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 13-FEB-2019, entry version 151. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA 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 RT the 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 RT project: 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 RP BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION RP BY 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 RP 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION RP 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 SER-227, AND IDENTIFICATION RP BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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 RP MASS 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 RP SER-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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- CC phosphoribose 1-diphosphate synthesis. CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. CC -!- INTERACTION: CC P60891:PRPS1; NbExp=5; IntAct=EBI-724960, EBI-749195; CC Q14558:PRPSAP1; NbExp=4; IntAct=EBI-724960, EBI-724449; 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 Note=No experimental confirmation available.; CC Name=3; CC IsoId=O60256-3; Sequence=VSP_046462; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O60256-4; Sequence=VSP_054765; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {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 UniGene; Hs.632236; -. DR PDB; 2JI4; X-ray; 2.55 A; A=13-369. DR PDBsum; 2JI4; -. DR ProteinModelPortal; O60256; -. DR SMR; O60256; -. DR BioGrid; 111619; 37. DR IntAct; O60256; 14. 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 MaxQB; O60256; -. DR PaxDb; O60256; -. DR PeptideAtlas; O60256; -. DR PRIDE; O60256; -. DR ProteomicsDB; 49283; -. 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; HPA021881; -. DR MIM; 603762; gene. DR neXtProt; NX_O60256; -. DR OpenTargets; ENSG00000141127; -. DR PharmGKB; PA33822; -. DR eggNOG; KOG1503; Eukaryota. DR eggNOG; COG0462; LUCA. DR GeneTree; ENSGT00940000153482; -. DR HOGENOM; HOG000210451; -. DR HOVERGEN; HBG001520; -. DR InParanoid; O60256; -. DR OMA; HYAYARS; -. DR OrthoDB; 1043963at2759; -. DR PhylomeDB; O60256; -. DR TreeFam; TF106367; -. DR ChiTaRS; PRPSAP2; human. DR EvolutionaryTrace; O60256; -. DR GeneWiki; PRPSAP2; -. DR GenomeRNAi; 5636; -. DR PRO; PR:O60256; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000141127; Expressed in 223 organ(s), highest expression level in testis. 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; Complete proteome; KW Direct protein sequencing; Nucleotide biosynthesis; Phosphoprotein; KW Reference proteome. FT CHAIN 1 369 Phosphoribosyl pyrophosphate synthase- FT associated protein 2. FT /FTId=PRO_0000141082. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19413330}. FT MOD_RES 5 5 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 219 219 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 227 227 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569, FT ECO:0000269|Ref.6}. FT MOD_RES 233 233 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT VAR_SEQ 1 86 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054765. FT VAR_SEQ 41 80 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044731. FT VAR_SEQ 269 317 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_046462. FT CONFLICT 121 121 K -> R (in Ref. 2; BAG64840). FT {ECO:0000305}. FT STRAND 21 24 {ECO:0000244|PDB:2JI4}. FT HELIX 29 32 {ECO:0000244|PDB:2JI4}. FT HELIX 33 42 {ECO:0000244|PDB:2JI4}. FT STRAND 49 53 {ECO:0000244|PDB:2JI4}. FT STRAND 59 63 {ECO:0000244|PDB:2JI4}. FT STRAND 71 75 {ECO:0000244|PDB:2JI4}. FT HELIX 82 98 {ECO:0000244|PDB:2JI4}. FT STRAND 102 107 {ECO:0000244|PDB:2JI4}. FT HELIX 126 136 {ECO:0000244|PDB:2JI4}. FT STRAND 141 146 {ECO:0000244|PDB:2JI4}. FT HELIX 150 155 {ECO:0000244|PDB:2JI4}. FT STRAND 156 158 {ECO:0000244|PDB:2JI4}. FT STRAND 160 163 {ECO:0000244|PDB:2JI4}. FT HELIX 166 176 {ECO:0000244|PDB:2JI4}. FT HELIX 180 182 {ECO:0000244|PDB:2JI4}. FT STRAND 183 189 {ECO:0000244|PDB:2JI4}. FT HELIX 190 192 {ECO:0000244|PDB:2JI4}. FT HELIX 193 202 {ECO:0000244|PDB:2JI4}. FT STRAND 206 210 {ECO:0000244|PDB:2JI4}. FT STRAND 256 258 {ECO:0000244|PDB:2JI4}. FT STRAND 263 272 {ECO:0000244|PDB:2JI4}. FT HELIX 276 287 {ECO:0000244|PDB:2JI4}. FT STRAND 292 300 {ECO:0000244|PDB:2JI4}. FT HELIX 306 312 {ECO:0000244|PDB:2JI4}. FT STRAND 317 324 {ECO:0000244|PDB:2JI4}. FT HELIX 327 331 {ECO:0000244|PDB:2JI4}. FT STRAND 336 339 {ECO:0000244|PDB:2JI4}. FT HELIX 342 354 {ECO:0000244|PDB:2JI4}. FT STRAND 362 364 {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 //