GenomeNet

Database: UniProt
Entry: Q9BXF3
LinkDB: Q9BXF3
Original site: Q9BXF3 
ID   CECR2_HUMAN             Reviewed;        1484 AA.
AC   Q9BXF3; A8MS90; A8MX16; Q658Z4; Q96P58; Q9C0C3;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   11-DEC-2019, entry version 158.
DE   RecName: Full=Cat eye syndrome critical region protein 2;
GN   Name=CECR2; Synonyms=KIAA1740;
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 A), AND VARIANT LEU-674.
RX   PubMed=11381032; DOI=10.1101/gr.154901;
RA   Footz T.K., Brinkman-Mills P., Banting G.S., Maier S.A., Riazi M.A.,
RA   Bridgland L.J., Hu S., Birren B., Minoshima S., Shimizu N., Pan H.,
RA   Nguyen T., Fang F., Fu Y., Ray L., Wu H., Shaull S., Phan S., Yao Z.,
RA   Chen F., Huan A., Hu P., Wang Q., Loh P., Qi S., Roe B.A., McDermid H.E.;
RT   "Analysis of the cat eye syndrome critical region in humans and the region
RT   of conserved synteny in mice: a search for candidate genes at or near the
RT   human chromosome 22 pericentromere.";
RL   Genome Res. 11:1053-1070(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1484 (ISOFORM C).
RC   TISSUE=Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-1484 (ISOFORM C), AND VARIANT
RP   LEU-674.
RC   TISSUE=Brain;
RX   PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA   Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:347-355(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 168-1484 (ISOFORM B), FUNCTION, AND
RP   INTERACTION WITH LRPPRC.
RC   TISSUE=Liver;
RX   PubMed=11827465; DOI=10.1006/geno.2001.6679;
RA   Liu L., McKeehan W.L.;
RT   "Sequence analysis of LRPPRC and its SEC1 domain interaction partners
RT   suggests roles in cytoskeletal organization, vesicular trafficking,
RT   nucleocytosolic shuttling, and chromosome activity.";
RL   Genomics 79:124-136(2002).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN THE CERF COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15640247; DOI=10.1093/hmg/ddi048;
RA   Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S.,
RA   Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.;
RT   "CECR2, a protein involved in neurulation, forms a novel chromatin
RT   remodeling complex with SNF2L.";
RL   Hum. Mol. Genet. 14:513-524(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; THR-546; SER-571;
RP   SER-1014 AND SER-1312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=26365797; DOI=10.1016/j.str.2015.08.004;
RA   Flynn E.M., Huang O.W., Poy F., Oppikofer M., Bellon S.F., Tang Y.,
RA   Cochran A.G.;
RT   "A subset of human bromodomains recognizes butyryllysine and crotonyllysine
RT   histone peptide modifications.";
RL   Structure 23:1801-1814(2015).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 424-538, FUNCTION, DOMAIN, AND
RP   SUBUNIT.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
CC   -!- FUNCTION: Chromatin reader component of histone-modifying complexes,
CC       such as the CERF (CECR2-containing-remodeling factor) complex and ISWI-
CC       type complex (PubMed:15640247, PubMed:26365797, PubMed:22464331). It
CC       thereby plays a role in various processes during development: required
CC       during embryogenesis for neural tube closure and inner ear development.
CC       In adults, required for spermatogenesis, via the formation of ISWI-type
CC       chromatin complexes (By similarity). In histone-modifying complexes,
CC       CECR2 recognizes and binds acylated histones: binds histones that are
CC       acetylated and/or butyrylated (PubMed:26365797, PubMed:22464331). May
CC       also be involved through its interaction with LRPPRC in the integration
CC       of cytoskeletal network with vesicular trafficking, nucleocytosolic
CC       shuttling, transcription, chromosome remodeling and cytokinesis
CC       (PubMed:11827465). {ECO:0000250|UniProtKB:E9Q2Z1,
CC       ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:15640247,
CC       ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:26365797}.
CC   -!- SUBUNIT: Part of the CECR2-containing remodeling factor (CERF) complex
CC       which contains CECR2 and SMARCA1 (PubMed:15640247). Interacts with
CC       acetylated lysine residues on histone H2A and H3 (in vitro)
CC       (PubMed:26365797, PubMed:22464331). Interacts with LRPPRC
CC       (PubMed:11827465). {ECO:0000269|PubMed:11827465,
CC       ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:22464331,
CC       ECO:0000269|PubMed:26365797}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=Q9BXF3-1; Sequence=Displayed;
CC       Name=B; Synonyms=CECR2B;
CC         IsoId=Q9BXF3-2; Sequence=VSP_000571, VSP_000572, VSP_000573;
CC       Name=C;
CC         IsoId=Q9BXF3-3; Sequence=VSP_020407;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, thymus,
CC       placenta and lung. Expressed at lower level in brain, heart, colon,
CC       spleen, kidney.
CC   -!- DOMAIN: The Bromo domain recognizes and binds acetylated histones
CC       (PubMed:22464331). Also recognizes and binds histones that are
CC       butyrylated (PubMed:26365797). {ECO:0000269|PubMed:22464331,
CC       ECO:0000269|PubMed:26365797}.
CC   -!- MISCELLANEOUS: Candidate gene for the Cat Eye Syndrome (CES), a
CC       developmental disorder associated with the duplication of a 2 Mb region
CC       of 22q11.2. Duplication usually takes in the form of a surpernumerary
CC       bisatellited isodicentric chromosome, resulting in four copies of the
CC       region (represents an inv dup(22)(q11)). CES is characterized
CC       clinically by the combination of coloboma of the iris and anal atresia
CC       with fistula, downslanting palpebral fissures, preauricular tags and/or
CC       pits, frequent occurrence of heart and renal malformations, and normal
CC       or near-normal mental development. {ECO:0000305|PubMed:11381032}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH56122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH56212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW57756.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AF336133; AAK15343.1; -; mRNA.
DR   EMBL; AC004019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471193; EAW57756.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX647449; CAH56122.1; ALT_INIT; mRNA.
DR   EMBL; AL832377; CAH56212.1; ALT_INIT; mRNA.
DR   EMBL; AB051527; BAB21831.1; -; mRNA.
DR   EMBL; AF411609; AAL07393.1; -; mRNA.
DR   RefSeq; NP_001276975.1; NM_001290046.1.
DR   RefSeq; NP_001276976.1; NM_001290047.1. [Q9BXF3-3]
DR   PDB; 3NXB; X-ray; 1.83 A; A/B=424-538.
DR   PDB; 5V84; X-ray; 2.70 A; A/B/C/D=424-538.
DR   PDBsum; 3NXB; -.
DR   PDBsum; 5V84; -.
DR   SMR; Q9BXF3; -.
DR   BioGrid; 118176; 7.
DR   ComplexPortal; CPX-446; CERF complex.
DR   CORUM; Q9BXF3; -.
DR   IntAct; Q9BXF3; 2.
DR   STRING; 9606.ENSP00000341219; -.
DR   BindingDB; Q9BXF3; -.
DR   ChEMBL; CHEMBL3108639; -.
DR   GuidetoPHARMACOLOGY; 2733; -.
DR   iPTMnet; Q9BXF3; -.
DR   PhosphoSitePlus; Q9BXF3; -.
DR   BioMuta; CECR2; -.
DR   DMDM; 114152782; -.
DR   jPOST; Q9BXF3; -.
DR   MassIVE; Q9BXF3; -.
DR   PaxDb; Q9BXF3; -.
DR   PeptideAtlas; Q9BXF3; -.
DR   PRIDE; Q9BXF3; -.
DR   ProteomicsDB; 79417; -. [Q9BXF3-1]
DR   ProteomicsDB; 79418; -. [Q9BXF3-2]
DR   ProteomicsDB; 79419; -. [Q9BXF3-3]
DR   DNASU; 27443; -.
DR   Ensembl; ENST00000342247; ENSP00000341219; ENSG00000099954. [Q9BXF3-1]
DR   GeneID; 27443; -.
DR   KEGG; hsa:27443; -.
DR   UCSC; uc062bgi.1; human. [Q9BXF3-1]
DR   CTD; 27443; -.
DR   DisGeNET; 27443; -.
DR   EuPathDB; HostDB:ENSG00000099954.18; -.
DR   GeneCards; CECR2; -.
DR   HGNC; HGNC:1840; CECR2.
DR   HPA; HPA002943; -.
DR   MIM; 607576; gene.
DR   neXtProt; NX_Q9BXF3; -.
DR   OpenTargets; ENSG00000099954; -.
DR   PharmGKB; PA26383; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   eggNOG; COG5076; LUCA.
DR   GeneTree; ENSGT00940000160360; -.
DR   HOGENOM; HOG000081808; -.
DR   InParanoid; Q9BXF3; -.
DR   OMA; SSGALYW; -.
DR   OrthoDB; 379050at2759; -.
DR   PhylomeDB; Q9BXF3; -.
DR   TreeFam; TF324727; -.
DR   ChiTaRS; CECR2; human.
DR   EvolutionaryTrace; Q9BXF3; -.
DR   GenomeRNAi; 27443; -.
DR   Pharos; Q9BXF3; Tchem.
DR   PRO; PR:Q9BXF3; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9BXF3; protein.
DR   Bgee; ENSG00000099954; Expressed in 147 organ(s), highest expression level in gastrocnemius.
DR   ExpressionAtlas; Q9BXF3; baseline and differential.
DR   Genevisible; Q9BXF3; HS.
DR   GO; GO:0090537; C:CERF complex; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:HGNC-UCL.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; NAS:UniProtKB.
DR   GO; GO:0097194; P:execution phase of apoptosis; IDA:BHF-UCL.
DR   GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
DR   Gene3D; 1.20.920.10; -; 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR029614; CECR2.
DR   PANTHER; PTHR47092; PTHR47092; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Bromodomain; Chromatin regulator;
KW   Methylation; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN           1..1484
FT                   /note="Cat eye syndrome critical region protein 2"
FT                   /id="PRO_0000211192"
FT   DOMAIN          451..521
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   COMPBIAS        333..337
FT                   /note="Poly-Glu"
FT   COMPBIAS        611..614
FT                   /note="Poly-Ser"
FT   COMPBIAS        1250..1253
FT                   /note="Poly-Pro"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         546
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         1014
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         1197
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q2Z1"
FT   MOD_RES         1203
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q2Z1"
FT   MOD_RES         1312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   VAR_SEQ         291..318
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:11827465"
FT                   /id="VSP_000571"
FT   VAR_SEQ         370..389
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000303|PubMed:11214970,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_020407"
FT   VAR_SEQ         519..526
FT                   /note="EYTKMSDN -> GKQGRSLC (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:11827465"
FT                   /id="VSP_000572"
FT   VAR_SEQ         527..1484
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:11827465"
FT                   /id="VSP_000573"
FT   VARIANT         293
FT                   /note="R -> H (in dbSNP:rs5747211)"
FT                   /id="VAR_027411"
FT   VARIANT         674
FT                   /note="P -> L (in dbSNP:rs1296794)"
FT                   /evidence="ECO:0000269|PubMed:11214970,
FT                   ECO:0000269|PubMed:11381032"
FT                   /id="VAR_027412"
FT   CONFLICT        352
FT                   /note="M -> I (in Ref. 4; CAH56122/CAH56212)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1029
FT                   /note="S -> C (in Ref. 1; AAK15343)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1045
FT                   /note="W -> R (in Ref. 1; AAK15343)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1441
FT                   /note="M -> T (in Ref. 4; CAH56122/CAH56212)"
FT                   /evidence="ECO:0000305"
FT   HELIX           439..452
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   HELIX           457..459
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   STRAND          460..462
FT                   /evidence="ECO:0000244|PDB:5V84"
FT   TURN            465..467
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   HELIX           471..474
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   HELIX           481..489
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   HELIX           496..514
FT                   /evidence="ECO:0000244|PDB:3NXB"
FT   HELIX           519..536
FT                   /evidence="ECO:0000244|PDB:3NXB"
SQ   SEQUENCE   1484 AA;  164213 MW;  8680DB16A0B90D0D CRC64;
     MCPEEGGAAG LGELRSWWEV PAIAHFCSLF RTAFRLPDFE IEELEAALHR DDVEFISDLI
     ACLLQGCYQR RDITPQTFHS YLEDIINYRW ELEEGKPNPL REASFQDLPL RTRVEILHRL
     CDYRLDADDV FDLLKGLDAD SLRVEPLGED NSGALYWYFY GTRMYKEDPV QGKSNGELSL
     SRESEGQKNV SSIPGKTGKR RGRPPKRKKL QEEILLSEKQ EENSLASEPQ TRHGSQGPGQ
     GTWWLLCQTE EEWRQVTESF RERTSLRERQ LYKLLSEDFL PEICNMIAQK GKRPQRTKAE
     LHPRWMSDHL SIKPVKQEET PVLTRIEKQK RKEEEEERQI LLAVQKKEQE QMLKEERKRE
     LEEKVKAVEG MCSVRVVWRG ACLSTSRPVD RAKRRKLREE RAWLLAQGKE LPPELSHLDP
     NSPMREEKKT KDLFELDDDF TAMYKVLDVV KAHKDSWPFL EPVDESYAPN YYQIIKAPMD
     ISSMEKKLNG GLYCTKEEFV NDMKTMFRNC RKYNGESSEY TKMSDNLERC FHRAMMKHFP
     GEDGDTDEEF WIREDEKREK RRSRAGRSGG SHVWTRSRDP EGSSRKQQPM ENGGKSLPPT
     RRAPSSGDDQ SSSSTQPPRE VGTSNGRGFS HPLHCGGTPS QAPFLNQMRP AVPGTFGPLR
     GSDPATLYGS SGVPEPHPGE PVQQRQPFTM QPPVGINSLR GPRLGTPEEK QMCGGLTHLS
     NMGPHPGSLQ LGQISGPSQD GSMYAPAQFQ PGFIPPRHGG APARPPDFPE SSEIPPSHMY
     RSYKYLNRVH SAVWNGNHGA TNQGPLGPDE KPHLGPGPSH QPRTLGHVMD SRVMRPPVPP
     NQWTEQSGFL PHGVPSSGYM RPPCKSAGHR LQPPPVPAPS SLFGAPAQAL RGVQGGDSMM
     DSPEMIAMQQ LSSRVCPPGV PYHPHQPAHP RLPGPFPQVA HPMSVTVSAP KPALGNPGRA
     PENSEAQEPE NDQAEPLPGL EEKPPGVGTS EGVYLTQLPH PTPPLQTDCT RQSSPQERET
     VGPELKSSSS ESADNCKAMK GKNPWPSDSS YPGPAAQGCV RDLSTVADRG ALSENGVIGE
     ASPCGSEGKG LGSSGSEKLL CPRGRTLQET MPCTGQNAAT PPSTDPGLTG GTVSQFPPLY
     MPGLEYPNSA AHYHISPGLQ GVGPVMGGKS PASHPQHFPP RGFQSNHPHS GGFPRYRPPQ
     GMRYSYHPPP QPSYHHYQRT PYYACPQSFS DWQRPLHPQG SPSGPPASQP PPPRSLFSDK
     NAMASLQGCE TLNAALTSPT RMDAVAAKVP NDGQNPGPEE EKLDESMERP ESPKEFLDLD
     NHNAATKRQS SLSASEYLYG TPPPLSSGMG FGSSAFPPHS VMLQTGPPYT PQRPASHFQP
     RAYSSPVAAL PPHHPGATQP NGLSQEGPIY RCQEEGLGHF QAVMMEQIGT RSGIRGPFQE
     MYRPSGMQMH PVQSQASFPK TPTAATSQEE VPPHKPPTLP LDQS
//
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