GenomeNet

Database: UniProt
Entry: O75626
LinkDB: O75626
Original site: O75626 
ID   PRDM1_HUMAN             Reviewed;         825 AA.
AC   O75626; B2REA6; E1P5E0; Q86WM7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   13-FEB-2019, entry version 172.
DE   RecName: Full=PR domain zinc finger protein 1;
DE            EC=2.1.1.-;
DE   AltName: Full=BLIMP-1;
DE   AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
DE   AltName: Full=PR domain-containing protein 1;
DE   AltName: Full=Positive regulatory domain I-binding factor 1;
DE            Short=PRDI-BF1;
DE            Short=PRDI-binding factor 1;
GN   Name=PRDM1; Synonyms=BLIMP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX   PubMed=1851123; DOI=10.1101/gad.5.5.868;
RA   Keller A.D., Maniatis T.;
RT   "Identification and characterization of a novel repressor of beta-
RT   interferon gene expression.";
RL   Genes Dev. 5:868-879(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND FUNCTION.
RX   PubMed=12626569; DOI=10.4049/jimmunol.170.6.3125;
RA   Gyory I., Fejer G., Ghosh N., Seto E., Wright K.L.;
RT   "Identification of a functionally impaired positive regulatory domain
RT   I binding factor 1 transcription repressor in myeloma cell lines.";
RL   J. Immunol. 170:3125-3133(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA   Julaton V.T., Reijo Pera R.A.;
RT   "NANOS3 function in human germ cell development.";
RL   Hum. Mol. Genet. 20:2238-2250(2011).
RN   [7]
RP   SUMOYLATION AT LYS-816.
RX   PubMed=22555612; DOI=10.1038/embor.2012.60;
RA   Ying H.Y., Su S.T., Hsu P.H., Chang C.C., Lin I.Y., Tseng Y.H.,
RA   Tsai M.D., Shih H.M., Lin K.I.;
RT   "SUMOylation of Blimp-1 is critical for plasma cell differentiation.";
RL   EMBO Rep. 13:631-637(2012).
RN   [8]
RP   INTERACTION WITH FBXO10 AND FBXO11, AND UBIQUITINATION.
RX   PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028;
RA   Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C.,
RA   Pagano M., Antebi A.;
RT   "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C.
RT   elegans developmental timing and maturation.";
RL   Dev. Cell 28:697-710(2014).
RN   [9]
RP   INTERACTION WITH FBXO11.
RX   PubMed=24968003; DOI=10.1371/journal.pgen.1004428;
RA   Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y.,
RA   Nishiwaki K., Chang S.C., Wu Y.C.;
RT   "BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in
RT   C. elegans.";
RL   PLoS Genet. 10:E1004428-E1004428(2014).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-816, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-223.
RG   Structural genomics consortium (SGC);
RT   "The crystal structure of methyltransferase domain of human PR domain-
RT   containing protein 1.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Transcription factor that mediates a transcriptional
CC       program in various innate and adaptive immune tissue-resident
CC       lymphocyte T cell types such as tissue-resident memory T (Trm),
CC       natural killer (trNK) and natural killer T (NKT) cells and
CC       negatively regulates gene expression of proteins that promote the
CC       egress of tissue-resident T-cell populations from non-lymphoid
CC       organs. Plays a role in the development, retention and long-term
CC       establishment of adaptive and innate tissue-resident lymphocyte T
CC       cell types in non-lymphoid organs, such as the skin and gut, but
CC       also in other nonbarrier tissues like liver and kidney, and
CC       therefore may provide immediate immunological protection against
CC       reactivating infections or viral reinfection (By similarity).
CC       Binds specifically to the PRDI element in the promoter of the
CC       beta-interferon gene (PubMed:1851123). Drives the maturation of B-
CC       lymphocytes into Ig secreting cells (PubMed:12626569). Associates
CC       with the transcriptional repressor ZNF683 to chromatin at gene
CC       promoter regions (By similarity). {ECO:0000250|UniProtKB:Q60636,
CC       ECO:0000269|PubMed:12626569, ECO:0000269|PubMed:1851123}.
CC   -!- SUBUNIT: Interacts with PRMT5 (By similarity). Interacts with
CC       FBXO10 (PubMed:24613396). Interacts with FBXO11 (PubMed:24613396,
CC       PubMed:24968003). {ECO:0000250|UniProtKB:Q60636,
CC       ECO:0000269|PubMed:24613396, ECO:0000269|PubMed:24968003}.
CC   -!- INTERACTION:
CC       O75925:PIAS1; NbExp=2; IntAct=EBI-948789, EBI-629434;
CC       P63165:SUMO1; NbExp=2; IntAct=EBI-7839538, EBI-80140;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60636}.
CC       Cytoplasm {ECO:0000269|PubMed:21421998}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O75626-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75626-2; Sequence=VSP_039188;
CC       Name=3;
CC         IsoId=O75626-3; Sequence=VSP_043646, VSP_043647;
CC   -!- PTM: Sumoylation at Lys-816 by PIAS1 augments transcriptional
CC       repressor activity, and is critical for plasma cell
CC       differentiation. {ECO:0000269|PubMed:22555612}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXO11) complex, leading to its
CC       degradation by the proteasome. {ECO:0000269|PubMed:24613396}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO45623.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PRDM1ID41831ch6q21.html";
DR   EMBL; AF084199; AAC33300.1; -; mRNA.
DR   EMBL; AY198414; AAO45623.1; ALT_INIT; mRNA.
DR   EMBL; AY198415; AAO45624.1; -; mRNA.
DR   EMBL; AL358952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48419.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48421.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48422.1; -; Genomic_DNA.
DR   EMBL; BC103832; AAI03833.1; -; mRNA.
DR   EMBL; BC103833; AAI03834.1; -; mRNA.
DR   EMBL; BC103834; AAI03835.1; -; mRNA.
DR   CCDS; CCDS34505.1; -. [O75626-3]
DR   CCDS; CCDS5054.2; -. [O75626-1]
DR   PIR; A39564; A39564.
DR   RefSeq; NP_001189.2; NM_001198.3. [O75626-1]
DR   RefSeq; NP_878911.1; NM_182907.2. [O75626-3]
DR   RefSeq; XP_011534365.1; XM_011536063.2. [O75626-2]
DR   RefSeq; XP_016866676.1; XM_017011187.1. [O75626-2]
DR   UniGene; Hs.436023; -.
DR   PDB; 3DAL; X-ray; 1.65 A; A/B=38-223.
DR   PDBsum; 3DAL; -.
DR   ProteinModelPortal; O75626; -.
DR   SMR; O75626; -.
DR   BioGrid; 107108; 32.
DR   IntAct; O75626; 7.
DR   MINT; O75626; -.
DR   STRING; 9606.ENSP00000358092; -.
DR   iPTMnet; O75626; -.
DR   PhosphoSitePlus; O75626; -.
DR   BioMuta; PRDM1; -.
DR   jPOST; O75626; -.
DR   MaxQB; O75626; -.
DR   PaxDb; O75626; -.
DR   PeptideAtlas; O75626; -.
DR   PRIDE; O75626; -.
DR   ProteomicsDB; 50124; -.
DR   ProteomicsDB; 50125; -. [O75626-2]
DR   ProteomicsDB; 50126; -. [O75626-3]
DR   DNASU; 639; -.
DR   Ensembl; ENST00000369089; ENSP00000358085; ENSG00000057657. [O75626-3]
DR   Ensembl; ENST00000369091; ENSP00000358087; ENSG00000057657. [O75626-2]
DR   Ensembl; ENST00000369096; ENSP00000358092; ENSG00000057657. [O75626-1]
DR   GeneID; 639; -.
DR   KEGG; hsa:639; -.
DR   UCSC; uc003prd.3; human. [O75626-1]
DR   CTD; 639; -.
DR   DisGeNET; 639; -.
DR   EuPathDB; HostDB:ENSG00000057657.14; -.
DR   GeneCards; PRDM1; -.
DR   H-InvDB; HIX0006099; -.
DR   HGNC; HGNC:9346; PRDM1.
DR   HPA; HPA030033; -.
DR   MIM; 603423; gene.
DR   neXtProt; NX_O75626; -.
DR   OpenTargets; ENSG00000057657; -.
DR   PharmGKB; PA33707; -.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; ENOG410ZFVU; LUCA.
DR   GeneTree; ENSGT00940000154798; -.
DR   HOGENOM; HOG000059670; -.
DR   HOVERGEN; HBG053670; -.
DR   InParanoid; O75626; -.
DR   OMA; HCHKSYI; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; O75626; -.
DR   TreeFam; TF316545; -.
DR   Reactome; R-HSA-6804754; Regulation of TP53 Expression.
DR   SIGNOR; O75626; -.
DR   ChiTaRS; PRDM1; human.
DR   EvolutionaryTrace; O75626; -.
DR   GeneWiki; PRDM1; -.
DR   GenomeRNAi; 639; -.
DR   PRO; PR:O75626; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000057657; Expressed in 179 organ(s), highest expression level in ectocervix.
DR   ExpressionAtlas; O75626; baseline and differential.
DR   Genevisible; O75626; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR   GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR   GO; GO:0003170; P:heart valve development; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
DR   GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0033082; P:regulation of extrathymic T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0032823; P:regulation of natural killer cell differentiation; ISS:UniProtKB.
DR   GO; GO:0051136; P:regulation of NK T cell differentiation; ISS:UniProtKB.
DR   GO; GO:1990654; P:sebum secreting cell proliferation; IEA:Ensembl.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing;
KW   Complete proteome; Cytoplasm; DNA-binding; Immunity; Innate immunity;
KW   Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW   Polymorphism; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    825       PR domain zinc finger protein 1.
FT                                /FTId=PRO_0000047757.
FT   DOMAIN       84    201       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     575    597       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     603    625       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     631    653       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     659    681       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      527    574       Interaction with PIAS1.
FT   CROSSLNK    816    816       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate. {ECO:0000269|PubMed:22555612}.
FT   CROSSLNK    816    816       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1     36       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1851123}.
FT                                /FTId=VSP_039188.
FT   VAR_SEQ       1      3       MLD -> MEK (in isoform 3).
FT                                {ECO:0000303|PubMed:12626569,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043646.
FT   VAR_SEQ       4    137       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:12626569,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043647.
FT   VARIANT      74     74       G -> S (in dbSNP:rs2185379).
FT                                /FTId=VAR_019983.
FT   VARIANT     203    203       D -> E (in dbSNP:rs811925).
FT                                /FTId=VAR_024221.
FT   HELIX        51     57       {ECO:0000244|PDB:3DAL}.
FT   STRAND       60     62       {ECO:0000244|PDB:3DAL}.
FT   HELIX        78     81       {ECO:0000244|PDB:3DAL}.
FT   STRAND       87     91       {ECO:0000244|PDB:3DAL}.
FT   STRAND       98    105       {ECO:0000244|PDB:3DAL}.
FT   STRAND      111    113       {ECO:0000244|PDB:3DAL}.
FT   STRAND      119    121       {ECO:0000244|PDB:3DAL}.
FT   TURN        123    125       {ECO:0000244|PDB:3DAL}.
FT   STRAND      135    140       {ECO:0000244|PDB:3DAL}.
FT   STRAND      143    149       {ECO:0000244|PDB:3DAL}.
FT   HELIX       158    161       {ECO:0000244|PDB:3DAL}.
FT   TURN        168    170       {ECO:0000244|PDB:3DAL}.
FT   STRAND      173    178       {ECO:0000244|PDB:3DAL}.
FT   STRAND      181    188       {ECO:0000244|PDB:3DAL}.
FT   STRAND      197    200       {ECO:0000244|PDB:3DAL}.
FT   HELIX       202    207       {ECO:0000244|PDB:3DAL}.
FT   HELIX       218    222       {ECO:0000244|PDB:3DAL}.
SQ   SEQUENCE   825 AA;  91771 MW;  07B389BACCD6172F CRC64;
     MLDICLEKRV GTTLAAPKCN SSTVRFQGLA EGTKGTMKMD MEDADMTLWT EAEFEEKCTY
     IVNDHPWDSG ADGGTSVQAE ASLPRNLLFK YATNSEEVIG VMSKEYIPKG TRFGPLIGEI
     YTNDTVPKNA NRKYFWRIYS RGELHHFIDG FNEEKSNWMR YVNPAHSPRE QNLAACQNGM
     NIYFYTIKPI PANQELLVWY CRDFAERLHY PYPGELTMMN LTQTQSSLKQ PSTEKNELCP
     KNVPKREYSV KEILKLDSNP SKGKDLYRSN ISPLTSEKDL DDFRRRGSPE MPFYPRVVYP
     IRAPLPEDFL KASLAYGIER PTYITRSPIP SSTTPSPSAR SSPDQSLKSS SPHSSPGNTV
     SPVGPGSQEH RDSYAYLNAS YGTEGLGSYP GYAPLPHLPP AFIPSYNAHY PKFLLPPYGM
     NCNGLSAVSS MNGINNFGLF PRLCPVYSNL LGGGSLPHPM LNPTSLPSSL PSDGARRLLQ
     PEHPREVLVP APHSAFSFTG AAASMKDKAC SPTSGSPTAG TAATAEHVVQ PKATSAAMAA
     PSSDEAMNLI KNKRNMTGYK TLPYPLKKQN GKIKYECNVC AKTFGQLSNL KVHLRVHSGE
     RPFKCQTCNK GFTQLAHLQK HYLVHTGEKP HECQVCHKRF SSTSNLKTHL RLHSGEKPYQ
     CKVCPAKFTQ FVHLKLHKRL HTRERPHKCS QCHKNYIHLC SLKVHLKGNC AAAPAPGLPL
     EDLTRINEEI EKFDISDNAD RLEDVEDDIS VISVVEKEIL AVVRKEKEET GLKVSLQRNM
     GNGLLSSGCS LYESSDLPLM KLPPSNPLPL VPVKVKQETV EPMDP
//
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