AIF1L_HUMAN
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 03-AUG-2022, entry version 179.
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;
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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; 38.
DR IntAct; Q9BQI0; 6.
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 PRIDE; Q9BQI0; -.
DR ProteomicsDB; 78678; -. [Q9BQI0-1]
DR ProteomicsDB; 78679; -. [Q9BQI0-2]
DR ProteomicsDB; 78680; -. [Q9BQI0-3]
DR ProteomicsDB; 78681; -. [Q9BQI0-4]
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 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; 1557466at2759; -.
DR PhylomeDB; Q9BQI0; -.
DR TreeFam; TF320736; -.
DR PathwayCommons; Q9BQI0; -.
DR SignaLink; Q9BQI0; -.
DR BioGRID-ORCS; 83543; 19 hits in 1076 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 174 other tissues.
DR ExpressionAtlas; Q9BQI0; baseline and differential.
DR Genevisible; Q9BQI0; HS.
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 InterPro; IPR028453; Aif1-like.
DR InterPro; IPR042433; AIF1/AIF1L.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10356; PTHR10356; 1.
DR PANTHER; PTHR10356:SF5; PTHR10356:SF5; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
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
