ID FAF1_HUMAN Reviewed; 650 AA. AC Q9UNN5; Q549F0; Q9UF34; Q9UNT3; Q9Y2Z3; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 22-APR-2020, entry version 183. DE RecName: Full=FAS-associated factor 1; DE Short=hFAF1; DE AltName: Full=UBX domain-containing protein 12; DE AltName: Full=UBX domain-containing protein 3A; GN Name=FAF1; Synonyms=UBXD12, UBXN3A; ORFNames=CGI-03; 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] (ISOFORMS LONG AND SHORT), INTERACTION WITH FAS, RP AND TISSUE SPECIFICITY. RC TISSUE=Brain, and Liver; RX PubMed=10462485; DOI=10.1006/bbrc.1999.1217; RA Ryu S.-W., Chae S.-K., Lee K.-J., Kim E.; RT "Identification and characterization of human Fas associated factor 1, RT hFAF1."; RL Biochem. Biophys. Res. Commun. 262:388-394(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). RA Ding J.B., Yu L., Zhao S.Y.; RT "Cloning of a new human cDNA homologous to Mus musculus FAF1."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). RA Boldyreff B.; RT "Full length cDNA sequence and chromosomal localization of the human Fas- RT associated factor 1 gene, hFaf1."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Brain, and Kidney; 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 [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG). RC TISSUE=Testis; 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP INTERACTION WITH NLRP12. RX PubMed=21978668; DOI=10.1016/j.jmb.2011.09.024; RA Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.; RT "The NLRP12 pyrin domain: structure, dynamics, and functional insights."; RL J. Mol. Biol. 413:790-803(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-580 AND SER-582, AND RP IDENTIFICATION BY 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 [15] RP FUNCTION, INTERACTION WITH CDT1 AND VCP, AND SUBCELLULAR LOCATION. RX PubMed=26842564; DOI=10.1038/ncomms10612; RA Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D., Kashkar H., RA Ramadan K., Hoppe T.; RT "Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard RT DNA replication fork progression."; RL Nat. Commun. 7:10612-10612(2016). RN [16] RP STRUCTURE BY NMR OF 569-650. RX PubMed=11243799; DOI=10.1006/jmbi.2000.4462; RA Buchberger A., Howard M.J., Proctor M., Bycroft M.M.; RT "The UBX domain: a widespread ubiquitin-like module."; RL J. Mol. Biol. 307:17-24(2001). RN [17] RP STRUCTURE BY NMR OF 99-191. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the ubiquitin-like domain in human FAS-associated RT factor 1 (hFAF1)."; RL Submitted (OCT-2007) to the PDB data bank. RN [18] RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, FUNCTION, AND DOMAIN UBA. RX PubMed=19722279; DOI=10.1002/pro.237; RA Song J., Park J.K., Lee J.J., Choi Y.S., Ryu K.S., Kim J.H., Kim E., RA Lee K.J., Jeon Y.H., Kim E.E.; RT "Structure and interaction of ubiquitin-associated domain of human Fas- RT associated factor 1."; RL Protein Sci. 18:2265-2276(2009). CC -!- FUNCTION: Ubiquitin-binding protein (PubMed:19722279). Required for the CC progression of DNA replication forks by targeting DNA replication CC licensing factor CDT1 for degradation (PubMed:26842564). Potentiates CC but cannot initiate FAS-induced apoptosis (By similarity). CC {ECO:0000250|UniProtKB:P54731, ECO:0000269|PubMed:19722279, CC ECO:0000269|PubMed:26842564}. CC -!- SUBUNIT: Interacts with CDT1 and ATPase VCP/p97 (PubMed:26842564). CC Interacts (via UBA domain) with FAS (via death domain) CC (PubMed:10462485). Interacts (via UBA domain) with NLRP12 (via CC DAPIN/PYRIN domain) (PubMed:21978668). {ECO:0000269|PubMed:10462485, CC ECO:0000269|PubMed:21978668, ECO:0000269|PubMed:26842564}. CC -!- INTERACTION: CC Q9UNN5-1; P55072: VCP; NbExp=4; IntAct=EBI-15930546, EBI-355164; CC Q9UNN5; Q7Z739: YTHDF3; NbExp=3; IntAct=EBI-718246, EBI-2849837; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26842564}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q9UNN5-1; Sequence=Displayed; CC Name=Short; Synonyms=hFAF1(s); CC IsoId=Q9UNN5-2; Sequence=VSP_006704; CC -!- TISSUE SPECIFICITY: Most abundant in testis, slightly less abundant in CC skeletal muscle and heart, followed by prostate, thymus, ovary, small CC intestine, and colon. Not detected in the peripheral blood leukocytes. CC {ECO:0000269|PubMed:10462485}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD51876.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF106798; AAD51886.1; -; mRNA. DR EMBL; AF094700; AAD51876.1; ALT_INIT; mRNA. DR EMBL; AF136173; AAP97263.1; -; mRNA. DR EMBL; AJ271408; CAB67705.1; -; mRNA. DR EMBL; AF132938; AAD27713.1; -; mRNA. DR EMBL; AC091610; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118557; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL603746; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06837.1; -; Genomic_DNA. DR EMBL; BC004970; AAH04970.1; -; mRNA. DR EMBL; BC067100; AAH67100.1; -; mRNA. DR EMBL; AL133631; CAB63755.1; -; mRNA. DR CCDS; CCDS554.1; -. [Q9UNN5-1] DR PIR; JC7093; JC7093. DR PIR; T43466; T43466. DR RefSeq; NP_008982.1; NM_007051.2. [Q9UNN5-1] DR PDB; 1H8C; NMR; -; A=569-650. DR PDB; 2DZM; NMR; -; A=99-191. DR PDB; 2EC4; NMR; -; A=325-495. DR PDB; 3E21; X-ray; 1.73 A; A=5-47. DR PDB; 3QC8; X-ray; 2.20 A; B=571-650. DR PDB; 3QCA; X-ray; 2.90 A; A/B/C/D=571-650. DR PDB; 3QQ8; X-ray; 2.00 A; B=568-650. DR PDB; 3QWZ; X-ray; 2.00 A; B=571-650. DR PDB; 3QX1; X-ray; 1.60 A; A/B=571-650. DR PDB; 3R3M; X-ray; 3.00 A; A/B/C/D=568-650. DR PDBsum; 1H8C; -. DR PDBsum; 2DZM; -. DR PDBsum; 2EC4; -. DR PDBsum; 3E21; -. DR PDBsum; 3QC8; -. DR PDBsum; 3QCA; -. DR PDBsum; 3QQ8; -. DR PDBsum; 3QWZ; -. DR PDBsum; 3QX1; -. DR PDBsum; 3R3M; -. DR SMR; Q9UNN5; -. DR BioGrid; 116298; 292. DR DIP; DIP-38245N; -. DR IntAct; Q9UNN5; 58. DR MINT; Q9UNN5; -. DR STRING; 9606.ENSP00000379457; -. DR ChEMBL; CHEMBL3758063; -. DR iPTMnet; Q9UNN5; -. DR PhosphoSitePlus; Q9UNN5; -. DR BioMuta; FAF1; -. DR DMDM; 20454906; -. DR EPD; Q9UNN5; -. DR jPOST; Q9UNN5; -. DR MassIVE; Q9UNN5; -. DR PaxDb; Q9UNN5; -. DR PeptideAtlas; Q9UNN5; -. DR PRIDE; Q9UNN5; -. DR ProteomicsDB; 85315; -. [Q9UNN5-1] DR ProteomicsDB; 85316; -. [Q9UNN5-2] DR Antibodypedia; 18936; 348 antibodies. DR DNASU; 11124; -. DR Ensembl; ENST00000396153; ENSP00000379457; ENSG00000185104. [Q9UNN5-1] DR GeneID; 11124; -. DR KEGG; hsa:11124; -. DR UCSC; uc001cse.2; human. [Q9UNN5-1] DR CTD; 11124; -. DR DisGeNET; 11124; -. DR GeneCards; FAF1; -. DR HGNC; HGNC:3578; FAF1. DR HPA; ENSG00000185104; Low tissue specificity. DR MIM; 604460; gene. DR neXtProt; NX_Q9UNN5; -. DR OpenTargets; ENSG00000185104; -. DR PharmGKB; PA27976; -. DR eggNOG; ENOG410IPG5; Eukaryota. DR eggNOG; ENOG410Z9BT; LUCA. DR GeneTree; ENSGT00940000154831; -. DR HOGENOM; CLU_028119_0_0_1; -. DR InParanoid; Q9UNN5; -. DR KO; K20703; -. DR OMA; LTNVFCD; -. DR OrthoDB; 845154at2759; -. DR PhylomeDB; Q9UNN5; -. DR TreeFam; TF314172; -. DR SignaLink; Q9UNN5; -. DR SIGNOR; Q9UNN5; -. DR ChiTaRS; FAF1; human. DR EvolutionaryTrace; Q9UNN5; -. DR GeneWiki; FAF1; -. DR GenomeRNAi; 11124; -. DR Pharos; Q9UNN5; Tbio. DR PRO; PR:Q9UNN5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UNN5; protein. DR Bgee; ENSG00000185104; Expressed in corpus callosum and 219 other tissues. DR ExpressionAtlas; Q9UNN5; baseline and differential. DR Genevisible; Q9UNN5; HS. DR GO; GO:0031265; C:CD95 death-inducing signaling complex; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:BHF-UCL. DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB. DR GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB. DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0008219; P:cell death; IMP:UniProtKB. DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0010942; P:positive regulation of cell death; IDA:CACAO. DR GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IMP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB. DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB. DR CDD; cd01771; UBX_UBXN3A; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR033043; FAF1-like_UBX. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR006577; UAS. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR001012; UBX_dom. DR Pfam; PF00789; UBX; 1. DR SMART; SM00594; UAS; 1. DR SMART; SM00166; UBX; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF54236; SSF54236; 3. DR PROSITE; PS50033; UBX; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..650 FT /note="FAS-associated factor 1" FT /id="PRO_0000211038" FT DOMAIN 1..57 FT /note="UBA" FT /evidence="ECO:0000269|PubMed:19722279" FT DOMAIN 569..646 FT /note="UBX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231" FT MOD_RES 580 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 582 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT VAR_SEQ 188..339 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:10462485" FT /id="VSP_006704" FT CONFLICT 448 FT /note="F -> K (in Ref. 1; AAD51886/AAD51876)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="E -> G (in Ref. 1; AAD51886/AAD51876)" FT /evidence="ECO:0000305" FT CONFLICT 529 FT /note="H -> R (in Ref. 1; AAD51886/AAD51876)" FT /evidence="ECO:0000305" FT HELIX 7..18 FT /evidence="ECO:0000244|PDB:3E21" FT HELIX 23..32 FT /evidence="ECO:0000244|PDB:3E21" FT TURN 33..35 FT /evidence="ECO:0000244|PDB:3E21" FT HELIX 37..41 FT /evidence="ECO:0000244|PDB:3E21" FT STRAND 100..106 FT /evidence="ECO:0000244|PDB:2DZM" FT STRAND 111..117 FT /evidence="ECO:0000244|PDB:2DZM" FT HELIX 122..133 FT /evidence="ECO:0000244|PDB:2DZM" FT TURN 137..139 FT /evidence="ECO:0000244|PDB:2DZM" FT STRAND 146..148 FT /evidence="ECO:0000244|PDB:2DZM" FT HELIX 156..159 FT /evidence="ECO:0000244|PDB:2DZM" FT STRAND 163..169 FT /evidence="ECO:0000244|PDB:2DZM" FT STRAND 172..174 FT /evidence="ECO:0000244|PDB:2DZM" FT HELIX 330..345 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 357..362 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 365..367 FT /evidence="ECO:0000244|PDB:2EC4" FT TURN 369..371 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 374..380 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 386..393 FT /evidence="ECO:0000244|PDB:2EC4" FT TURN 394..396 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 398..406 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 408..414 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 418..431 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 434..442 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 449..454 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 463..467 FT /evidence="ECO:0000244|PDB:2EC4" FT HELIX 473..490 FT /evidence="ECO:0000244|PDB:2EC4" FT STRAND 573..579 FT /evidence="ECO:0000244|PDB:3QX1" FT STRAND 585..591 FT /evidence="ECO:0000244|PDB:3QX1" FT HELIX 596..605 FT /evidence="ECO:0000244|PDB:3QX1" FT TURN 610..612 FT /evidence="ECO:0000244|PDB:3QX1" FT STRAND 613..616 FT /evidence="ECO:0000244|PDB:3QX1" FT STRAND 618..620 FT /evidence="ECO:0000244|PDB:3QX1" FT HELIX 624..626 FT /evidence="ECO:0000244|PDB:3QX1" FT TURN 633..637 FT /evidence="ECO:0000244|PDB:3QX1" FT STRAND 640..648 FT /evidence="ECO:0000244|PDB:3QX1" SQ SEQUENCE 650 AA; 73954 MW; 7FB9018B9A230488 CRC64; MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSEYGGET IPGPAFNPAS HPASAPTSSS SSAFRPVMPS RQIVERQPRM LDFRVEYRDR NVDVVLEDTC TVGEIKQILE NELQIPVSKM LLKGWKTGDV EDSTVLKSLH LPKNNSLYVL TPDLPPPSSS SHAGALQESL NQNFMLIITH REVQREYNLN FSGSSTIQEV KRNVYDLTSI PVRHQLWEGW PTSATDDSMC LAESGLSYPC HRLTVGRRSS PAQTREQSEE QITDVHMVSD SDGDDFEDAT EFGVDDGEVF GMASSALRKS PMMPENAENE GDALLQFTAE FSSRYGDCHP VFFIGSLEAA FQEAFYVKAR DRKLLAIYLH HDESVLTNVF CSQMLCAESI VSYLSQNFIT WAWDLTKDSN RARFLTMCNR HFGSVVAQTI RTQKTDQFPL FLIIMGKRSS NEVLNVIQGN TTVDELMMRL MAAMEIFTAQ QQEDIKDEDE REARENVKRE QDEAYRLSLE ADRAKREAHE REMAEQFRLE QIRKEQEEER EAIRLSLEQA LPPEPKEENA EPVSKLRIRT PSGEFLERRF LASNKLQIVF DFVASKGFPW DEYKLLSTFP RRDVTQLDPN KSLLEVKLFP QETLFLEAKE //