ID KPRB_HUMAN Reviewed; 369 AA. AC O60256; B4E1M8; B4E329; B7ZKZ1; E7EMY2; Q6IAS2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 12-AUG-2020, entry version 161. DE RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2; DE Short=PRPP synthase-associated protein 2; DE AltName: Full=41 kDa phosphoribosypyrophosphate synthetase-associated protein; DE Short=PAP41; GN Name=PRPSAP2; 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). RX PubMed=9545573; DOI=10.1016/s0167-4781(97)00217-0; RA Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T., RA Tatibana M., Itakura M.; RT "Molecular cloning of a human cDNA for the 41-kDa RT phosphoribosylpyrophosphate synthetase-associated protein."; RL Biochim. Biophys. Acta 1396:245-250(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Trachea; 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=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Uterus; 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 PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232; RP 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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-227, AND IDENTIFICATION BY RP 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 SER-227, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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-227, AND IDENTIFICATION BY RP 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-5, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-227 AND SER-233, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369. RG Structural genomics consortium (SGC); RT "Human phosphoribosylpyrophosphate synthetase-associated protein 41 RT (Pap41)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose CC 1-diphosphate synthesis. CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. CC -!- INTERACTION: CC O60256; P60891: PRPS1; NbExp=8; IntAct=EBI-724960, EBI-749195; CC O60256; P11908-2: PRPS2; NbExp=4; IntAct=EBI-724960, EBI-12063547; CC O60256; Q14558: PRPSAP1; NbExp=6; IntAct=EBI-724960, EBI-724449; CC O60256; O60256: PRPSAP2; NbExp=3; IntAct=EBI-724960, EBI-724960; CC O60256; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-724960, EBI-11523345; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O60256-1; Sequence=Displayed; CC Name=2; CC IsoId=O60256-2; Sequence=VSP_044731; CC Name=3; CC IsoId=O60256-3; Sequence=VSP_046462; CC Name=4; CC IsoId=O60256-4; Sequence=VSP_054765; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB007851; BAA25435.1; -; mRNA. DR EMBL; AK303911; BAG64840.1; -; mRNA. DR EMBL; AK304544; BAG65341.1; -; mRNA. DR EMBL; CR457082; CAG33363.1; -; mRNA. DR EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC106050; AAI06051.1; -; mRNA. DR EMBL; BC101670; AAI01671.1; -; mRNA. DR EMBL; BC101672; AAI01673.1; -; mRNA. DR EMBL; BC143475; AAI43476.1; -; mRNA. DR CCDS; CCDS11200.1; -. [O60256-1] DR CCDS; CCDS58525.1; -. [O60256-3] DR CCDS; CCDS58526.1; -. [O60256-2] DR CCDS; CCDS58527.1; -. [O60256-4] DR RefSeq; NP_001230865.1; NM_001243936.1. [O60256-2] DR RefSeq; NP_001230869.1; NM_001243940.1. [O60256-3] DR RefSeq; NP_001230870.1; NM_001243941.1. [O60256-4] DR RefSeq; NP_001230871.1; NM_001243942.1. [O60256-4] DR RefSeq; NP_002758.1; NM_002767.3. [O60256-1] DR RefSeq; XP_005256782.1; XM_005256725.2. DR RefSeq; XP_005256783.1; XM_005256726.1. DR RefSeq; XP_005256786.1; XM_005256729.4. DR RefSeq; XP_016880354.1; XM_017024865.1. [O60256-1] DR RefSeq; XP_016880355.1; XM_017024866.1. [O60256-1] DR RefSeq; XP_016880356.1; XM_017024867.1. DR RefSeq; XP_016880360.1; XM_017024871.1. [O60256-4] DR RefSeq; XP_016880361.1; XM_017024872.1. DR RefSeq; XP_016880362.1; XM_017024873.1. [O60256-4] DR RefSeq; XP_016880363.1; XM_017024874.1. [O60256-4] DR RefSeq; XP_016880364.1; XM_017024875.1. [O60256-4] DR RefSeq; XP_016880365.1; XM_017024876.1. DR PDB; 2JI4; X-ray; 2.55 A; A=13-369. DR PDBsum; 2JI4; -. DR SMR; O60256; -. DR BioGRID; 111619; 45. DR IntAct; O60256; 50. DR MINT; O60256; -. DR STRING; 9606.ENSP00000268835; -. DR BindingDB; O60256; -. DR ChEMBL; CHEMBL2646; -. DR iPTMnet; O60256; -. DR PhosphoSitePlus; O60256; -. DR BioMuta; PRPSAP2; -. DR EPD; O60256; -. DR jPOST; O60256; -. DR MassIVE; O60256; -. DR MaxQB; O60256; -. DR PaxDb; O60256; -. DR PeptideAtlas; O60256; -. DR PRIDE; O60256; -. DR ProteomicsDB; 17038; -. DR ProteomicsDB; 49283; -. [O60256-1] DR ProteomicsDB; 5873; -. DR ProteomicsDB; 7202; -. DR Antibodypedia; 13570; 142 antibodies. DR Ensembl; ENST00000268835; ENSP00000268835; ENSG00000141127. [O60256-1] DR Ensembl; ENST00000419071; ENSP00000392536; ENSG00000141127. [O60256-2] DR Ensembl; ENST00000536323; ENSP00000443967; ENSG00000141127. [O60256-4] DR Ensembl; ENST00000542013; ENSP00000439129; ENSG00000141127. [O60256-3] DR Ensembl; ENST00000610773; ENSP00000481322; ENSG00000141127. [O60256-4] DR GeneID; 5636; -. DR KEGG; hsa:5636; -. DR UCSC; uc002guo.3; human. [O60256-1] DR CTD; 5636; -. DR DisGeNET; 5636; -. DR EuPathDB; HostDB:ENSG00000141127.14; -. DR GeneCards; PRPSAP2; -. DR HGNC; HGNC:9467; PRPSAP2. DR HPA; ENSG00000141127; Low tissue specificity. DR MIM; 603762; gene. DR neXtProt; NX_O60256; -. DR OpenTargets; ENSG00000141127; -. DR PharmGKB; PA33822; -. DR eggNOG; KOG1503; Eukaryota. DR GeneTree; ENSGT00950000182803; -. DR HOGENOM; CLU_033546_0_0_1; -. DR InParanoid; O60256; -. DR OMA; HYAYARS; -. DR OrthoDB; 1043963at2759; -. DR PhylomeDB; O60256; -. DR TreeFam; TF106367; -. DR PathwayCommons; O60256; -. DR BioGRID-ORCS; 5636; 6 hits in 870 CRISPR screens. DR ChiTaRS; PRPSAP2; human. DR EvolutionaryTrace; O60256; -. DR GeneWiki; PRPSAP2; -. DR GenomeRNAi; 5636; -. DR Pharos; O60256; Tbio. DR PRO; PR:O60256; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O60256; protein. DR Bgee; ENSG00000141127; Expressed in cortical plate and 237 other tissues. DR ExpressionAtlas; O60256; baseline and differential. DR Genevisible; O60256; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central. DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0060348; P:bone development; IEA:Ensembl. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR CDD; cd06223; PRTases_typeI; 1. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR PANTHER; PTHR10210; PTHR10210; 1. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 2. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Nucleotide biosynthesis; Phosphoprotein; Reference proteome. FT CHAIN 1..369 FT /note="Phosphoribosyl pyrophosphate synthase-associated FT protein 2" FT /id="PRO_0000141082" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000244|PubMed:19413330" FT MOD_RES 5 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569, ECO:0000269|Ref.6" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT VAR_SEQ 1..86 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054765" FT VAR_SEQ 41..80 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044731" FT VAR_SEQ 269..317 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046462" FT CONFLICT 121 FT /note="K -> R (in Ref. 2; BAG64840)" FT /evidence="ECO:0000305" FT STRAND 21..24 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 29..32 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 33..42 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 49..53 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 59..63 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 71..75 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 82..98 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 102..107 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 126..136 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 141..146 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 150..155 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 156..158 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 160..163 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 166..176 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 180..182 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 183..189 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 190..192 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 193..202 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 206..210 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 256..258 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 263..272 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 276..287 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 292..300 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 306..312 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 317..324 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 327..331 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 336..339 FT /evidence="ECO:0000244|PDB:2JI4" FT HELIX 342..354 FT /evidence="ECO:0000244|PDB:2JI4" FT STRAND 362..364 FT /evidence="ECO:0000244|PDB:2JI4" SQ SEQUENCE 369 AA; 40926 MW; 12A0E46BD4AC55BF CRC64; MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY LFRNIGLDD //