ID DDRGK_HUMAN Reviewed; 314 AA. AC Q96HY6; A6NIU5; C9JSZ5; Q9BW47; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 2. DT 18-SEP-2019, entry version 152. DE RecName: Full=DDRGK domain-containing protein 1 {ECO:0000305}; DE AltName: Full=Dashurin {ECO:0000303|PubMed:20036718}; DE AltName: Full=UFM1-binding and PCI domain-containing protein 1 {ECO:0000305}; DE Flags: Precursor; GN Name=DDRGK1 {ECO:0000312|HGNC:HGNC:16110}; GN Synonyms=C20orf116 {ECO:0000312|HGNC:HGNC:16110}, UFBP1; 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), AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=20036718; DOI=10.1016/j.bbagen.2009.12.004; RA Neziri D., Ilhan A., Maj M., Majdic O., Baumgartner-Parzer S., RA Cohen G., Base W., Wagner L.; RT "Cloning and molecular characterization of Dashurin encoded by RT C20orf116, a PCI-domain containing protein."; RL Biochim. Biophys. Acta 1800:430-438(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP THR-303. RC TISSUE=Brain, 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP UFMYLATION AT LYS-267, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MUTAGENESIS OF LYS-116; LYS-121; LYS-124; LYS-128; LYS-193; LYS-224; RP LYS-227 AND LYS-267. RX PubMed=20018847; DOI=10.1074/jbc.m109.036814; RA Tatsumi K., Sou Y.S., Tada N., Nakamura E., Iemura S., Natsume T., RA Kang S.H., Chung C.H., Kasahara M., Kominami E., Yamamoto M., RA Tanaka K., Komatsu M.; RT "A novel type of E3 ligase for the Ufm1 conjugation system."; RL J. Biol. Chem. 285:5417-5427(2010). RN [7] RP INTERACTION WITH CDK5RAP3, REGION, SUBCELLULAR LOCATION, AND RP UBIQUITINATION. RX PubMed=20228063; DOI=10.1074/jbc.m110.110619; RA Wu J., Lei G., Mei M., Tang Y., Li H.; RT "A novel C53/LZAP-interacting protein regulates stability of C53/LZAP RT and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB RT signaling."; RL J. Biol. Chem. 285:15126-15136(2010). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [10] RP FUNCTION, AND INTERACTION WITH NFKBIA. RX PubMed=23675531; DOI=10.1371/journal.pone.0064231; RA Xi P., Ding D., Zhou J., Wang M., Cong Y.S.; RT "DDRGK1 regulates NF-kappaB activity by modulating IkappaBalpha RT stability."; RL PLoS ONE 8:E64231-E64231(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION RP 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., 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 [12] RP FUNCTION, INTERACTION WITH TRIP4 AND UFL1, REGION, AND MUTAGENESIS OF RP LYS-267. RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007; RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., RA Ka S.H., Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., RA Baek S.H., Jeon Y.J., Chung C.H.; RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation RT and breast cancer development."; RL Mol. Cell 56:261-274(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP INVOLVEMENT IN SEMDSH, FUNCTION, AND INTERACTION WITH SOX9. RX PubMed=28263186; DOI=10.1172/jci90193; RA Egunsola A.T., Bae Y., Jiang M.M., Liu D.S., Chen-Evenson Y., RA Bertin T., Chen S., Lu J.T., Nevarez L., Magal N., Raas-Rothschild A., RA Swindell E.C., Cohn D.H., Gibbs R.A., Campeau P.M., Shohat M., RA Lee B.H.; RT "Loss of DDRGK1 modulates SOX9 ubiquitination in RT spondyloepimetaphyseal dysplasia."; RL J. Clin. Invest. 127:1475-1484(2017). CC -!- FUNCTION: Protein which interacts with the E3 UFM1-protein ligase CC UFL1 and one of its substrates TRIP4 and is required for TRIP4 CC ufmylation. Through TRIP4 ufmylation may regulate nuclear CC receptors-mediated transcription (PubMed:25219498). May play a CC role in NF-kappa-B-mediated transcription through regulation of CC the phosphorylation and the degradation of NFKBIA, the inhibitor CC of NF-kappa-B (PubMed:23675531). May also play a role in the CC cellular response to endoplasmic reticulum stress (By similarity). CC Plays a role in cartilage development through SOX9, inhibiting the CC ubiquitin-mediated proteasomal degradation of this transcriptional CC regulator (PubMed:28263186). {ECO:0000250|UniProtKB:Q80WW9, CC ECO:0000269|PubMed:23675531, ECO:0000269|PubMed:25219498, CC ECO:0000269|PubMed:28263186}. CC -!- SUBUNIT: Interacts with TRIP4; the interaction with TRIP4 is CC direct (PubMed:25219498). Interacts with UFL1 (PubMed:25219498). CC Interacts with NFKBIA (PubMed:23675531). Interacts with CDK5RAP3 CC (PubMed:20228063). Interacts with SOX9 (PubMed:28263186). CC {ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:23675531, CC ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:28263186}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:20018847}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96HY6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96HY6-2; Sequence=VSP_008391; CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). In the CC brain, highest levels in medulla oblongata, followed by cerebral CC cortex, cerebellum and frontal lobe. {ECO:0000269|PubMed:20018847, CC ECO:0000269|PubMed:20036718}. CC -!- PTM: Ubiquitinated. Ubiquitination probably triggers proteasomal CC degradation and is negatively regulated by UFL1, the enzyme CC involved in the ufmylation of DDRGK1. CC {ECO:0000269|PubMed:20228063}. CC -!- PTM: Ufmylated. Conjugated to ubiquitin-like protein UFM1, CC probably at Lys-267 by UFL1. {ECO:0000269|PubMed:20018847}. CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Shohat type (SEMDSH) CC [MIM:602557]: An autosomal recessive skeletal dysplasia that CC affects cartilage development. It is characterized by vertebral, CC epiphyseal, and metaphyseal abnormalities, including scoliosis CC with vertebral compression fractures, flattened vertebral bodies, CC and hypomineralization of long bones. Affected individuals may CC exhibit a small trunk, short neck, small limbs, joint laxity, CC bowlegs, and/or abdominal distension with hepatosplenomegaly. CC {ECO:0000269|PubMed:28263186}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DDRGK1 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; AL121891; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10544.1; -; Genomic_DNA. DR EMBL; BC000643; AAH00643.1; -; mRNA. DR EMBL; BC007957; AAH07957.1; -; mRNA. DR EMBL; BC011851; AAH11851.1; -; mRNA. DR CCDS; CCDS13050.1; -. [Q96HY6-1] DR RefSeq; NP_076424.1; NM_023935.2. [Q96HY6-1] DR BioGrid; 122441; 46. DR IntAct; Q96HY6; 30. DR MINT; Q96HY6; -. DR STRING; 9606.ENSP00000346483; -. DR iPTMnet; Q96HY6; -. DR PhosphoSitePlus; Q96HY6; -. DR BioMuta; DDRGK1; -. DR DMDM; 37077728; -. DR EPD; Q96HY6; -. DR jPOST; Q96HY6; -. DR MassIVE; Q96HY6; -. DR MaxQB; Q96HY6; -. DR PaxDb; Q96HY6; -. DR PeptideAtlas; Q96HY6; -. DR PRIDE; Q96HY6; -. DR ProteomicsDB; 76794; -. [Q96HY6-1] DR ProteomicsDB; 76795; -. [Q96HY6-2] DR DNASU; 65992; -. DR Ensembl; ENST00000354488; ENSP00000346483; ENSG00000198171. [Q96HY6-1] DR GeneID; 65992; -. DR KEGG; hsa:65992; -. DR UCSC; uc002wic.4; human. [Q96HY6-1] DR CTD; 65992; -. DR DisGeNET; 65992; -. DR GeneCards; DDRGK1; -. DR HGNC; HGNC:16110; DDRGK1. DR HPA; HPA013373; -. DR HPA; HPA013705; -. DR MalaCards; DDRGK1; -. DR MIM; 602557; phenotype. DR MIM; 616177; gene. DR neXtProt; NX_Q96HY6; -. DR OpenTargets; ENSG00000198171; -. DR Orphanet; 93352; Spondyloepimetaphyseal dysplasia, Shohat type. DR PharmGKB; PA164718734; -. DR eggNOG; KOG3054; Eukaryota. DR eggNOG; ENOG4111IPW; LUCA. DR GeneTree; ENSGT00390000017193; -. DR HOGENOM; HOG000005758; -. DR InParanoid; Q96HY6; -. DR KO; K23344; -. DR OMA; EERGAGM; -. DR OrthoDB; 1553559at2759; -. DR PhylomeDB; Q96HY6; -. DR TreeFam; TF314645; -. DR ChiTaRS; DDRGK1; human. DR GenomeRNAi; 65992; -. DR Pharos; Q96HY6; -. DR PRO; PR:Q96HY6; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000198171; Expressed in 216 organ(s), highest expression level in tendon of biceps brachii. DR ExpressionAtlas; Q96HY6; baseline and differential. DR Genevisible; Q96HY6; HS. DR GO; GO:0005737; C:cytoplasm; TAS:ParkinsonsUK-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB. DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:ParkinsonsUK-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IC:ParkinsonsUK-UCL. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ParkinsonsUK-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:ParkinsonsUK-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IMP:UniProtKB. DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:ParkinsonsUK-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; ISS:ParkinsonsUK-UCL. DR GO; GO:1905636; P:positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IMP:ParkinsonsUK-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL. DR GO; GO:1990592; P:protein K69-linked ufmylation; IDA:UniProtKB. DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR019153; DDRGK_dom-contain. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR Pfam; PF09756; DDRGK; 1. DR SMART; SM01128; DDRGK; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Dwarfism; KW Endoplasmic reticulum; Isopeptide bond; Phosphoprotein; Polymorphism; KW Reference proteome; Signal; Ubl conjugation. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 314 DDRGK domain-containing protein 1. FT /FTId=PRO_0000021033. FT DOMAIN 229 273 PCI. FT REGION 1 114 Mediates interaction with CDK5RAP3. FT {ECO:0000269|PubMed:20228063}. FT REGION 118 216 Mediates interaction with TRIP4. FT {ECO:0000269|PubMed:25219498}. FT REGION 216 314 Mediates interaction with UFL1. FT {ECO:0000269|PubMed:25219498}. FT MOD_RES 72 72 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 114 114 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT CROSSLNK 267 267 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in UFM1). FT {ECO:0000305|PubMed:20018847}. FT VAR_SEQ 244 299 DTINRIQDLLAEGTITGVIDDRGKFIYITPEELAAVANFIR FT QRGRVSIAELAQASN -> VSPGTWPAVCSVARGLWLAERT FT CPKDRVLMHRLPCPQPRVSSAQKSPGTLGILHF (in FT isoform 2). {ECO:0000305}. FT /FTId=VSP_008391. FT VARIANT 303 303 A -> T (in dbSNP:rs11591). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_016923. FT MUTAGEN 116 116 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 121 121 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 124 124 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 128 128 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 193 193 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 224 224 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 227 227 K->R: Weak or no effect on ufmylation. FT {ECO:0000269|PubMed:20018847}. FT MUTAGEN 267 267 K->R: Impairs ufmylation. Impairs FT interaction with UFL1. FT {ECO:0000269|PubMed:20018847, FT ECO:0000269|PubMed:25219498}. SQ SEQUENCE 314 AA; 35611 MW; 2190D30B0D6D674A CRC64; MVAPVWYLVA AALLVGFILF LTRSRGRAAS AGQEPLHNEE LAGAGRVAQP GPLEPEEPRA GGRPRRRRDL GSRLQAQRRA QRVAWAEADE NEEEAVILAQ EEEGVEKPAE THLSGKIGAK KLRKLEEKQA RKAQREAEEA EREERKRLES QREAEWKKEE ERLRLEEEQK EEEERKAREE QAQREHEEYL KLKEAFVVEE EGVGETMTEE QSQSFLTEFI NYIKQSKVVL LEDLASQVGL RTQDTINRIQ DLLAEGTITG VIDDRGKFIY ITPEELAAVA NFIRQRGRVS IAELAQASNS LIAWGRESPA QAPA //