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FAS-associated factor 1 (hFAF1) (UBX domain-containing protein 12) (UBX domain-containing protein 3A)

 FAF1_HUMAN              Reviewed;         650 AA.
Q9UNN5; Q549F0; Q9UF34; Q9UNT3; Q9Y2Z3;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=FAS-associated factor 1;
Short=hFAF1;
AltName: Full=UBX domain-containing protein 12;
AltName: Full=UBX domain-containing protein 3A;
Name=FAF1; Synonyms=UBXD12, UBXN3A; ORFNames=CGI-03;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), INTERACTION WITH
FAS, AND TISSUE SPECIFICITY.
TISSUE=Brain, and Liver;
PubMed=10462485; DOI=10.1006/bbrc.1999.1217;
Ryu S.-W., Chae S.-K., Lee K.-J., Kim E.;
"Identification and characterization of human Fas associated factor 1,
hFAF1.";
Biochem. Biophys. Res. Commun. 262:388-394(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Ding J.B., Yu L., Zhao S.Y.;
"Cloning of a new human cDNA homologous to Mus musculus FAF1.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Boldyreff B.;
"Full length cDNA sequence and chromosomal localization of the human
Fas-associated factor 1 gene, hFaf1.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Brain, and Kidney;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
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).
[13]
INTERACTION WITH NLRP12.
PubMed=21978668; DOI=10.1016/j.jmb.2011.09.024;
Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.;
"The NLRP12 pyrin domain: structure, dynamics, and functional
insights.";
J. Mol. Biol. 413:790-803(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-580 AND SER-582, 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).
[15]
FUNCTION, INTERACTION WITH CDT1 AND VCP, AND SUBCELLULAR LOCATION.
PubMed=26842564; DOI=10.1038/ncomms10612;
Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D.,
Kashkar H., Ramadan K., Hoppe T.;
"Chromatin-associated degradation is defined by UBXN-3/FAF1 to
safeguard DNA replication fork progression.";
Nat. Commun. 7:10612-10612(2016).
[16]
STRUCTURE BY NMR OF 569-650.
PubMed=11243799; DOI=10.1006/jmbi.2000.4462;
Buchberger A., Howard M.J., Proctor M., Bycroft M.M.;
"The UBX domain: a widespread ubiquitin-like module.";
J. Mol. Biol. 307:17-24(2001).
[17]
STRUCTURE BY NMR OF 99-191.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the ubiquitin-like domain in human FAS-
associated factor 1 (hFAF1).";
Submitted (OCT-2007) to the PDB data bank.
[18]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, FUNCTION, AND DOMAIN
UBA.
PubMed=19722279; DOI=10.1002/pro.237;
Song J., Park J.K., Lee J.J., Choi Y.S., Ryu K.S., Kim J.H., Kim E.,
Lee K.J., Jeon Y.H., Kim E.E.;
"Structure and interaction of ubiquitin-associated domain of human
Fas-associated factor 1.";
Protein Sci. 18:2265-2276(2009).
-!- FUNCTION: Ubiquitin-binding protein (PubMed:19722279). Required
for the progression of DNA replication forks by targeting DNA
replication licensing factor CDT1 for degradation
(PubMed:26842564). Potentiates but cannot initiate FAS-induced
apoptosis (By similarity). {ECO:0000250|UniProtKB:P54731,
ECO:0000269|PubMed:19722279, ECO:0000269|PubMed:26842564}.
-!- SUBUNIT: Interacts with CDT1 and ATPase VCP/p97 (PubMed:26842564).
Interacts (via UBA domain) with FAS (via death domain)
(PubMed:10462485). Interacts (via UBA domain) with NLRP12 (via
DAPIN/PYRIN domain) (PubMed:21978668).
{ECO:0000269|PubMed:10462485, ECO:0000269|PubMed:21978668,
ECO:0000269|PubMed:26842564}.
-!- INTERACTION:
P55072:VCP; NbExp=4; IntAct=EBI-15930546, EBI-355164;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26842564}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9UNN5-1; Sequence=Displayed;
Name=Short; Synonyms=hFAF1(s);
IsoId=Q9UNN5-2; Sequence=VSP_006704;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Most abundant in testis, slightly less
abundant in skeletal muscle and heart, followed by prostate,
thymus, ovary, small intestine, and colon. Not detected in the
peripheral blood leukocytes. {ECO:0000269|PubMed:10462485}.
-!- SEQUENCE CAUTION:
Sequence=AAD51876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF106798; AAD51886.1; -; mRNA.
EMBL; AF094700; AAD51876.1; ALT_INIT; mRNA.
EMBL; AF136173; AAP97263.1; -; mRNA.
EMBL; AJ271408; CAB67705.1; -; mRNA.
EMBL; AF132938; AAD27713.1; -; mRNA.
EMBL; AC091610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL603746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06837.1; -; Genomic_DNA.
EMBL; BC004970; AAH04970.1; -; mRNA.
EMBL; BC067100; AAH67100.1; -; mRNA.
EMBL; AL133631; CAB63755.1; -; mRNA.
CCDS; CCDS554.1; -. [Q9UNN5-1]
PIR; JC7093; JC7093.
PIR; T43466; T43466.
RefSeq; NP_008982.1; NM_007051.2. [Q9UNN5-1]
UniGene; Hs.530402; -.
PDB; 1H8C; NMR; -; A=569-650.
PDB; 2DZM; NMR; -; A=99-191.
PDB; 2EC4; NMR; -; A=325-495.
PDB; 3E21; X-ray; 1.73 A; A=5-47.
PDB; 3QC8; X-ray; 2.20 A; B=571-650.
PDB; 3QCA; X-ray; 2.90 A; A/B/C/D=571-650.
PDB; 3QQ8; X-ray; 2.00 A; B=568-650.
PDB; 3QWZ; X-ray; 2.00 A; B=571-650.
PDB; 3QX1; X-ray; 1.60 A; A/B=571-650.
PDB; 3R3M; X-ray; 3.00 A; A/B/C/D=568-650.
PDBsum; 1H8C; -.
PDBsum; 2DZM; -.
PDBsum; 2EC4; -.
PDBsum; 3E21; -.
PDBsum; 3QC8; -.
PDBsum; 3QCA; -.
PDBsum; 3QQ8; -.
PDBsum; 3QWZ; -.
PDBsum; 3QX1; -.
PDBsum; 3R3M; -.
ProteinModelPortal; Q9UNN5; -.
SMR; Q9UNN5; -.
BioGrid; 116298; 134.
DIP; DIP-38245N; -.
IntAct; Q9UNN5; 50.
MINT; Q9UNN5; -.
STRING; 9606.ENSP00000360843; -.
ChEMBL; CHEMBL3758063; -.
iPTMnet; Q9UNN5; -.
PhosphoSitePlus; Q9UNN5; -.
BioMuta; FAF1; -.
DMDM; 20454906; -.
EPD; Q9UNN5; -.
PaxDb; Q9UNN5; -.
PeptideAtlas; Q9UNN5; -.
PRIDE; Q9UNN5; -.
ProteomicsDB; 85315; -.
ProteomicsDB; 85316; -. [Q9UNN5-2]
DNASU; 11124; -.
Ensembl; ENST00000396153; ENSP00000379457; ENSG00000185104. [Q9UNN5-1]
GeneID; 11124; -.
KEGG; hsa:11124; -.
UCSC; uc001cse.2; human. [Q9UNN5-1]
CTD; 11124; -.
DisGeNET; 11124; -.
EuPathDB; HostDB:ENSG00000185104.19; -.
GeneCards; FAF1; -.
HGNC; HGNC:3578; FAF1.
HPA; CAB072814; -.
HPA; HPA018253; -.
MIM; 604460; gene.
neXtProt; NX_Q9UNN5; -.
OpenTargets; ENSG00000185104; -.
PharmGKB; PA27976; -.
eggNOG; ENOG410IPG5; Eukaryota.
eggNOG; ENOG410Z9BT; LUCA.
GeneTree; ENSGT00530000063422; -.
HOGENOM; HOG000043073; -.
HOVERGEN; HBG002876; -.
InParanoid; Q9UNN5; -.
KO; K20703; -.
OMA; MEIFSAQ; -.
OrthoDB; EOG091G04LQ; -.
PhylomeDB; Q9UNN5; -.
TreeFam; TF314172; -.
SignaLink; Q9UNN5; -.
SIGNOR; Q9UNN5; -.
ChiTaRS; FAF1; human.
EvolutionaryTrace; Q9UNN5; -.
GeneWiki; FAF1; -.
GenomeRNAi; 11124; -.
PRO; PR:Q9UNN5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000185104; Expressed in 220 organ(s), highest expression level in corpus callosum.
CleanEx; HS_FAF1; -.
ExpressionAtlas; Q9UNN5; baseline and differential.
Genevisible; Q9UNN5; HS.
GO; GO:0031265; C:CD95 death-inducing signaling complex; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:BHF-UCL.
GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:CACAO.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
CDD; cd01771; Faf1_UBX; 1.
InterPro; IPR033043; FAF1_UBX.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR006577; UAS.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR001012; UBX_dom.
Pfam; PF00789; UBX; 1.
SMART; SM00594; UAS; 1.
SMART; SM00166; UBX; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF54236; SSF54236; 3.
PROSITE; PS50033; UBX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 650 FAS-associated factor 1.
/FTId=PRO_0000211038.
DOMAIN 1 57 UBA. {ECO:0000269|PubMed:19722279}.
DOMAIN 569 646 UBX. {ECO:0000255|PROSITE-
ProRule:PRU00215}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 580 580 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 188 339 Missing (in isoform Short).
{ECO:0000303|PubMed:10462485}.
/FTId=VSP_006704.
CONFLICT 448 448 F -> K (in Ref. 1; AAD51886/AAD51876).
{ECO:0000305}.
CONFLICT 498 498 E -> G (in Ref. 1; AAD51886/AAD51876).
{ECO:0000305}.
CONFLICT 529 529 H -> R (in Ref. 1; AAD51886/AAD51876).
{ECO:0000305}.
HELIX 7 18 {ECO:0000244|PDB:3E21}.
HELIX 23 32 {ECO:0000244|PDB:3E21}.
TURN 33 35 {ECO:0000244|PDB:3E21}.
HELIX 37 41 {ECO:0000244|PDB:3E21}.
STRAND 100 106 {ECO:0000244|PDB:2DZM}.
STRAND 111 117 {ECO:0000244|PDB:2DZM}.
HELIX 122 133 {ECO:0000244|PDB:2DZM}.
TURN 137 139 {ECO:0000244|PDB:2DZM}.
STRAND 146 148 {ECO:0000244|PDB:2DZM}.
HELIX 156 159 {ECO:0000244|PDB:2DZM}.
STRAND 163 169 {ECO:0000244|PDB:2DZM}.
STRAND 172 174 {ECO:0000244|PDB:2DZM}.
HELIX 330 345 {ECO:0000244|PDB:2EC4}.
HELIX 357 362 {ECO:0000244|PDB:2EC4}.
STRAND 365 367 {ECO:0000244|PDB:2EC4}.
TURN 369 371 {ECO:0000244|PDB:2EC4}.
STRAND 374 380 {ECO:0000244|PDB:2EC4}.
HELIX 386 393 {ECO:0000244|PDB:2EC4}.
TURN 394 396 {ECO:0000244|PDB:2EC4}.
HELIX 398 406 {ECO:0000244|PDB:2EC4}.
STRAND 408 414 {ECO:0000244|PDB:2EC4}.
HELIX 418 431 {ECO:0000244|PDB:2EC4}.
HELIX 434 442 {ECO:0000244|PDB:2EC4}.
STRAND 449 454 {ECO:0000244|PDB:2EC4}.
STRAND 463 467 {ECO:0000244|PDB:2EC4}.
HELIX 473 490 {ECO:0000244|PDB:2EC4}.
STRAND 573 579 {ECO:0000244|PDB:3QX1}.
STRAND 585 591 {ECO:0000244|PDB:3QX1}.
HELIX 596 605 {ECO:0000244|PDB:3QX1}.
TURN 610 612 {ECO:0000244|PDB:3QX1}.
STRAND 613 616 {ECO:0000244|PDB:3QX1}.
STRAND 618 620 {ECO:0000244|PDB:3QX1}.
HELIX 624 626 {ECO:0000244|PDB:3QX1}.
TURN 633 637 {ECO:0000244|PDB:3QX1}.
STRAND 640 648 {ECO:0000244|PDB:3QX1}.
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


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