ID FANCA_HUMAN Reviewed; 1455 AA. AC O15360; A5D923; B4DRI7; H3BSR5; O75266; Q6PL10; Q92497; Q96H18; Q9UEA5; AC Q9UEL8; Q9UEL9; Q9UPK3; Q9Y6M2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Fanconi anemia group A protein; DE Short=Protein FACA; GN Name=FANCA; Synonyms=FAA, FACA, FANCH; 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), AND VARIANTS SER-501 AND ILE-717. RC TISSUE=Lymphoblast; RX PubMed=8896563; DOI=10.1038/ng1196-320; RA Lo Ten Foe J.R., Rooimans M.A., Bosnoyan-Collins L., Alon N., Wijker M., RA Parker L., Lightfoot J., Carreau M., Callen D.F., Savoia A., Cheng N.C., RA van Berkel C.G.M., Strunk M.H.P., Gille J.J.P., Pals G., Kruyt F.A.E., RA Pronk J.C., Arwert F., Buchwald M., Joenje H.; RT "Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA."; RL Nat. Genet. 14:320-323(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-501. RX PubMed=9169126; DOI=10.1006/geno.1997.4675; RA Ianzano L., D'Apolito M., Centra M., Savino M., Levran O., Auerbach A.D., RA Cleton-Jansen A.-M., Doggett N.A., Pronk J.C., Tipping A.J., Gibson R.A., RA Mathew C.G., Whitmore S.A., Apostolou S., Callen F.C., Zelante L., RA Savoia A.; RT "The genomic organization of the Fanconi anemia group A (FAA) gene."; RL Genomics 41:309-314(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RA Ricke D.O., Bruce D., Mundt M., Doggett N., Munk C., Saunders E., RA Robinson D., Jones M., Buckingham J., Chasteen L., Thompson S., Goodwin L., RA Bryant J., Tesmer J., Meincke L., Longmire J., White S., Ueng S., Tatum O., RA Campbell C., Fawcett J., Maltbie M., Deaven L.; RT "Sequencing of human Fanconi anemia complementation group A gene genomic RT region."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-266; SER-501 AND RP ASP-809. RG NIEHS SNPs program; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-717. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-266. RC TISSUE=Cervix; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 491-571 AND 610-671, AND VARIANT RP SER-501. RX PubMed=9721219; DOI=10.1006/geno.1998.5353; RA Centra M., Memeo E., D'Apolito M., Savino M., Ianzano L., Notarangelo A., RA Liu J., Doggett N.A., Zelante L., Savoia A.; RT "Fine exon-intron structure of the Fanconi anemia group A (FAA) gene and RT characterization of two genomic deletions."; RL Genomics 51:463-467(1998). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 491-542. RX PubMed=9711872; RX DOI=10.1002/(sici)1098-1004(1998)12:3<145::aid-humu2>3.0.co;2-g; RA Levran O., Doggett N.A., Auerbach A.D.; RT "Identification of Alu-mediated deletions in the Fanconi anemia gene FAA."; RL Hum. Mutat. 12:145-152(1998). RN [10] RP SUBCELLULAR LOCATION, AND MUTAGENESIS. RX PubMed=9742112; DOI=10.1128/mcb.18.10.5952; RA Naef D., Kupfer G.M., Suliman A., Lambert K., D'Andrea A.D.; RT "Functional activity of the Fanconi anemia protein FAA requires FAC binding RT and nuclear localization."; RL Mol. Cell. Biol. 18:5952-5960(1998). RN [11] RP IDENTIFICATION IN A COMPLEX WITH FANCC; FANCE; FANCF; FANCG AND FANCL. RX PubMed=12724401; DOI=10.1128/mcb.23.10.3417-3426.2003; RA Meetei A.R., Sechi S., Wallisch M., Yang D., Young M.K., Joenje H., RA Hoatlin M.E., Wang W.; RT "A multiprotein nuclear complex connects Fanconi anemia and Bloom RT syndrome."; RL Mol. Cell. Biol. 23:3417-3426(2003). RN [12] RP PHOSPHORYLATION. RX PubMed=9789045; DOI=10.1073/pnas.95.22.13085; RA Yamashita T., Kupfer G.M., Naf D., Suliman A., Joenje H., Asano S., RA D'Andrea A.D.; RT "The Fanconi anemia pathway requires FAA phosphorylation and FAA/FAC RT nuclear accumulation."; RL Proc. Natl. Acad. Sci. U.S.A. 95:13085-13090(1998). RN [13] RP IDENTIFICATION IN A COMPLEX WITH EIF2AK2; FANCC; FANCG AND HSP70. RX PubMed=15299030; DOI=10.1074/jbc.m403884200; RA Zhang X., Li J., Sejas D.P., Rathbun K.R., Bagby G.C., Pang Q.; RT "The Fanconi anemia proteins functionally interact with the protein kinase RT regulated by RNA (PKR)."; RL J. Biol. Chem. 279:43910-43919(2004). RN [14] RP IDENTIFICATION IN A COMPLEX WITH FANCB; FANCC; FANCE; FANCF; FANCG AND RP FANCL. RX PubMed=15502827; DOI=10.1038/ng1458; RA Meetei A.R., Levitus M., Xue Y., Medhurst A.L., Zwaan M., Ling C., RA Rooimans M.A., Bier P., Hoatlin M., Pals G., de Winter J.P., Wang W., RA Joenje H.; RT "X-linked inheritance of Fanconi anemia complementation group B."; RL Nat. Genet. 36:1219-1224(2004). RN [15] RP IDENTIFICATION IN A COMPLEX WITH FANCB; FANCC; FANCE; FANCF; FANCG; FANCL RP AND FANCM. RX PubMed=16116422; DOI=10.1038/ng1626; RA Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P., RA Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H., RA de Winter J.P., Wang W.; RT "A human ortholog of archaeal DNA repair protein Hef is defective in RT Fanconi anemia complementation group M."; RL Nat. Genet. 37:958-963(2005). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1449, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [17] RP INTERACTION WITH HES1, AND SUBCELLULAR LOCATION. RX PubMed=18550849; DOI=10.1182/blood-2008-04-152710; RA Tremblay C.S., Huang F.F., Habi O., Huard C.C., Godin C., Levesque G., RA Carreau M.; RT "HES1 is a novel interactor of the Fanconi anemia core complex."; RL Blood 112:2062-2070(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1449, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [19] RP IDENTIFICATION IN THE FA COMPLEX, AND INTERACTION WITH C1ORF86. RX PubMed=22343915; DOI=10.1182/blood-2011-10-385963; RA Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K., Grassman E., RA Auerbach A.D., Pang Q., Meetei A.R.; RT "FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required RT for functional integrity of the FA-BRCA DNA repair pathway."; RL Blood 119:3285-3294(2012). RN [20] RP IDENTIFICATION IN THE FA COMPLEX, AND INTERACTION WITH C1ORF86. RX PubMed=22705371; DOI=10.1016/j.molcel.2012.05.026; RA Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y., RA Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E., Schindler D., RA Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.; RT "A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to RT the Fanconi anemia DNA repair network."; RL Mol. Cell 47:61-75(2012). RN [21] RP IDENTIFICATION IN THE FA COMPLEX. RX PubMed=22266823; DOI=10.1038/nsmb.2222; RA Kim H., Yang K., Dejsuphong D., D'Andrea A.D.; RT "Regulation of Rev1 by the Fanconi anemia core complex."; RL Nat. Struct. Mol. Biol. 19:164-170(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1449, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [23] RP VARIANT FANCA TYR-1359, AND VARIANTS ALA-266; SER-501 AND ASP-809. RX PubMed=9399890; DOI=10.1086/301632; RA Savino M., Ianzano L., Strippoli P., Ramenghi U., Arslanian A., RA Bagnara G.P., Joenje H., Zelante L., Savoia A.; RT "Mutations of the Fanconi anemia group A gene (FAA) in Italian patients."; RL Am. J. Hum. Genet. 61:1246-1253(1997). RN [24] RP VARIANTS FANCA PHE-244; CYS-435; ARG-492; PRO-817; PRO-845; LEU-1055; RP GLY-1117; GLU-1128; ALA-1131; PHE-1263 DEL; ARG-1302 AND ASP-1417, AND RP VARIANTS LYS-8; VAL-181; GLY-252; SER-501; LEU-739; ASP-809 AND ALA-1328. RX PubMed=9371798; DOI=10.1073/pnas.94.24.13051; RA Levran O., Erlich T., Magdalena N., Gregory J.J., Batish S.D., RA Verlander P.C., Auerbach A.D.; RT "Sequence variation in the Fanconi anemia gene FAA."; RL Proc. Natl. Acad. Sci. U.S.A. 94:13051-13056(1997). RN [25] RP VARIANTS FANCA ASN-598; PRO-1110; LEU-1262; PHE-1263 DEL; LEU-1324 AND RP ILE-1360. RX PubMed=10521298; DOI=10.1086/302627; RA Morgan N.V., Tipping A.J., Joenje H., Mathew C.G.; RT "High frequency of large intragenic deletions in the Fanconi anemia group A RT gene."; RL Am. J. Hum. Genet. 65:1330-1341(1999). RN [26] RP VARIANTS FANCA ASN-598; ARG-858 AND PHE-1088. RX PubMed=10094191; DOI=10.1038/sj.ejhg.5200248; RA Wijker M., Morgan N.V., Herterich S., van Berkel C.G., Tipping A.J., RA Gross H.J., Gille J.J., Pals G., Savino M., Altay C., Mohan S., Dokal I., RA Cavenagh J., Marsh J., van Weel M., Ortega J.J., Schuler D., RA Samochatova E., Karwacki M., Bekassy A.N., Abecasis M., Ebell W., RA Kwee M.L., de Ravel T., Mathew C.G.; RT "Heterogeneous spectrum of mutations in the Fanconi anaemia group A gene."; RL Eur. J. Hum. Genet. 7:52-59(1999). RN [27] RP VARIANTS FANCA PRO-1110 AND GLY-1117, AND CHARACTERIZATION OF VARIANT FANCA RP PRO-1110. RX PubMed=10210316; DOI=10.1016/s0301-472x(99)00022-3; RA Kupfer G., Naef D., Garcia-Higuera I., Wasik J., Cheng A., Yamashita T., RA Tipping A., Morgan N., Mathew C.G., D'Andrea A.D.; RT "A patient-derived mutant form of the Fanconi anemia protein, FANCA, is RT defective in nuclear accumulation."; RL Exp. Hematol. 27:587-593(1999). RN [28] RP VARIANT FANCA TRP-1055. RX PubMed=9929978; DOI=10.1007/s100380050106; RA Nakamura A., Matsuura S., Tauchi H., Hanada R., Ohashi H., Hasegawa T., RA Honda K., Masuno M., Imaizumi K., Sugita K., Ide T., Komatsu K.; RT "Four novel mutations of the Fanconi anemia group A gene (FAA) in Japanese RT patients."; RL J. Hum. Genet. 44:48-51(1999). RN [29] RP VARIANT FANCA ARG-858. RX PubMed=11091222; DOI=10.1046/j.1365-2141.2000.02323.x; RA Tamary H., Bar-Yam R., Shalmon L., Rachavi G., Krostichevsky M., RA Elhasid R., Barak Y., Kapelushnik J., Yaniv I., Auerbach A.D., Zaizov R.; RT "Fanconi anaemia group A (FANCA) mutations in Israeli non-Ashkenazi Jewish RT patients."; RL Br. J. Haematol. 111:338-343(2000). RN [30] RP VARIANT FANCA PRO-1082. RX PubMed=10807541; DOI=10.1007/s100380050203; RA Yamada T., Tachibana A., Shimizu T., Mugishima H., Okubo M., Sasaki M.S.; RT "Novel mutations of the FANCG gene causing alternative splicing in Japanese RT Fanconi anemia."; RL J. Hum. Genet. 45:159-166(2000). RN [31] RP VARIANTS FANCA ARG-210; PRO-660; ASP-843; PRO-869; PRO-1249; LEU-1324; RP THR-1346 AND HIS-1400, AND VARIANTS GLU-761; GLN-951; TRP-951 AND ALA-1131. RX PubMed=17924555; DOI=10.1002/humu.20625; RA Ameziane N., Errami A., Leveille F., Fontaine C., de Vries Y., RA van Spaendonk R.M., de Winter J.P., Pals G., Joenje H.; RT "Genetic subtyping of Fanconi anemia by comprehensive mutation screening."; RL Hum. Mutat. 29:159-166(2008). RN [32] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-266; VAL-412; SER-501; ASP-809 AND RP PHE-1088. RX PubMed=18987736; DOI=10.1038/nature07485; RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., RA DiPersio J.F., Wilson R.K.; RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia RT genome."; RL Nature 456:66-72(2008). CC -!- FUNCTION: DNA repair protein that may operate in a postreplication CC repair or a cell cycle checkpoint function. May be involved in CC interstrand DNA cross-link repair and in the maintenance of normal CC chromosome stability. CC -!- SUBUNIT: Belongs to the multisubunit FA complex composed of FANCA, CC FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is CC not found in FA patients. In complex with FANCF, FANCG and FANCL, but CC not with FANCC, nor FANCE, interacts with HES1; this interaction may be CC essential for the stability and nuclear localization of FA core complex CC proteins. The complex with FANCC and FANCG may also include EIF2AK2 and CC HSP70. Interacts with FAAP20/C1orf86; interaction is direct. CC {ECO:0000269|PubMed:12724401, ECO:0000269|PubMed:15299030, CC ECO:0000269|PubMed:15502827, ECO:0000269|PubMed:16116422, CC ECO:0000269|PubMed:18550849, ECO:0000269|PubMed:22266823, CC ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22705371}. CC -!- INTERACTION: CC O15360; Q0VG06: FAAP100; NbExp=3; IntAct=EBI-81570, EBI-2557990; CC O15360; Q6NZ36-1: FAAP20; NbExp=5; IntAct=EBI-81570, EBI-15965017; CC O15360; Q9NPI8: FANCF; NbExp=5; IntAct=EBI-81570, EBI-81589; CC O15360; O15287: FANCG; NbExp=13; IntAct=EBI-81570, EBI-81610; CC O15360; P62993: GRB2; NbExp=2; IntAct=EBI-81570, EBI-401755; CC O15360-3; O15287: FANCG; NbExp=5; IntAct=EBI-21315382, EBI-81610; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The major form is CC nuclear. The minor form is cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O15360-1; Sequence=Displayed; CC Name=2; CC IsoId=O15360-2; Sequence=VSP_007039; CC Name=3; CC IsoId=O15360-3; Sequence=VSP_054682; CC -!- PTM: Phosphorylation is required for the formation of the nuclear CC complex. Not phosphorylated in cells derived from groups A, B, C, E, F, CC G, and H. {ECO:0000269|PubMed:9789045}. CC -!- DISEASE: Fanconi anemia, complementation group A (FANCA) [MIM:227650]: CC A disorder affecting all bone marrow elements and resulting in anemia, CC leukopenia and thrombopenia. It is associated with cardiac, renal and CC limb malformations, dermal pigmentary changes, and a predisposition to CC the development of malignancies. At the cellular level it is associated CC with hypersensitivity to DNA-damaging agents, chromosomal instability CC (increased chromosome breakage) and defective DNA repair. CC {ECO:0000269|PubMed:10094191, ECO:0000269|PubMed:10210316, CC ECO:0000269|PubMed:10521298, ECO:0000269|PubMed:10807541, CC ECO:0000269|PubMed:11091222, ECO:0000269|PubMed:17924555, CC ECO:0000269|PubMed:9371798, ECO:0000269|PubMed:9399890, CC ECO:0000269|PubMed:9929978}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/102/FA1"; CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database; CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpa"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/fanca/"; 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; X99226; CAA67610.1; -; mRNA. DR EMBL; Z83067; CAB05445.1; -; Genomic_DNA. DR EMBL; Z83068; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83069; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83070; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83071; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83072; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83073; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83074; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83075; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83076; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83077; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83078; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83079; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83080; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83081; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83082; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83083; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83084; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83085; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83086; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83087; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83088; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83089; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83090; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83091; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83092; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83093; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83094; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83095; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; Z83151; CAB05445.1; JOINED; Genomic_DNA. DR EMBL; AK299282; BAG61299.1; -; mRNA. DR EMBL; AC005360; AAC28751.1; -; Genomic_DNA. DR EMBL; AC005565; AAC33304.1; -; Genomic_DNA. DR EMBL; AC005567; AAC33401.1; -; Genomic_DNA. DR EMBL; AY598423; AAS99350.1; -; Genomic_DNA. DR EMBL; AC092385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008979; AAH08979.1; -; mRNA. DR EMBL; BC141972; AAI41973.1; -; mRNA. DR EMBL; AJ225084; CAA12393.1; -; Genomic_DNA. DR EMBL; AJ225085; CAA12394.1; -; Genomic_DNA. DR EMBL; AF054569; AAC28331.1; -; Genomic_DNA. DR CCDS; CCDS32515.1; -. [O15360-1] DR CCDS; CCDS42221.1; -. [O15360-2] DR CCDS; CCDS67099.1; -. [O15360-3] DR PIR; T02755; T02755. DR RefSeq; NP_000126.2; NM_000135.2. [O15360-1] DR RefSeq; NP_001018122.1; NM_001018112.1. [O15360-2] DR RefSeq; NP_001273096.1; NM_001286167.1. [O15360-3] DR PDB; 7KZP; EM; 3.10 A; A/S=1-1455. DR PDB; 7KZQ; EM; 4.20 A; A/S=1-1455. DR PDB; 7KZR; EM; 4.20 A; A/S=1-1455. DR PDB; 7KZS; EM; 4.20 A; A/S=1-1455. DR PDB; 7KZT; EM; 4.20 A; A/S=1-1455. DR PDB; 7KZV; EM; 4.20 A; A/S=1-1455. DR PDBsum; 7KZP; -. DR PDBsum; 7KZQ; -. DR PDBsum; 7KZR; -. DR PDBsum; 7KZS; -. DR PDBsum; 7KZT; -. DR PDBsum; 7KZV; -. DR AlphaFoldDB; O15360; -. DR EMDB; EMD-23085; -. DR EMDB; EMD-23086; -. DR EMDB; EMD-23087; -. DR EMDB; EMD-23088; -. DR EMDB; EMD-23089; -. DR EMDB; EMD-23090; -. DR SMR; O15360; -. DR BioGRID; 108472; 191. DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex. DR CORUM; O15360; -. DR DIP; DIP-32650N; -. DR IntAct; O15360; 27. DR MINT; O15360; -. DR STRING; 9606.ENSP00000373952; -. DR MoonDB; O15360; Predicted. DR GlyGen; O15360; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O15360; -. DR PhosphoSitePlus; O15360; -. DR BioMuta; FANCA; -. DR CPTAC; CPTAC-3226; -. DR EPD; O15360; -. DR jPOST; O15360; -. DR MassIVE; O15360; -. DR MaxQB; O15360; -. DR PaxDb; 9606-ENSP00000373952; -. DR PeptideAtlas; O15360; -. DR ProteomicsDB; 42431; -. DR ProteomicsDB; 48611; -. [O15360-1] DR ProteomicsDB; 48612; -. [O15360-2] DR Pumba; O15360; -. DR Antibodypedia; 30916; 471 antibodies from 39 providers. DR DNASU; 2175; -. DR Ensembl; ENST00000389301.8; ENSP00000373952.3; ENSG00000187741.16. [O15360-1] DR Ensembl; ENST00000389302.7; ENSP00000373953.3; ENSG00000187741.16. [O15360-2] DR Ensembl; ENST00000568369.6; ENSP00000456829.1; ENSG00000187741.16. [O15360-3] DR Ensembl; ENST00000696275.1; ENSP00000512517.1; ENSG00000187741.16. [O15360-2] DR GeneID; 2175; -. DR KEGG; hsa:2175; -. DR MANE-Select; ENST00000389301.8; ENSP00000373952.3; NM_000135.4; NP_000126.2. DR UCSC; uc002fou.2; human. [O15360-1] DR AGR; HGNC:3582; -. DR CTD; 2175; -. DR DisGeNET; 2175; -. DR GeneCards; FANCA; -. DR GeneReviews; FANCA; -. DR HGNC; HGNC:3582; FANCA. DR HPA; ENSG00000187741; Tissue enhanced (testis). DR MalaCards; FANCA; -. DR MIM; 227650; phenotype. DR MIM; 607139; gene. DR neXtProt; NX_O15360; -. DR OpenTargets; ENSG00000187741; -. DR Orphanet; 84; Fanconi anemia. DR PharmGKB; PA27995; -. DR VEuPathDB; HostDB:ENSG00000187741; -. DR eggNOG; ENOG502QT8N; Eukaryota. DR GeneTree; ENSGT00390000007852; -. DR HOGENOM; CLU_005268_0_0_1; -. DR InParanoid; O15360; -. DR OMA; AIPHCPA; -. DR OrthoDB; 5400084at2759; -. DR PhylomeDB; O15360; -. DR TreeFam; TF333412; -. DR PathwayCommons; O15360; -. DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; O15360; -. DR SIGNOR; O15360; -. DR BioGRID-ORCS; 2175; 110 hits in 1170 CRISPR screens. DR ChiTaRS; FANCA; human. DR GeneWiki; FANCA; -. DR GenomeRNAi; 2175; -. DR Pharos; O15360; Tbio. DR PRO; PR:O15360; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O15360; Protein. DR Bgee; ENSG00000187741; Expressed in right testis and 116 other cell types or tissues. DR ExpressionAtlas; O15360; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0008585; P:female gonad development; IEA:Ensembl. DR GO; GO:0036297; P:interstrand cross-link repair; NAS:ComplexPortal. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:2000348; P:regulation of CD40 signaling pathway; IEA:Ensembl. DR GO; GO:1905936; P:regulation of germ cell proliferation; IEA:Ensembl. DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IBA:GO_Central. DR InterPro; IPR003516; FANCA. DR InterPro; IPR031729; Fanconi_A_N. DR PANTHER; PTHR12047; FANCONI ANEMIA GROUP A PROTEIN; 1. DR PANTHER; PTHR12047:SF2; FANCONI ANEMIA GROUP A PROTEIN; 1. DR Pfam; PF03511; Fanconi_A; 1. DR Pfam; PF15865; Fanconi_A_N; 1. DR PRINTS; PR00826; FANCONIAGENE. DR Genevisible; O15360; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; DNA damage; KW DNA repair; Fanconi anemia; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..1455 FT /note="Fanconi anemia group A protein" FT /id="PRO_0000087179" FT MOTIF 18..34 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOD_RES 1449 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT VAR_SEQ 298..1455 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007039" FT VAR_SEQ 1390..1455 FT /note="GNPVELITKARLFLLQLIPRCPKKSFSHVAELLADRGDCDPEVSAALQSRQQ FT AAPDADLSQEPHLF -> AGQPRGTDNKSSSFSAAVNTSVPEKELLTRGRAAG (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054682" FT VARIANT 6 FT /note="V -> D (in dbSNP:rs1800282)" FT /id="VAR_009637" FT VARIANT 8 FT /note="N -> K (in FANCA; benign; dbSNP:rs76275444)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009638" FT VARIANT 131 FT /note="T -> S (in dbSNP:rs34491278)" FT /id="VAR_050982" FT VARIANT 176 FT /note="S -> F (in dbSNP:rs35566151)" FT /id="VAR_050983" FT VARIANT 181 FT /note="A -> V (in FANCA; benign; dbSNP:rs17232246)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009639" FT VARIANT 210 FT /note="L -> R (in FANCA; dbSNP:rs2040601073)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038012" FT VARIANT 244 FT /note="L -> F (in FANCA; dbSNP:rs2040522671)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009640" FT VARIANT 252 FT /note="D -> G (in FANCA; benign; dbSNP:rs17225943)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009641" FT VARIANT 266 FT /note="T -> A (in dbSNP:rs7190823)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18987736, ECO:0000269|PubMed:9399890, FT ECO:0000269|Ref.4" FT /id="VAR_017496" FT VARIANT 277 FT /note="A -> G (in dbSNP:rs35880318)" FT /id="VAR_050984" FT VARIANT 286 FT /note="Q -> R (in dbSNP:rs13336566)" FT /id="VAR_050985" FT VARIANT 412 FT /note="A -> V (in dbSNP:rs11646374)" FT /evidence="ECO:0000269|PubMed:18987736" FT /id="VAR_050986" FT VARIANT 435 FT /note="R -> C (in FANCA; dbSNP:rs148473140)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009642" FT VARIANT 492 FT /note="H -> R (in FANCA; dbSNP:rs925457555)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009643" FT VARIANT 501 FT /note="G -> S (in dbSNP:rs2239359)" FT /evidence="ECO:0000269|PubMed:18987736, FT ECO:0000269|PubMed:8896563, ECO:0000269|PubMed:9169126, FT ECO:0000269|PubMed:9371798, ECO:0000269|PubMed:9399890, FT ECO:0000269|PubMed:9721219, ECO:0000269|Ref.4" FT /id="VAR_009644" FT VARIANT 598 FT /note="D -> N (in FANCA; dbSNP:rs2039605345)" FT /evidence="ECO:0000269|PubMed:10094191, FT ECO:0000269|PubMed:10521298" FT /id="VAR_017497" FT VARIANT 643 FT /note="P -> A (in dbSNP:rs17232910)" FT /id="VAR_050987" FT VARIANT 660 FT /note="L -> P (in FANCA; dbSNP:rs1567621042)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038013" FT VARIANT 717 FT /note="M -> I (in dbSNP:rs1131660)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:8896563" FT /id="VAR_061649" FT VARIANT 739 FT /note="P -> L (in dbSNP:rs45441106)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009645" FT VARIANT 761 FT /note="V -> E (in dbSNP:rs2039276663)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038014" FT VARIANT 809 FT /note="G -> D (in dbSNP:rs7195066)" FT /evidence="ECO:0000269|PubMed:18987736, FT ECO:0000269|PubMed:9371798, ECO:0000269|PubMed:9399890, FT ECO:0000269|Ref.4" FT /id="VAR_009646" FT VARIANT 817 FT /note="L -> P (in FANCA)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009647" FT VARIANT 843 FT /note="Y -> D (in FANCA; dbSNP:rs374030577)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038015" FT VARIANT 845 FT /note="L -> P (in FANCA; dbSNP:rs1173704265)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009648" FT VARIANT 858 FT /note="S -> R (in FANCA; dbSNP:rs17233141)" FT /evidence="ECO:0000269|PubMed:10094191, FT ECO:0000269|PubMed:11091222" FT /id="VAR_017498" FT VARIANT 869 FT /note="Q -> P (in FANCA; dbSNP:rs780825099)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038016" FT VARIANT 951 FT /note="R -> Q (in dbSNP:rs755922289)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038017" FT VARIANT 951 FT /note="R -> W (in dbSNP:rs755546887)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038018" FT VARIANT 1055 FT /note="R -> L (in FANCA; dbSNP:rs1429943036)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009649" FT VARIANT 1055 FT /note="R -> W (in FANCA; dbSNP:rs753063086)" FT /evidence="ECO:0000269|PubMed:9929978" FT /id="VAR_017499" FT VARIANT 1082 FT /note="L -> P (in FANCA)" FT /evidence="ECO:0000269|PubMed:10807541" FT /id="VAR_017500" FT VARIANT 1088 FT /note="S -> F (in FANCA; benign; dbSNP:rs17233497)" FT /evidence="ECO:0000269|PubMed:10094191, FT ECO:0000269|PubMed:18987736" FT /id="VAR_017501" FT VARIANT 1110 FT /note="H -> P (in FANCA; loss of function)" FT /evidence="ECO:0000269|PubMed:10210316, FT ECO:0000269|PubMed:10521298" FT /id="VAR_009650" FT VARIANT 1117 FT /note="R -> G (in FANCA; dbSNP:rs149277003)" FT /evidence="ECO:0000269|PubMed:10210316, FT ECO:0000269|PubMed:9371798" FT /id="VAR_009651" FT VARIANT 1128 FT /note="Q -> E (in FANCA; dbSNP:rs1439817346)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009652" FT VARIANT 1131 FT /note="T -> A (in FANCA; dbSNP:rs574034197)" FT /evidence="ECO:0000269|PubMed:17924555, FT ECO:0000269|PubMed:9371798" FT /id="VAR_009653" FT VARIANT 1249 FT /note="L -> P (in FANCA; dbSNP:rs753316789)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038019" FT VARIANT 1262 FT /note="F -> L (in FANCA; dbSNP:rs1555534579)" FT /evidence="ECO:0000269|PubMed:10521298" FT /id="VAR_017502" FT VARIANT 1263 FT /note="Missing (in FANCA)" FT /evidence="ECO:0000269|PubMed:10521298, FT ECO:0000269|PubMed:9371798" FT /id="VAR_009654" FT VARIANT 1287 FT /note="V -> I (in dbSNP:rs17227354)" FT /id="VAR_009655" FT VARIANT 1302 FT /note="W -> R (in FANCA; dbSNP:rs878853665)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009656" FT VARIANT 1324 FT /note="P -> L (in FANCA; dbSNP:rs182657062)" FT /evidence="ECO:0000269|PubMed:10521298, FT ECO:0000269|PubMed:17924555" FT /id="VAR_017505" FT VARIANT 1328 FT /note="T -> A (in dbSNP:rs9282681)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009657" FT VARIANT 1346 FT /note="A -> T (in FANCA; likely benign; dbSNP:rs17227396)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038020" FT VARIANT 1359 FT /note="D -> Y (in FANCA; dbSNP:rs1555533313)" FT /evidence="ECO:0000269|PubMed:9399890" FT /id="VAR_017503" FT VARIANT 1360 FT /note="M -> I (in FANCA; dbSNP:rs1555533300)" FT /evidence="ECO:0000269|PubMed:10521298" FT /id="VAR_017504" FT VARIANT 1400 FT /note="R -> H (in FANCA; dbSNP:rs149851163)" FT /evidence="ECO:0000269|PubMed:17924555" FT /id="VAR_038021" FT VARIANT 1417 FT /note="H -> D (in FANCA; dbSNP:rs17227403)" FT /evidence="ECO:0000269|PubMed:9371798" FT /id="VAR_009658" SQ SEQUENCE 1455 AA; 162775 MW; 5A1918F2BEF4BC50 CRC64; MSDSWVPNSA SGQDPGGRRR AWAELLAGRV KREKYNPERA QKLKESAVRL LRSHQDLNAL LLEVEGPLCK KLSLSKVIDC DSSEAYANHS SSFIGSALQD QASRLGVPVG ILSAGMVASS VGQICTAPAE TSHPVLLTVE QRKKLSSLLE FAQYLLAHSM FSRLSFCQEL WKIQSSLLLE AVWHLHVQGI VSLQELLESH PDMHAVGSWL FRNLCCLCEQ MEASCQHADV ARAMLSDFVQ MFVLRGFQKN SDLRRTVEPE KMPQVTVDVL QRMLIFALDA LAAGVQEESS THKIVRCWFG VFSGHTLGSV ISTDPLKRFF SHTLTQILTH SPVLKASDAV QMQREWSFAR THPLLTSLYR RLFVMLSAEE LVGHLQEVLE TQEVHWQRVL SFVSALVVCF PEAQQLLEDW VARLMAQAFE SCQLDSMVTA FLVVRQAALE GPSAFLSYAD WFKASFGSTR GYHGCSKKAL VFLFTFLSEL VPFESPRYLQ VHILHPPLVP GKYRSLLTDY ISLAKTRLAD LKVSIENMGL YEDLSSAGDI TEPHSQALQD VEKAIMVFEH TGNIPVTVME ASIFRRPYYV SHFLPALLTP RVLPKVPDSR VAFIESLKRA DKIPPSLYST YCQACSAAEE KPEDAALGVR AEPNSAEEPL GQLTAALGEL RASMTDPSQR DVISAQVAVI SERLRAVLGH NEDDSSVEIS KIQLSINTPR LEPREHMAVD LLLTSFCQNL MAASSVAPPE RQGPWAALFV RTMCGRVLPA VLTRLCQLLR HQGPSLSAPH VLGLAALAVH LGESRSALPE VDVGPPAPGA GLPVPALFDS LLTCRTRDSL FFCLKFCTAA ISYSLCKFSS QSRDTLCSCL SPGLIKKFQF LMFRLFSEAR QPLSEEDVAS LSWRPLHLPS ADWQRAALSL WTHRTFREVL KEEDVHLTYQ DWLHLELEIQ PEADALSDTE RQDFHQWAIH EHFLPESSAS GGCDGDLQAA CTILVNALMD FHQSSRSYDH SENSDLVFGG RTGNEDIISR LQEMVADLEL QQDLIVPLGH TPSQEHFLFE IFRRRLQALT SGWSVAASLQ RQRELLMYKR ILLRLPSSVL CGSSFQAEQP ITARCEQFFH LVNSEMRNFC SHGGALTQDI TAHFFRGLLN ACLRSRDPSL MVDFILAKCQ TKCPLILTSA LVWWPSLEPV LLCRWRRHCQ SPLPRELQKL QEGRQFASDF LSPEAASPAP NPDWLSAAAL HFAIQQVREE NIRKQLKKLD CEREELLVFL FFFSLMGLLS SHLTSNSTTD LPKAFHVCAA ILECLEKRKI SWLALFQLTE SDLRLGRLLL RVAPDQHTRL LPFAFYSLLS YFHEDAAIRE EAFLHVAVDM YLKLVQLFVA GDTSTVSPPA GRSLELKGQG NPVELITKAR LFLLQLIPRC PKKSFSHVAE LLADRGDCDP EVSAALQSRQ QAAPDADLSQ EPHLF //