DPOA2_HUMAN
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 03-AUG-2022, entry version 181.
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; DOI=10.1016/s0021-9258(20)89534-9;
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 2-598, AND SUBUNIT.
RX PubMed=26975377; DOI=10.1074/jbc.m116.717405;
RA Baranovskiy A.G., Babayeva N.D., Zhang Y., Gu J., Suwa Y., Pavlov Y.I.,
RA Tahirov T.H.;
RT "Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.";
RL J. Biol. Chem. 291:10006-10020(2016).
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,
CC PubMed:26975377). Within the complex, POLA1 directly interacts with
CC PRIM2/p58 (By similarity). {ECO:0000250|UniProtKB:P20664,
CC ECO:0000269|PubMed:9705292}.
CC -!- INTERACTION:
CC Q14181; P55212: CASP6; NbExp=3; IntAct=EBI-712752, EBI-718729;
CC Q14181; O75460-2: ERN1; NbExp=3; IntAct=EBI-712752, EBI-25852368;
CC Q14181; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-712752, EBI-10226858;
CC Q14181; P54652: HSPA2; NbExp=3; IntAct=EBI-712752, EBI-356991;
CC Q14181; P13473-2: LAMP2; NbExp=3; IntAct=EBI-712752, EBI-21591415;
CC Q14181; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-712752, EBI-5280197;
CC Q14181; P62826: RAN; NbExp=3; IntAct=EBI-712752, EBI-286642;
CC Q14181; P49591: SARS1; NbExp=3; IntAct=EBI-712752, EBI-1053431;
CC Q14181; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712752, EBI-2623095;
CC Q14181; P31948: STIP1; NbExp=3; IntAct=EBI-712752, EBI-1054052;
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}.
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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 PDB; 7OPL; EM; 4.12 A; B=149-598.
DR PDBsum; 2KEB; -.
DR PDBsum; 4E2I; -.
DR PDBsum; 4Y97; -.
DR PDBsum; 5EXR; -.
DR PDBsum; 7OPL; -.
DR AlphaFoldDB; Q14181; -.
DR BMRB; Q14181; -.
DR SMR; Q14181; -.
DR BioGRID; 117176; 88.
DR ComplexPortal; CPX-2087; DNA polymerase alpha:primase complex.
DR CORUM; Q14181; -.
DR IntAct; Q14181; 67.
DR MINT; Q14181; -.
DR STRING; 9606.ENSP00000265465; -.
DR ChEMBL; CHEMBL2363042; -.
DR DrugBank; DB00851; Dacarbazine.
DR DrugCentral; Q14181; -.
DR GlyGen; Q14181; 1 site, 1 O-linked glycan (1 site).
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; 300 antibodies from 28 providers.
DR DNASU; 23649; -.
DR Ensembl; ENST00000265465.8; ENSP00000265465.3; ENSG00000014138.9. [Q14181-1]
DR GeneID; 23649; -.
DR KEGG; hsa:23649; -.
DR MANE-Select; ENST00000265465.8; ENSP00000265465.3; NM_002689.4; NP_002680.2.
DR UCSC; uc001odj.4; human. [Q14181-1]
DR CTD; 23649; -.
DR DisGeNET; 23649; -.
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 VEuPathDB; HostDB:ENSG00000014138; -.
DR eggNOG; KOG1625; Eukaryota.
DR GeneTree; ENSGT00390000016784; -.
DR HOGENOM; CLU_014923_3_1_1; -.
DR InParanoid; Q14181; -.
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 Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; Q14181; -.
DR SIGNOR; Q14181; -.
DR BioGRID-ORCS; 23649; 725 hits in 1082 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 ventricular zone and 130 other tissues.
DR ExpressionAtlas; Q14181; baseline and differential.
DR Genevisible; Q14181; HS.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:UniProtKB.
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; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
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; Reference proteome.
FT CHAIN 1..598
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194035"
FT REGION 112..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:2KEB"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:2KEB"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2KEB"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:2KEB"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:2KEB"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 213..234
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 251..263
FT /evidence="ECO:0007829|PDB:4Y97"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 476..481
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 494..505
FT /evidence="ECO:0007829|PDB:4Y97"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:4Y97"
FT STRAND 589..597
FT /evidence="ECO:0007829|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
