQI0-3] DR Ensembl; ENST00000372309.7; ENSP00000361383.3; ENSG00000126878.13. [Q9BQI0-2] DR GeneID; 83543; -. DR KEGG; hsa:83543; -. DR MANE-Select; ENST00000247291.8; ENSP00000247291.3; NM_031426.4; NP_113614.1. DR UCSC; uc004cab.3; human. [Q9BQI0-1] DR AGR; HGNC:28904; -. DR CTD; 83543; -. DR DisGeNET; 83543; -. DR GeneCards; AIF1L; -. DR HGNC; HGNC:28904; AIF1L. DR HPA; ENSG00000126878; Tissue enhanced (brain, kidney, lymphoid tissue). DR neXtProt; NX_Q9BQI0; -. DR OpenTargets; ENSG00000126878; -. DR PharmGKB; PA164715250; -. DR VEuPathDB; HostDB:ENSG00000126878; -. DR GeneTree; ENSGT00390000013846; -. DR HOGENOM; CLU_134149_1_0_1; -. DR InParanoid; Q9BQI0; -. DR OMA; KILMFEE; -. DR OrthoDB; 6227at2759; -. DR PhylomeDB; Q9BQI0; -. DR TreeFam; TF320736; -. DR PathwayCommons; Q9BQI0; -. DR SignaLink; Q9BQI0; -. DR BioGRID-ORCS; 83543; 19 hits in 1152 CRISPR screens. DR ChiTaRS; AIF1L; human. DR EvolutionaryTrace; Q9BQI0; -. DR GeneWiki; C9orf58; -. DR GenomeRNAi; 83543; -. DR Pharos; Q9BQI0; Tbio. DR PRO; PR:Q9BQI0; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9BQI0; Protein. DR Bgee; ENSG00000126878; Expressed in renal medulla and 176 other cell types or tissues. DR ExpressionAtlas; Q9BQI0; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:LIFEdb. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central. DR GO; GO:0097178; P:ruffle assembly; IBA:GO_Central. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR049025; AIF-1_EF_pair. DR InterPro; IPR042433; AIF1/AIF1L. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR10356:SF5; ALLOGRAFT INFLAMMATORY FACTOR 1-LIKE; 1. DR PANTHER; PTHR10356; ALLOGRAFT INFLAMMATORY FACTOR-1; 1. DR Pfam; PF21008; AIF-1; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR Genevisible; Q9BQI0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane; KW Metal-binding; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT CHAIN 2..150 FT /note="Allograft inflammatory factor 1-like" FT /id="PRO_0000073870" FT DOMAIN 47..82 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 83..117 FT /note="EF-hand 2; degenerate" FT /evidence="ECO:0000305" FT REGION 129..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 60 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000305" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 31 FT /note="R -> RYCAGREPQLQRISCSQHSCLLALLFQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017150" FT VAR_SEQ 60..67 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017151" FT VAR_SEQ 99..102 FT /note="VSDT -> SHDV (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017152" FT VAR_SEQ 103..150 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017153" FT CONFLICT 33 FT /note="F -> L (in Ref. 3; BAB14269)" FT /evidence="ECO:0000305" FT HELIX 17..34 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 45..56 FT /evidence="ECO:0007829|PDB:2JJZ" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 69..78 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 85..96 FT /evidence="ECO:0007829|PDB:2JJZ" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 105..113 FT /evidence="ECO:0007829|PDB:2JJZ" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:2JJZ" FT HELIX 119..124 FT /evidence="ECO:0007829|PDB:2JJZ" SQ SEQUENCE 150 AA; 17068 MW; 74614436B9DEB5F6 CRC64; MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP //