ID RRP7A_HUMAN Reviewed; 280 AA. AC Q9Y3A4; A4FTX2; B2RBG4; Q0VAD0; Q5JZ94; Q6P4B5; Q8IVR9; Q8IVY0; Q8N5Q3; AC Q8NEY6; Q9Y3H5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 2. DT 27-MAR-2024, entry version 176. DE RecName: Full=Ribosomal RNA-processing protein 7 homolog A; DE AltName: Full=Gastric cancer antigen Zg14; GN Name=RRP7A {ECO:0000312|HGNC:HGNC:24286}; ORFNames=CGI-96; 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 PRELIMINARY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-85. RC TISSUE=Brain, Duodenum, Liver, Lymph, 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-280. RC TISSUE=Gastric adenocarcinoma; RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321; RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.; RT "Serological identification and expression analysis of gastric cancer- RT associated genes."; RL Br. J. Cancer 86:1824-1830(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, 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 [8] RP INVOLVEMENT IN MCPH28, VARIANT MCPH28 CYS-155, CHARACTERIZATION OF VARIANT RP MCPH28 CYS-155, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP INTERACTION WITH NOL6. RX PubMed=33199730; DOI=10.1038/s41467-020-19658-0; RA Farooq M., Lindbaek L., Krogh N., Doganli C., Keller C., Moennich M., RA Goncalves A.B., Sakthivel S., Mang Y., Fatima A., Andersen V.S., RA Hussain M.S., Eiberg H., Hansen L., Kjaer K.W., Gopalakrishnan J., RA Pedersen L.B., Moellgaard K., Nielsen H., Baig S.M., Tommerup N., RA Christensen S.T., Larsen L.A.; RT "RRP7A links primary microcephaly to dysfunction of ribosome biogenesis, RT resorption of primary cilia, and neurogenesis."; RL Nat. Commun. 11:5816-5816(2020). RN [9] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=34516797; DOI=10.1126/science.abj5338; RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.; RT "Nucleolar maturation of the human small subunit processome."; RL Science 373:eabj5338-eabj5338(2021). CC -!- FUNCTION: Nucleolar protein that is involved in ribosomal RNA (rRNA) CC processing (PubMed:33199730). Also plays a role in primary cilia CC resorption, and cell cycle progression in neurogenesis and neocortex CC development (PubMed:33199730). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit. CC During the assembly of the SSU processome in the nucleolus, many CC ribosome biogenesis factors, an RNA chaperone and ribosomal proteins CC associate with the nascent pre-rRNA and work in concert to generate RNA CC folding, modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). CC {ECO:0000269|PubMed:33199730, ECO:0000269|PubMed:34516797}. CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 CC (PubMed:34516797). Interacts with NOL6; required for NOL6 localization CC to nucleolus. {ECO:0000269|PubMed:33199730, CC ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC Q9Y3A4; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-7223720, EBI-742909; CC Q9Y3A4; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-7223720, EBI-5278764; CC Q9Y3A4; O95257: GADD45G; NbExp=3; IntAct=EBI-7223720, EBI-448202; CC Q9Y3A4; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-7223720, EBI-1105213; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:33199730, CC ECO:0000269|PubMed:34516797}. Cell projection, cilium CC {ECO:0000269|PubMed:33199730}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:33199730}. CC -!- TISSUE SPECIFICITY: Expressed in the apical radial glial cells in the CC developing brain. {ECO:0000269|PubMed:33199730}. CC -!- DISEASE: Microcephaly 28, primary, autosomal recessive (MCPH28) CC [MIM:619453]: A form of microcephaly, a disease defined as a head CC circumference more than 3 standard deviations below the age, sex and CC ethnically matched mean. Brain weight is markedly reduced and the CC cerebral cortex is disproportionately small. MCPH28 is an autosomal CC recessive form characterized by reduced head size (down to -8 SD) and CC variably impaired intellectual development apparent from early CC childhood. {ECO:0000269|PubMed:33199730}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RRP7 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH31838.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AL022316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK314650; BAG37211.1; -; mRNA. DR EMBL; BC031838; AAH31838.1; ALT_INIT; mRNA. DR EMBL; BC041639; AAH41639.1; -; mRNA. DR EMBL; BC042335; AAH42335.1; -; mRNA. DR EMBL; BC063537; AAH63537.1; -; mRNA. DR EMBL; BC073834; AAH73834.1; -; mRNA. DR EMBL; BC121118; AAI21119.1; -; mRNA. DR EMBL; BC121119; AAI21120.1; -; mRNA. DR EMBL; AY039240; AAK68659.1; -; mRNA. DR CCDS; CCDS14036.1; -. DR RefSeq; NP_056518.2; NM_015703.4. DR PDB; 7MQ8; EM; 3.60 A; NI=1-280. DR PDB; 7MQ9; EM; 3.87 A; NI=1-280. DR PDB; 7MQA; EM; 2.70 A; NI=1-280. DR PDBsum; 7MQ8; -. DR PDBsum; 7MQ9; -. DR PDBsum; 7MQA; -. DR AlphaFoldDB; Q9Y3A4; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR SMR; Q9Y3A4; -. DR BioGRID; 118153; 109. DR ComplexPortal; CPX-2511; Small ribosomal subunit processome. DR IntAct; Q9Y3A4; 33. DR MINT; Q9Y3A4; -. DR STRING; 9606.ENSP00000321449; -. DR iPTMnet; Q9Y3A4; -. DR PhosphoSitePlus; Q9Y3A4; -. DR SwissPalm; Q9Y3A4; -. DR BioMuta; RRP7A; -. DR DMDM; 66774227; -. DR EPD; Q9Y3A4; -. DR jPOST; Q9Y3A4; -. DR MassIVE; Q9Y3A4; -. DR MaxQB; Q9Y3A4; -. DR PaxDb; 9606-ENSP00000321449; -. DR PeptideAtlas; Q9Y3A4; -. DR ProteomicsDB; 85996; -. DR Pumba; Q9Y3A4; -. DR Antibodypedia; 277; 155 antibodies from 26 providers. DR DNASU; 27341; -. DR Ensembl; ENST00000323013.7; ENSP00000321449.6; ENSG00000189306.11. DR GeneID; 27341; -. DR KEGG; hsa:27341; -. DR MANE-Select; ENST00000323013.7; ENSP00000321449.6; NM_015703.5; NP_056518.2. DR UCSC; uc003bcq.4; human. DR AGR; HGNC:24286; -. DR CTD; 27341; -. DR GeneCards; RRP7A; -. DR HGNC; HGNC:24286; RRP7A. DR HPA; ENSG00000189306; Low tissue specificity. DR MalaCards; RRP7A; -. DR MIM; 619449; gene. DR MIM; 619453; phenotype. DR neXtProt; NX_Q9Y3A4; -. DR OpenTargets; ENSG00000189306; -. DR PharmGKB; PA162402175; -. DR VEuPathDB; HostDB:ENSG00000189306; -. DR eggNOG; KOG4008; Eukaryota. DR GeneTree; ENSGT00390000018482; -. DR HOGENOM; CLU_036234_2_1_1; -. DR InParanoid; Q9Y3A4; -. DR OMA; VPPYCSE; -. DR OrthoDB; 5394928at2759; -. DR PhylomeDB; Q9Y3A4; -. DR TreeFam; TF313949; -. DR PathwayCommons; Q9Y3A4; -. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q9Y3A4; -. DR BioGRID-ORCS; 27341; 681 hits in 1123 CRISPR screens. DR ChiTaRS; RRP7A; human. DR GeneWiki; CTA-126B4.3; -. DR GenomeRNAi; 27341; -. DR Pharos; Q9Y3A4; Tbio. DR PRO; PR:Q9Y3A4; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9Y3A4; Protein. DR Bgee; ENSG00000189306; Expressed in mucosa of transverse colon and 114 other cell types or tissues. DR ExpressionAtlas; Q9Y3A4; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. DR GO; GO:0032545; C:CURI complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB. DR GO; GO:0034456; C:UTP-C complex; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl. DR GO; GO:0061523; P:cilium disassembly; IMP:UniProtKB. DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB. DR CDD; cd12294; RRM_Rrp7A; 1. DR CDD; cd12951; RRP7_Rrp7A; 1. DR Gene3D; 3.30.70.330; -; 1. DR Gene3D; 6.10.250.1770; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR040447; RRM_Rrp7. DR InterPro; IPR040446; RRP7. DR InterPro; IPR024326; RRP7_C. DR InterPro; IPR034890; Rrp7A_RRM. DR PANTHER; PTHR13191; RIBOSOMAL RNA PROCESSING PROTEIN 7-RELATED; 1. DR PANTHER; PTHR13191:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 7 HOMOLOG A; 1. DR Pfam; PF17799; RRM_Rrp7; 1. DR Pfam; PF12923; RRP7; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR Genevisible; Q9Y3A4; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell projection; Cytoplasm; Cytoskeleton; Disease variant; KW Intellectual disability; Nucleus; Phosphoprotein; Primary microcephaly; KW Reference proteome; RNA-binding. FT CHAIN 1..280 FT /note="Ribosomal RNA-processing protein 7 homolog A" FT /id="PRO_0000082008" FT DOMAIN 59..159 FT /note="RRM" FT /evidence="ECO:0000255" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT VARIANT 75 FT /note="L -> M (in dbSNP:rs8139383)" FT /id="VAR_052227" FT VARIANT 85 FT /note="V -> I (in dbSNP:rs1812240)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_052228" FT VARIANT 88 FT /note="V -> I (in dbSNP:rs11553441)" FT /id="VAR_052229" FT VARIANT 155 FT /note="W -> C (in MCPH28; increased proteolytic FT degradation; decreased recruitment to the nucleolus; FT decreased interaction with NOL6; decreased function in FT localization of NOL6 to the nucleolus; loss of function in FT rRNA processing; changed function in cilia resorption; FT dbSNP:rs1356719738)" FT /evidence="ECO:0000269|PubMed:33199730" FT /id="VAR_086134" FT CONFLICT 16..17 FT /note="RI -> SA (in Ref. 4; AAH31838)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="E -> K (in Ref. 2; BAG37211)" FT /evidence="ECO:0000305" SQ SEQUENCE 280 AA; 32334 MW; 3625D609B0FF2F76 CRC64; MVARRRKCAA RDPEDRIPSP LGYAAIPIKF SEKQQASHYL YVRAHGVRQG TKSTWPQKRT LFVLNVPPYC TEESLSRLLS TCGLVQSVEL QEKPDLAESP KESRSKFFHP KPVPGFQVAY VVFQKPSGVS AALALKGPLL VSTESHPVKS GIHKWISDYA DSVPDPEALR VEVDTFMEAY DQKIAEEEAK AKEEEGVPDE EGWVKVTRRG RRPVLPRTEA ASLRVLERER RKRSRKELLN FYAWQHRESK MEHLAQLRKK FEEDKQRIEL LRAQRKFRPY //