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Apoptosis-inducing factor 1, mitochondrial (EC 1.1.1.-) (Programmed cell death protein 8)

 AIFM1_HUMAN             Reviewed;         613 AA.
O95831; A4QPB4; B1ALN1; B2RB08; D3DTE9; Q1L6K4; Q1L6K6; Q2QKE4;
Q5JUZ7; Q6I9X6; Q9Y3I3; Q9Y3I4;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
10-OCT-2018, entry version 195.
RecName: Full=Apoptosis-inducing factor 1, mitochondrial;
EC=1.1.1.-;
AltName: Full=Programmed cell death protein 8;
Flags: Precursor;
Name=AIFM1; Synonyms=AIF, PDCD8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9989411; DOI=10.1038/17135;
Susin S.A., Lorenzo H.K., Zamzami N., Marzo I., Snow B.E.,
Brothers G.M., Mangion J., Jacotot E., Costantini P., Loeffler M.,
Larochette N., Goodlett D.R., Aebersold R., Siderovski D.P.,
Penninger J.M., Kroemer G.;
"Molecular characterization of mitochondrial apoptosis-inducing
factor.";
Nature 397:441-446(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF
N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 5), AND TISSUE SPECIFICITY.
PubMed=16365034; DOI=10.1074/jbc.M509884200;
Delettre C., Yuste V.J., Moubarak R.S., Bras M.,
Lesbordes-Brion J.-C., Petres S., Bellalou J., Susin S.A.;
"AIFsh, a novel apoptosis-inducing factor (AIF) pro-apoptotic isoform
with potential pathological relevance in human cancer.";
J. Biol. Chem. 281:6413-6427(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), AND ALTERNATIVE
SPLICING.
PubMed=16644725; DOI=10.1074/jbc.M601751200;
Delettre C., Yuste V.J., Moubarak R.S., Bras M., Robert N.,
Susin S.A.;
"Identification and characterization of AIFsh2, a mitochondrial
apoptosis-inducing factor (AIF) isoform with NADH oxidase activity.";
J. Biol. Chem. 281:18507-18518(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Rhodes S.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 55-59, SUBCELLULAR LOCATION, AND PROTEOLYTIC
CLEAVAGE.
PubMed=15775970; DOI=10.1038/sj.emboj.7600614;
Otera H., Ohsakaya S., Nagaura Z., Ishihara N., Mihara K.;
"Export of mitochondrial AIF in response to proapoptotic stimuli
depends on processing at the intermembrane space.";
EMBO J. 24:1375-1386(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-613.
TISSUE=Brain;
Mei G., Yu W., Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[12]
REVIEW.
PubMed=10913597; DOI=10.1016/S0014-5793(00)01731-2;
Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N.,
Kroemer G.;
"Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial
oxidoreductase involved in apoptosis.";
FEBS Lett. 476:118-123(2000).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF3G.
PubMed=17094969; DOI=10.1016/j.febslet.2006.10.049;
Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W.,
Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.;
"Apoptosis-inducing factor (AIF) inhibits protein synthesis by
interacting with the eukaryotic translation initiation factor 3
subunit p44 (eIF3g).";
FEBS Lett. 580:6375-6383(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
UBIQUITINATION BY XIAP/BIRC4, AND INTERACTION WITH XIAP/BIRC4.
PubMed=17967870; DOI=10.1128/MCB.01065-07;
Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S.;
"Apoptosis-inducing factor is a target for ubiquitination through
interaction with XIAP.";
Mol. Cell. Biol. 28:237-247(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
FUNCTION.
PubMed=19418225; DOI=10.1007/s10495-009-0353-7;
Son Y.O., Jang Y.S., Heo J.S., Chung W.T., Choi K.C., Lee J.C.;
"Apoptosis-inducing factor plays a critical role in caspase-
independent, pyknotic cell death in hydrogen peroxide-exposed cells.";
Apoptosis 14:796-808(2009).
[18]
ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3),
AND SUBUNIT.
PubMed=20111043; DOI=10.1038/cdd.2009.211;
Hangen E., De Zio D., Bordi M., Zhu C., Dessen P., Caffin F.,
Lachkar S., Perfettini J.L., Lazar V., Benard J., Fimia G.M.,
Piacentini M., Harper F., Pierron G., Vicencio J.M., Benit P.,
de Andrade A., Hoglinger G., Culmsee C., Rustin P., Blomgren K.,
Cecconi F., Kroemer G., Modjtahedi N.;
"A brain-specific isoform of mitochondrial apoptosis-inducing factor:
AIF2.";
Cell Death Differ. 17:1155-1166(2010).
[19]
INTERACTION WITH PRELID1.
PubMed=21364629; DOI=10.1038/cddis.2009.19;
McKeller M.R., Herrera-Rodriguez S., Ma W., Ortiz-Quintero B.,
Rangel R., Cande C., Sims-Mourtada J.C., Melnikova V., Kashi C.,
Phan L.M., Chen Z., Huang P., Dunner K. Jr., Kroemer G., Singh K.K.,
Martinez-Valdez H.;
"Vital function of PRELI and essential requirement of its LEA motif.";
Cell Death Dis. 1:E21-E21(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
UBIQUITINATION AT LYS-255 BY XIAP/BIRC4.
PubMed=22103349; DOI=10.1021/bi201483g;
Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C.;
"Nondegradative ubiquitination of apoptosis inducing factor (AIF) by
X-linked inhibitor of apoptosis at a residue critical for AIF-mediated
chromatin degradation.";
Biochemistry 50:11084-11096(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105; SER-116; SER-268
AND SER-292, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-268;
SER-371; THR-521; SER-524 AND SER-530, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-54, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-613 IN COMPLEX WITH FAD,
SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=12198487; DOI=10.1038/nsb836;
Ye H., Cande C., Stephanou N.C., Jiang S., Gurbuxani S.,
Larochette N., Daugas E., Garrido C., Kroemer G., Wu H.;
"DNA binding is required for the apoptogenic action of apoptosis
inducing factor.";
Nat. Struct. Biol. 9:680-684(2002).
[26]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 103-613 IN COMPLEX WITH FAD,
FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DNA-BINDING,
SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT COWCK
VAL-493, AND CHARACTERIZATION OF VARIANT COWCK VAL-493.
PubMed=23217327; DOI=10.1016/j.ajhg.2012.10.008;
Rinaldi C., Grunseich C., Sevrioukova I.F., Schindler A.,
Horkayne-Szakaly I., Lamperti C., Landoure G., Kennerson M.L.,
Burnett B.G., Boennemann C., Biesecker L.G., Ghezzi D., Zeviani M.,
Fischbeck K.H.;
"Cowchock syndrome is associated with a mutation in apoptosis-inducing
factor.";
Am. J. Hum. Genet. 91:1095-1102(2012).
[27]
VARIANT COXPD6 ARG-201 DEL, CHARACTERIZATION OF VARIANT COXPD6 ARG-201
DEL, AND FUNCTION.
PubMed=20362274; DOI=10.1016/j.ajhg.2010.03.002;
Ghezzi D., Sevrioukova I., Invernizzi F., Lamperti C., Mora M.,
D'Adamo P., Novara F., Zuffardi O., Uziel G., Zeviani M.;
"Severe X-linked mitochondrial encephalomyopathy associated with a
mutation in apoptosis-inducing factor.";
Am. J. Hum. Genet. 86:639-649(2010).
[28]
VARIANT COXPD6 GLU-308.
PubMed=22019070; DOI=10.1016/j.ymgme.2011.09.020;
Berger I., Ben-Neriah Z., Dor-Wolman T., Shaag A., Saada A.,
Zenvirt S., Raas-Rothschild A., Nadjari M., Kaestner K.H., Elpeleg O.;
"Early prenatal ventriculomegaly due to an AIFM1 mutation identified
by linkage analysis and whole exome sequencing.";
Mol. Genet. Metab. 104:517-520(2011).
[29]
INVOLVEMENT IN DFNX5, AND VARIANTS DFNX5 ALA-260; PHE-344; ARG-360;
GLN-422; TRP-422; CYS-430; GLN-451; VAL-472; LEU-475; MET-498 AND
MET-591.
PubMed=25986071; DOI=10.1136/jmedgenet-2014-102961;
Zong L., Guan J., Ealy M., Zhang Q., Wang D., Wang H., Zhao Y.,
Shen Z., Campbell C.A., Wang F., Yang J., Sun W., Lan L., Ding D.,
Xie L., Qi Y., Lou X., Huang X., Shi Q., Chang S., Xiong W., Yin Z.,
Yu N., Zhao H., Wang J., Wang J., Salvi R.J., Petit C., Smith R.J.,
Wang Q.;
"Mutations in apoptosis-inducing factor cause X-linked recessive
auditory neuropathy spectrum disorder.";
J. Med. Genet. 52:523-531(2015).
[30]
VARIANT LEU-243, AND CHARACTERIZATION OF VARIANT LEU-243.
PubMed=25583628; DOI=10.1016/j.mito.2015.01.001;
Kettwig M., Schubach M., Zimmermann F.A., Klinge L., Mayr J.A.,
Biskup S., Sperl W., Gaertner J., Huppke P.;
"From ventriculomegaly to severe muscular atrophy: Expansion of the
clinical spectrum related to mutations in AIFM1.";
Mitochondrion 21C:12-18(2015).
-!- FUNCTION: Functions both as NADH oxidoreductase and as regulator
of apoptosis. In response to apoptotic stimuli, it is released
from the mitochondrion intermembrane space into the cytosol and to
the nucleus, where it functions as a proapoptotic factor in a
caspase-independent pathway. In contrast, functions as an
antiapoptotic factor in normal mitochondria via its NADH
oxidoreductase activity. The soluble form (AIFsol) found in the
nucleus induces 'parthanatos' i.e. caspase-independent
fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby
inhibits the EIF3 machinery and protein synthesis, and activates
casapse-7 to amplify apoptosis. Plays a critical role in caspase-
independent, pyknotic cell death in hydrogen peroxide-exposed
cells. Binds to DNA in a sequence-independent manner.
{ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225,
ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:23217327};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.53 mM for NADH {ECO:0000269|PubMed:23217327};
KM=26 uM for cytochrome c {ECO:0000269|PubMed:23217327};
-!- SUBUNIT: Monomer (oxidized form). Homodimer (reduced form). Also
dimerizes with isoform 3 preventing its release from mitochondria.
Interacts with XIAP/BIRC4. Interacts (via N-terminus) with EIF3G
(via C-terminus). Interacts with PRELID1.
{ECO:0000269|PubMed:12198487, ECO:0000269|PubMed:17094969,
ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:20111043,
ECO:0000269|PubMed:21364629, ECO:0000269|PubMed:23217327}.
-!- INTERACTION:
O75821:EIF3G; NbExp=9; IntAct=EBI-356440, EBI-366632;
Q63ZY3:KANK2; NbExp=2; IntAct=EBI-356440, EBI-2556193;
Q63ZY3-2:KANK2; NbExp=4; IntAct=EBI-356440, EBI-6244894;
Q9Y3Q8:TSC22D4; NbExp=2; IntAct=EBI-356440, EBI-739485;
-!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
Mitochondrion inner membrane. Cytoplasm. Nucleus. Cytoplasm,
perinuclear region. Note=Proteolytic cleavage during or just after
translocation into the mitochondrial intermembrane space (IMS)
results in the formation of an inner-membrane-anchored mature form
(AIFmit). During apoptosis, further proteolytic processing leads
to a mature form, which is confined to the mitochondrial IMS in a
soluble form (AIFsol). AIFsol is released to the cytoplasm in
response to specific death signals, and translocated to the
nucleus, where it induces nuclear apoptosis. Colocalizes with
EIF3G in the nucleus and perinuclear region.
-!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion intermembrane space
{ECO:0000269|PubMed:20111043}. Mitochondrion inner membrane
{ECO:0000269|PubMed:20111043}. Note=Has a stronger membrane
anchorage than isoform 1.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
{ECO:0000269|PubMed:16365034}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=AIF;
IsoId=O95831-1; Sequence=Displayed;
Name=2;
IsoId=O95831-2; Sequence=VSP_004357;
Name=3; Synonyms=AIF-exB, AIF2;
IsoId=O95831-3; Sequence=VSP_022953;
Note=Brain-specific.;
Name=4; Synonyms=AIFsh2;
IsoId=O95831-4; Sequence=VSP_043637, VSP_043638;
Note=Does not induce nuclear apoptosis.;
Name=5; Synonyms=AIFsh;
IsoId=O95831-5; Sequence=VSP_046248;
Note=Pro-apoptotic isoform, strongly down-regulated in many
tumor cells, up-regulated by gamma-irradiation.;
Name=6;
IsoId=O95831-6; Sequence=VSP_047646, VSP_043637, VSP_043638;
-!- TISSUE SPECIFICITY: Detected in muscle and skin fibroblasts (at
protein level). Isoform 5 is frequently down-regulated in human
cancers. {ECO:0000269|PubMed:16365034,
ECO:0000269|PubMed:23217327}.
-!- PTM: Under normal conditions, a 54-residue N-terminal segment is
first proteolytically removed during or just after translocation
into the mitochondrial intermembrane space (IMS) by the
mitochondrial processing peptidase (MPP) to form the inner-
membrane-anchored mature form (AIFmit). During apoptosis, it is
further proteolytically processed at amino-acid position 101
leading to the generation of the mature form, which is confined to
the mitochondrial IMS in a soluble form (AIFsol). AIFsol is
released to the cytoplasm in response to specific death signals,
and translocated to the nucleus, where it induces nuclear
apoptosis in a caspase-independent manner.
{ECO:0000269|PubMed:15775970}.
-!- PTM: Ubiquitination by XIAP/BIRC4 does not lead to proteasomal
degradation. Ubiquitination at Lys-255 by XIAP/BIRC4 blocks its
ability to bind DNA and induce chromatin degradation, thereby
inhibiting its ability to induce cell death.
{ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:22103349}.
-!- DISEASE: Combined oxidative phosphorylation deficiency 6 (COXPD6)
[MIM:300816]: A mitochondrial disease resulting in a
neurodegenerative disorder characterized by psychomotor delay,
hypotonia, areflexia, muscle weakness and wasting. Some patients
manifest prenatal ventriculomegaly and severe postnatal
encephalomyopathy. {ECO:0000269|PubMed:20362274,
ECO:0000269|PubMed:22019070}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cowchock syndrome (COWCK) [MIM:310490]: An X-linked
recessive neuromuscular disorder characterized by early childhood
onset of a slowly progressive axonal sensorimotor neuropathy
associated in some patients with sensorineural deafness and
cognitive impairment. {ECO:0000269|PubMed:23217327}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Deafness, X-linked, 5 (DFNX5) [MIM:300614]: A form of
hearing loss characterized by absent or severely abnormal auditory
brainstem response, abnormal middle ear reflexes, abnormal speech
discrimination, loss of outer hair cell function, and cochlear
nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with
childhood onset, associated with distal sensory impairment
affecting the peripheral nervous system.
{ECO:0000269|PubMed:25986071}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AIFM1ID44053chXq25.html";
-----------------------------------------------------------------------
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EMBL; AF100928; AAD16436.1; -; mRNA.
EMBL; DQ016496; AAY84737.1; -; mRNA.
EMBL; DQ016498; AAY84739.1; -; mRNA.
EMBL; DQ016500; AAY84741.1; -; mRNA.
EMBL; AL049703; CAB41267.1; -; mRNA.
EMBL; AL049704; CAB41268.1; -; mRNA.
EMBL; AK314446; BAG37055.1; -; mRNA.
EMBL; CR457379; CAG33660.1; -; mRNA.
EMBL; AL139234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471107; EAX11811.1; -; Genomic_DNA.
EMBL; CH471107; EAX11812.1; -; Genomic_DNA.
EMBL; CH471107; EAX11810.1; -; Genomic_DNA.
EMBL; BC111065; AAI11066.1; -; mRNA.
EMBL; BC139738; AAI39739.1; -; mRNA.
EMBL; AF131759; AAD20036.1; -; mRNA.
CCDS; CCDS14618.1; -. [O95831-1]
CCDS; CCDS14619.1; -. [O95831-3]
CCDS; CCDS48167.1; -. [O95831-4]
RefSeq; NP_001124318.2; NM_001130846.3.
RefSeq; NP_001124319.1; NM_001130847.3. [O95831-4]
RefSeq; NP_004199.1; NM_004208.3. [O95831-1]
RefSeq; NP_665811.1; NM_145812.2. [O95831-3]
UniGene; Hs.424932; -.
PDB; 1M6I; X-ray; 1.80 A; A=121-613.
PDB; 4BUR; X-ray; 2.88 A; A/B/C/D=103-613.
PDB; 4BV6; X-ray; 1.80 A; A=121-613.
PDB; 4FDC; X-ray; 2.40 A; B=103-613.
PDB; 4LII; X-ray; 1.88 A; A=100-611.
PDB; 5FMH; X-ray; 1.80 A; A=104-613.
PDB; 5FS6; X-ray; 1.90 A; A/B=103-613.
PDB; 5FS7; X-ray; 1.85 A; A/B=103-613.
PDB; 5FS8; X-ray; 1.40 A; A=103-613.
PDB; 5FS9; X-ray; 1.75 A; A/B=103-613.
PDB; 5KVH; X-ray; 2.27 A; A/B=78-613.
PDB; 5KVI; X-ray; 2.00 A; A=78-613.
PDBsum; 1M6I; -.
PDBsum; 4BUR; -.
PDBsum; 4BV6; -.
PDBsum; 4FDC; -.
PDBsum; 4LII; -.
PDBsum; 5FMH; -.
PDBsum; 5FS6; -.
PDBsum; 5FS7; -.
PDBsum; 5FS8; -.
PDBsum; 5FS9; -.
PDBsum; 5KVH; -.
PDBsum; 5KVI; -.
ProteinModelPortal; O95831; -.
SMR; O95831; -.
BioGrid; 114579; 112.
CORUM; O95831; -.
DIP; DIP-32975N; -.
IntAct; O95831; 228.
MINT; O95831; -.
STRING; 9606.ENSP00000287295; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB05282; MCC.
CarbonylDB; O95831; -.
iPTMnet; O95831; -.
PhosphoSitePlus; O95831; -.
SwissPalm; O95831; -.
BioMuta; AIFM1; -.
REPRODUCTION-2DPAGE; IPI00157908; -.
UCD-2DPAGE; O95831; -.
EPD; O95831; -.
MaxQB; O95831; -.
PaxDb; O95831; -.
PeptideAtlas; O95831; -.
PRIDE; O95831; -.
ProteomicsDB; 51073; -.
ProteomicsDB; 51074; -. [O95831-2]
ProteomicsDB; 51075; -. [O95831-3]
ProteomicsDB; 51076; -. [O95831-4]
DNASU; 51060; -.
Ensembl; ENST00000287295; ENSP00000287295; ENSG00000156709. [O95831-1]
Ensembl; ENST00000319908; ENSP00000315122; ENSG00000156709. [O95831-3]
Ensembl; ENST00000346424; ENSP00000316320; ENSG00000156709. [O95831-2]
Ensembl; ENST00000416073; ENSP00000402535; ENSG00000156709. [O95831-4]
Ensembl; ENST00000535724; ENSP00000446113; ENSG00000156709. [O95831-4]
GeneID; 9131; -.
KEGG; hsa:9131; -.
UCSC; uc004evg.4; human. [O95831-1]
CTD; 9131; -.
DisGeNET; 9131; -.
EuPathDB; HostDB:ENSG00000156709.13; -.
GeneCards; AIFM1; -.
HGNC; HGNC:8768; AIFM1.
HPA; CAB003764; -.
HPA; HPA030611; -.
MalaCards; AIFM1; -.
MIM; 300169; gene.
MIM; 300614; phenotype.
MIM; 300816; phenotype.
MIM; 310490; phenotype.
neXtProt; NX_O95831; -.
OpenTargets; ENSG00000156709; -.
Orphanet; 238329; Severe X-linked mitochondrial encephalomyopathy.
Orphanet; 101078; X-linked Charcot-Marie-Tooth disease type 4.
PharmGKB; PA162376129; -.
eggNOG; KOG1346; Eukaryota.
eggNOG; COG0446; LUCA.
GeneTree; ENSGT00530000063416; -.
HOGENOM; HOG000124580; -.
HOVERGEN; HBG056326; -.
InParanoid; O95831; -.
KO; K04727; -.
OMA; CFYDIRL; -.
OrthoDB; EOG091G05ST; -.
PhylomeDB; O95831; -.
TreeFam; TF314028; -.
SABIO-RK; O95831; -.
SignaLink; O95831; -.
SIGNOR; O95831; -.
ChiTaRS; AIFM1; human.
EvolutionaryTrace; O95831; -.
GeneWiki; AIFM1; -.
GenomeRNAi; 9131; -.
PRO; PR:O95831; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000156709; Expressed in 213 organ(s), highest expression level in apex of heart.
CleanEx; HS_AIFM1; -.
ExpressionAtlas; O95831; baseline and differential.
Genevisible; O95831; HS.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0071949; F:FAD binding; IEA:Ensembl.
GO; GO:0016174; F:NAD(P)H oxidase activity; TAS:UniProtKB.
GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:1904045; P:cellular response to aldosterone; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl.
GO; GO:0030261; P:chromosome condensation; TAS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 5.
InterPro; IPR029324; AIF_C.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
Pfam; PF14721; AIF_C; 1.
Pfam; PF07992; Pyr_redox_2; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF55424; SSF55424; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm; Deafness;
Direct protein sequencing; Disease mutation; DNA-binding; FAD;
Flavoprotein; Isopeptide bond; Membrane; Mental retardation;
Mitochondrion; Mitochondrion inner membrane; NAD; Neurodegeneration;
Neuropathy; Nucleus; Oxidoreductase; Phosphoprotein;
Primary mitochondrial disease; Reference proteome; Transit peptide;
Ubl conjugation.
TRANSIT 1 54 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:15775970,
ECO:0000269|PubMed:16365034}.
PROPEP 55 101 Removed in mature form.
{ECO:0000269|PubMed:16365034}.
/FTId=PRO_0000401935.
CHAIN 102 613 Apoptosis-inducing factor 1,
mitochondrial.
/FTId=PRO_0000022030.
NP_BIND 138 142 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
NP_BIND 164 165 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
NP_BIND 454 455 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
REGION 134 483 FAD-dependent oxidoreductase.
{ECO:0000250}.
MOTIF 446 451 Nuclear localization signal.
{ECO:0000255}.
BINDING 172 172 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
BINDING 177 177 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
BINDING 233 233 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
BINDING 285 285 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
BINDING 438 438 FAD. {ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
BINDING 483 483 FAD; via carbonyl oxygen.
{ECO:0000269|PubMed:12198487,
ECO:0000269|PubMed:23217327}.
MOD_RES 105 105 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 109 109 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z0X1}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 388 388 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z0X1}.
MOD_RES 521 521 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 593 593 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z0X1}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22103349}.
VAR_SEQ 1 352 Missing (in isoform 5).
{ECO:0000303|PubMed:16365034}.
/FTId=VSP_046248.
VAR_SEQ 1 87 Missing (in isoform 6).
{ECO:0000303|PubMed:16644725}.
/FTId=VSP_047646.
VAR_SEQ 36 322 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_004357.
VAR_SEQ 36 82 GNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLS
TVGAGA -> VVQSHHLGSPSRSLASTGASGKDGSNLVYFL
IVGATVTGAGVY (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_022953.
VAR_SEQ 323 324 AR -> DI (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:16644725}.
/FTId=VSP_043637.
VAR_SEQ 325 613 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:16644725}.
/FTId=VSP_043638.
VARIANT 201 201 Missing (in COXPD6; higher DNA binding
affinity, partially impaired flavin
binding and association with increased
parthanatos-linked cell death).
{ECO:0000269|PubMed:20362274}.
/FTId=VAR_063827.
VARIANT 243 243 V -> L (probable disease-associated
mutation found in patient with severe
myopathy; myopathic changes with partial
type II fiber hypotrophy; reduced protein
amount in muscle compared to controls).
{ECO:0000269|PubMed:25583628}.
/FTId=VAR_072791.
VARIANT 260 260 T -> A (in DFNX5; dbSNP:rs863225432).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076211.
VARIANT 308 308 G -> E (in COXPD6; with prenatal
ventriculomegaly and severe postnatal
encephalomyopathy).
{ECO:0000269|PubMed:22019070}.
/FTId=VAR_067334.
VARIANT 344 344 L -> F (in DFNX5; unknown pathological
significance; dbSNP:rs184474885).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076212.
VARIANT 360 360 G -> R (in DFNX5; unknown pathological
significance; dbSNP:rs724160026).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076213.
VARIANT 422 422 R -> Q (in DFNX5; dbSNP:rs724160021).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076214.
VARIANT 422 422 R -> W (in DFNX5; dbSNP:rs724160020).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076215.
VARIANT 430 430 R -> C (in DFNX5; unknown pathological
significance).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076216.
VARIANT 451 451 R -> Q (in DFNX5; dbSNP:rs863225431).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076217.
VARIANT 472 472 A -> V (in DFNX5; unknown pathological
significance).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076218.
VARIANT 475 475 P -> L (in DFNX5; unknown pathological
significance; dbSNP:rs724160022).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076219.
VARIANT 493 493 E -> V (in COWCK; increases affinity for
NADH and electron transfer activity;
increases affinity for DNA, resulting in
increased apoptosis; dbSNP:rs281864468).
{ECO:0000269|PubMed:23217327}.
/FTId=VAR_069468.
VARIANT 498 498 V -> M (in DFNX5; unknown pathological
significance; dbSNP:rs724160023).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076220.
VARIANT 591 591 I -> M (in DFNX5; unknown pathological
significance).
{ECO:0000269|PubMed:25986071}.
/FTId=VAR_076221.
STRAND 130 138 {ECO:0000244|PDB:5FS8}.
HELIX 141 153 {ECO:0000244|PDB:5FS8}.
STRAND 158 162 {ECO:0000244|PDB:5FS8}.
STRAND 164 167 {ECO:0000244|PDB:5FS8}.
HELIX 173 176 {ECO:0000244|PDB:5FS8}.
HELIX 178 180 {ECO:0000244|PDB:5FS8}.
HELIX 187 190 {ECO:0000244|PDB:5FS8}.
STRAND 192 194 {ECO:0000244|PDB:5FS8}.
STRAND 200 206 {ECO:0000244|PDB:5FS8}.
HELIX 208 210 {ECO:0000244|PDB:5FS8}.
TURN 214 219 {ECO:0000244|PDB:5FS8}.
STRAND 224 228 {ECO:0000244|PDB:5FS8}.
STRAND 233 237 {ECO:0000244|PDB:5FS8}.
TURN 238 241 {ECO:0000244|PDB:5FS8}.
STRAND 242 245 {ECO:0000244|PDB:5FS8}.
STRAND 250 258 {ECO:0000244|PDB:5FS8}.
STRAND 262 264 {ECO:0000244|PDB:5FS8}.
HELIX 268 271 {ECO:0000244|PDB:5FS8}.
HELIX 275 279 {ECO:0000244|PDB:5FS8}.
STRAND 281 283 {ECO:0000244|PDB:5FS8}.
HELIX 287 299 {ECO:0000244|PDB:5FS8}.
STRAND 301 306 {ECO:0000244|PDB:5FS8}.
HELIX 310 326 {ECO:0000244|PDB:5FS8}.
STRAND 329 333 {ECO:0000244|PDB:5FS8}.
STRAND 335 338 {ECO:0000244|PDB:5FS8}.
TURN 339 343 {ECO:0000244|PDB:5FS8}.
HELIX 346 358 {ECO:0000244|PDB:5FS8}.
STRAND 362 364 {ECO:0000244|PDB:5FS8}.
STRAND 369 375 {ECO:0000244|PDB:5FS8}.
STRAND 378 383 {ECO:0000244|PDB:5FS8}.
STRAND 388 396 {ECO:0000244|PDB:5FS8}.
STRAND 400 402 {ECO:0000244|PDB:5FS8}.
HELIX 407 410 {ECO:0000244|PDB:5FS8}.
TURN 416 418 {ECO:0000244|PDB:5FS8}.
STRAND 420 422 {ECO:0000244|PDB:5FS8}.
STRAND 427 430 {ECO:0000244|PDB:5FS8}.
STRAND 433 435 {ECO:0000244|PDB:5FS8}.
HELIX 437 439 {ECO:0000244|PDB:5FS8}.
STRAND 440 444 {ECO:0000244|PDB:5FS8}.
TURN 445 447 {ECO:0000244|PDB:5FS8}.
STRAND 448 450 {ECO:0000244|PDB:5FS8}.
HELIX 455 468 {ECO:0000244|PDB:5FS8}.
TURN 469 471 {ECO:0000244|PDB:5FS8}.
STRAND 481 487 {ECO:0000244|PDB:5FS8}.
STRAND 491 496 {ECO:0000244|PDB:5FS8}.
STRAND 504 509 {ECO:0000244|PDB:5FS8}.
STRAND 513 515 {ECO:0000244|PDB:4BUR}.
HELIX 517 524 {ECO:0000244|PDB:5FS8}.
HELIX 529 533 {ECO:0000244|PDB:5FS8}.
STRAND 538 542 {ECO:0000244|PDB:5KVI}.
STRAND 562 569 {ECO:0000244|PDB:5FS8}.
STRAND 572 580 {ECO:0000244|PDB:5FS8}.
HELIX 585 594 {ECO:0000244|PDB:5FS8}.
HELIX 601 605 {ECO:0000244|PDB:5FS8}.
HELIX 606 608 {ECO:0000244|PDB:5FS8}.
SEQUENCE 613 AA; 66901 MW; A156762BC64E6340 CRC64;
MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPGNLFQ RWHVPLELQM TRQMASSGAS
GGKIDNSVLV LIVGLSTVGA GAYAYKTMKE DEKRYNERIS GLGLTPEQKQ KKAALSASEG
EEVPQDKAPS HVPFLLIGGG TAAFAAARSI RARDPGARVL IVSEDPELPY MRPPLSKELW
FSDDPNVTKT LRFKQWNGKE RSIYFQPPSF YVSAQDLPHI ENGGVAVLTG KKVVQLDVRD
NMVKLNDGSQ ITYEKCLIAT GGTPRSLSAI DRAGAEVKSR TTLFRKIGDF RSLEKISREV
KSITIIGGGF LGSELACALG RKARALGTEV IQLFPEKGNM GKILPEYLSN WTMEKVRREG
VKVMPNAIVQ SVGVSSGKLL IKLKDGRKVE TDHIVAAVGL EPNVELAKTG GLEIDSDFGG
FRVNAELQAR SNIWVAGDAA CFYDIKLGRR RVEHHDHAVV SGRLAGENMT GAAKPYWHQS
MFWSDLGPDV GYEAIGLVDS SLPTVGVFAK ATAQDNPKSA TEQSGTGIRS ESETESEASE
ITIPPSTPAV PQAPVQGEDY GKGVIFYLRD KVVVGIVLWN IFNRMPIARK IIKDGEQHED
LNEVAKLFNI HED


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