KPRB_HUMAN
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 03-AUG-2022, entry version 170.
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}.
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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 AlphaFoldDB; O60256; -.
DR SMR; O60256; -.
DR BioGRID; 111619; 84.
DR IntAct; O60256; 50.
DR MINT; O60256; -.
DR STRING; 9606.ENSP00000268835; -.
DR BindingDB; O60256; -.
DR ChEMBL; CHEMBL2646; -.
DR GlyGen; O60256; 1 site, 1 O-linked glycan (1 site).
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; 147 antibodies from 23 providers.
DR DNASU; 5636; -.
DR Ensembl; ENST00000268835.7; ENSP00000268835.2; ENSG00000141127.15. [O60256-1]
DR Ensembl; ENST00000419071.6; ENSP00000392536.2; ENSG00000141127.15. [O60256-2]
DR Ensembl; ENST00000536323.5; ENSP00000443967.1; ENSG00000141127.15. [O60256-4]
DR Ensembl; ENST00000542013.5; ENSP00000439129.1; ENSG00000141127.15. [O60256-3]
DR Ensembl; ENST00000610773.4; ENSP00000481322.1; ENSG00000141127.15. [O60256-4]
DR GeneID; 5636; -.
DR KEGG; hsa:5636; -.
DR MANE-Select; ENST00000268835.7; ENSP00000268835.2; NM_002767.4; NP_002758.1.
DR UCSC; uc002guo.3; human. [O60256-1]
DR CTD; 5636; -.
DR DisGeNET; 5636; -.
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 VEuPathDB; HostDB:ENSG00000141127; -.
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 SignaLink; O60256; -.
DR BioGRID-ORCS; 5636; 17 hits in 1079 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 202 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:0042802; F:identical protein binding; IPI:IntAct.
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:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
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:0007744|PubMed:19413330"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:2JI4"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2JI4"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:2JI4"
FT STRAND 362..364
FT /evidence="ECO:0007829|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
