GenomeNet

Database: UniProt
Entry: Q14181
LinkDB: Q14181
Original site: Q14181 
ID   DPOA2_HUMAN             Reviewed;         598 AA.
AC   Q14181; B4DNB4; Q9BPV3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   12-AUG-2020, entry version 172.
DE   RecName: Full=DNA polymerase alpha subunit B;
DE   AltName: Full=DNA polymerase alpha 70 kDa subunit;
GN   Name=POLA2;
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).
RC   TISSUE=Cervix epithelium;
RX   PubMed=8223465; DOI=10.1002/j.1460-2075.1993.tb06144.x;
RA   Collins K.L., Russo A.A.R., Tseng B.Y., Kelly T.J.;
RT   "The role of the 70 kDa subunit of human DNA polymerase alpha in DNA
RT   replication.";
RL   EMBO J. 12:4555-4566(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Heart;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [6]
RP   PHOSPHORYLATION.
RX   PubMed=1902230;
RA   Nasheuer H.-P., Moore A., Wahl A.F., Wang T.S.-F.;
RT   "Cell cycle-dependent phosphorylation of human DNA polymerase alpha.";
RL   J. Biol. Chem. 266:7893-7903(1991).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX.
RX   PubMed=9705292; DOI=10.1074/jbc.273.34.21608;
RA   Schneider A., Smith R.W., Kautz A.R., Weisshart K., Grosse F.,
RA   Nasheuer H.P.;
RT   "Primase activity of human DNA polymerase alpha-primase. Divalent cations
RT   stabilize the enzyme activity of the p48 subunit.";
RL   J. Biol. Chem. 273:21608-21615(1998).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-127; THR-130;
RP   SER-141 AND SER-147, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP   IDENTIFICATION BY 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 THR-127; THR-130; SER-141;
RP   SER-147 AND SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127; THR-130; SER-141;
RP   SER-147; SER-152 AND SER-154, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: Accessory subunit of the DNA polymerase alpha complex (also
CC       known as the alpha DNA polymerase-primase complex) which plays an
CC       essential role in the initiation of DNA synthesis (PubMed:9705292).
CC       During the S phase of the cell cycle, the DNA polymerase alpha complex
CC       (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and
CC       two primase subunits, the catalytic subunit PRIM1 and the regulatory
CC       subunit PRIM2) is recruited to DNA at the replicative forks via direct
CC       interactions with MCM10 and WDHD1 (By similarity). The primase subunit
CC       of the polymerase alpha complex initiates DNA synthesis by
CC       oligomerising short RNA primers on both leading and lagging strands (By
CC       similarity). These primers are initially extended by the polymerase
CC       alpha catalytic subunit and subsequently transferred to polymerase
CC       delta and polymerase epsilon for processive synthesis on the lagging
CC       and leading strand, respectively (By similarity).
CC       {ECO:0000250|UniProtKB:P09884, ECO:0000250|UniProtKB:P20664,
CC       ECO:0000269|PubMed:9705292}.
CC   -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC       the alpha DNA polymerase-primase complex) consisting of four subunits:
CC       the catalytic subunit POLA1, the regulatory subunit POLA2, and primase
CC       complex subunits PRIM1 and PRIM2 respectively (PubMed:9705292). Within
CC       the complex, POLA1 directly interacts with PRIM2/p58 (By similarity).
CC       {ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:9705292}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14181-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14181-2; Sequence=VSP_056608, VSP_056609;
CC   -!- DOMAIN: The N-terminal 240 amino acids are sufficient to mediate
CC       complex formation.
CC   -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M phase.
CC       {ECO:0000269|PubMed:1902230}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC       {ECO:0000305}.
DR   EMBL; L24559; AAA16459.1; -; mRNA.
DR   EMBL; AK297842; BAG60176.1; -; mRNA.
DR   EMBL; CR456737; CAG33018.1; -; mRNA.
DR   EMBL; AP000944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002990; AAH02990.1; -; mRNA.
DR   EMBL; BC001347; AAH01347.1; -; mRNA.
DR   CCDS; CCDS8098.1; -. [Q14181-1]
DR   PIR; S39621; S39621.
DR   RefSeq; NP_002680.2; NM_002689.3. [Q14181-1]
DR   PDB; 2KEB; NMR; -; A=1-78.
DR   PDB; 4E2I; X-ray; 5.00 A; 1/2/3/4/5/6/7/8/9/U/W=1-78.
DR   PDB; 4Y97; X-ray; 2.51 A; A/C/E/G=1-598.
DR   PDB; 5EXR; X-ray; 3.60 A; D/H=2-598.
DR   PDBsum; 2KEB; -.
DR   PDBsum; 4E2I; -.
DR   PDBsum; 4Y97; -.
DR   PDBsum; 5EXR; -.
DR   SMR; Q14181; -.
DR   BioGRID; 117176; 71.
DR   ComplexPortal; CPX-2087; DNA polymerase alpha:primase complex.
DR   CORUM; Q14181; -.
DR   IntAct; Q14181; 50.
DR   MINT; Q14181; -.
DR   STRING; 9606.ENSP00000265465; -.
DR   ChEMBL; CHEMBL2363042; -.
DR   DrugBank; DB00851; Dacarbazine.
DR   DrugCentral; Q14181; -.
DR   iPTMnet; Q14181; -.
DR   PhosphoSitePlus; Q14181; -.
DR   SwissPalm; Q14181; -.
DR   BioMuta; POLA2; -.
DR   DMDM; 90110415; -.
DR   EPD; Q14181; -.
DR   jPOST; Q14181; -.
DR   MassIVE; Q14181; -.
DR   MaxQB; Q14181; -.
DR   PaxDb; Q14181; -.
DR   PeptideAtlas; Q14181; -.
DR   PRIDE; Q14181; -.
DR   ProteomicsDB; 4684; -.
DR   ProteomicsDB; 59900; -. [Q14181-1]
DR   Antibodypedia; 29737; 275 antibodies.
DR   DNASU; 23649; -.
DR   Ensembl; ENST00000265465; ENSP00000265465; ENSG00000014138. [Q14181-1]
DR   GeneID; 23649; -.
DR   KEGG; hsa:23649; -.
DR   UCSC; uc001odj.4; human. [Q14181-1]
DR   CTD; 23649; -.
DR   DisGeNET; 23649; -.
DR   EuPathDB; HostDB:ENSG00000014138.8; -.
DR   GeneCards; POLA2; -.
DR   HGNC; HGNC:30073; POLA2.
DR   HPA; ENSG00000014138; Low tissue specificity.
DR   neXtProt; NX_Q14181; -.
DR   OpenTargets; ENSG00000014138; -.
DR   PharmGKB; PA411; -.
DR   eggNOG; KOG1625; Eukaryota.
DR   GeneTree; ENSGT00390000016784; -.
DR   HOGENOM; CLU_014923_3_1_1; -.
DR   InParanoid; Q14181; -.
DR   KO; K02321; -.
DR   OMA; PFLDIEH; -.
DR   OrthoDB; 513979at2759; -.
DR   PhylomeDB; Q14181; -.
DR   TreeFam; TF314249; -.
DR   PathwayCommons; Q14181; -.
DR   Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR   Reactome; R-HSA-174430; Telomere C-strand synthesis initiation.
DR   Reactome; R-HSA-68952; DNA replication initiation.
DR   Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR   Reactome; R-HSA-69091; Polymerase switching.
DR   Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR   Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR   BioGRID-ORCS; 23649; 695 hits in 872 CRISPR screens.
DR   ChiTaRS; POLA2; human.
DR   EvolutionaryTrace; Q14181; -.
DR   GeneWiki; POLA2; -.
DR   GenomeRNAi; 23649; -.
DR   Pharos; Q14181; Tbio.
DR   PRO; PR:Q14181; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q14181; protein.
DR   Bgee; ENSG00000014138; Expressed in tonsil and 184 other tissues.
DR   ExpressionAtlas; Q14181; baseline and differential.
DR   Genevisible; Q14181; HS.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   Gene3D; 1.10.8.530; -; 1.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR043034; DNA_pol_alpha_B_N_sf.
DR   InterPro; IPR016722; DNA_pol_alpha_bsu.
DR   InterPro; IPR013627; Pol_alpha_B_N.
DR   PANTHER; PTHR23061; PTHR23061; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   Pfam; PF08418; Pol_alpha_B_N; 1.
DR   PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA replication; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN           1..598
FT                   /note="DNA polymerase alpha subunit B"
FT                   /id="PRO_0000194035"
FT   COMPBIAS        101..107
FT                   /note="Poly-Glu"
FT   COMPBIAS        115..157
FT                   /note="Pro/Ser/Thr-rich"
FT   COMPBIAS        486..489
FT                   /note="Poly-Ser"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         127
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   MOD_RES         130
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         1..208
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056608"
FT   VAR_SEQ         550..598
FT                   /note="DVLGCVCVNPGRLTKGQVGGTFARLYLRRPAADGAERQSPCIAVQVVRI ->
FT                   VGLNSAFSQKHQNPVFDFPF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056609"
FT   VARIANT         583
FT                   /note="G -> R (in dbSNP:rs487989)"
FT                   /id="VAR_033896"
FT   VARIANT         588
FT                   /note="S -> N (in dbSNP:rs7123885)"
FT                   /id="VAR_033897"
FT   CONFLICT        383..384
FT                   /note="DA -> ES (in Ref. 1; AAA16459)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..15
FT                   /evidence="ECO:0000244|PDB:2KEB"
FT   HELIX           21..34
FT                   /evidence="ECO:0000244|PDB:2KEB"
FT   HELIX           38..52
FT                   /evidence="ECO:0000244|PDB:2KEB"
FT   HELIX           59..68
FT                   /evidence="ECO:0000244|PDB:2KEB"
FT   HELIX           70..73
FT                   /evidence="ECO:0000244|PDB:2KEB"
FT   HELIX           159..162
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          170..176
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          178..180
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          193..195
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           213..234
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          251..263
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   TURN            267..269
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          270..274
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           276..279
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          283..287
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          292..296
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          301..307
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          309..312
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          314..319
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           333..336
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          340..347
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           358..370
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          373..379
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          381..383
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           387..390
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           398..412
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           414..416
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          419..423
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          434..437
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           449..451
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          453..455
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          458..464
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          467..471
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           476..481
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          485..488
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           494..505
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   HELIX           522..528
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          532..534
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          536..539
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          547..551
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          554..558
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          562..564
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          570..576
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          583..585
FT                   /evidence="ECO:0000244|PDB:4Y97"
FT   STRAND          589..597
FT                   /evidence="ECO:0000244|PDB:4Y97"
SQ   SEQUENCE   598 AA;  65948 MW;  F5CBD7E022ADDDBF CRC64;
     MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT STHKVGLTSE
     ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI EVEEEEEILL NSYTTPSKGS
     QKRAISTPET PLTKRSVSTR SPHQLLSPSS FSPSATPSQK YNSRSNRGEV VTSFGLAQGV
     SWSGRGGAGN ISLKVLGCPE ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF
     TPLLAPAQEP VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ
     VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT TSDSITYDPL
     LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED IFKQCLRTII EGTRSSGSHL
     VFVPSLRDVH HEPVYPQPPF SYSDLSREDK KQVQFVSEPC SLSINGVIFG LTSTDLLFHL
     GAEEISSSSG TSDRFSRILK HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII
     PSELRYFVKD VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI
//
DBGET integrated database retrieval system