ID UB2J2_HUMAN Reviewed; 259 AA. AC Q8N2K1; A8MYC7; Q504T9; Q96N26; Q96T84; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUL-2009, sequence version 3. DT 27-MAR-2024, entry version 178. DE RecName: Full=Ubiquitin-conjugating enzyme E2 J2; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme J2; DE AltName: Full=Non-canonical ubiquitin-conjugating enzyme 2; DE Short=NCUBE-2; GN Name=UBE2J2; Synonyms=NCUBE2; 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=11278356; DOI=10.1074/jbc.m007640200; RA Tiwari S., Weissman A.M.; RT "Endoplasmic reticulum (ER)-associated degradation of T cell receptor RT subunits. Involvement of ER-associated ubiquitin-conjugating enzymes RT (E2s)."; RL J. Biol. Chem. 276:16193-16200(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Ovary; 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-205 (ISOFORM 3). RC TISSUE=Brain, Hippocampus, and Placenta; 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 FUNCTION. RX PubMed=36528027; DOI=10.1016/j.molcel.2022.11.021; RA Jiang C., Dai X., He S., Zhou H., Fang L., Guo J., Liu S., Zhang T., RA Pan W., Yu H., Fu T., Li D., Inuzuka H., Wang P., Xiao J., Wei W.; RT "Ring domains are essential for GATOR2-dependent mTORC1 activation."; RL Mol. Cell 83:74-89(2023). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-185. RG Structural genomics consortium (SGC); RT "Structure of the endoplasmic reticulum (ER)-associated human ubiquitin- RT conjugating enzyme E2 J2."; RL Submitted (NOV-2005) to the PDB data bank. RN [8] {ECO:0007744|PDB:2F4W} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-185, AND AUTOUBIQUITINATION. RX PubMed=22496338; DOI=10.1074/mcp.o111.013706; RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V., RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H., RA Raught B., Dhe-Paganon S.; RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure- RT function screen."; RL Mol. Cell. Proteomics 11:329-341(2012). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Seems to function in the selective degradation of misfolded CC membrane proteins from the endoplasmic reticulum (ERAD) (By CC similarity). In cooperation with the GATOR2 complex, catalyzes 'Lys-6'- CC linked ubiquitination of NPRL2 (PubMed:36528027). CC {ECO:0000250|UniProtKB:Q6P073, ECO:0000269|PubMed:36528027}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- INTERACTION: CC Q8N2K1; Q13520: AQP6; NbExp=3; IntAct=EBI-2340110, EBI-13059134; CC Q8N2K1; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-2340110, EBI-10285373; CC Q8N2K1; P62879: GNB2; NbExp=3; IntAct=EBI-2340110, EBI-356942; CC Q8N2K1; P09455: RBP1; NbExp=3; IntAct=EBI-2340110, EBI-2623483; CC Q8N2K1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2340110, EBI-8638294; CC Q8N2K1; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-2340110, EBI-10262539; CC Q8N2K1; O76024: WFS1; NbExp=3; IntAct=EBI-2340110, EBI-720609; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9Y385}; Single-pass type IV membrane protein CC {ECO:0000250|UniProtKB:Q9Y385}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N2K1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N2K1-2; Sequence=VSP_011572; CC Name=3; CC IsoId=Q8N2K1-3; Sequence=VSP_045219; CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:22496338}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SEQUENCE CAUTION: CC Sequence=BM544827; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BM544827; Type=Miscellaneous discrepancy; 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; AF296658; AAK52609.1; -; mRNA. DR EMBL; AK056065; BAB71086.1; -; mRNA. DR EMBL; AK075017; BAC11355.1; -; mRNA. DR EMBL; AK291935; BAF84624.1; -; mRNA. DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471183; EAW56256.1; -; Genomic_DNA. DR EMBL; CH471183; EAW56259.1; -; Genomic_DNA. DR EMBL; BC094777; AAH94777.1; -; mRNA. DR EMBL; BC104890; AAI04891.1; -; mRNA. DR EMBL; BC113430; AAI13431.1; -; mRNA. DR EMBL; BC143657; AAI43658.1; -; mRNA. DR EMBL; BM544827; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS14.1; -. [Q8N2K1-1] DR CCDS; CCDS15.1; -. [Q8N2K1-3] DR RefSeq; NP_477515.2; NM_058167.2. [Q8N2K1-1] DR RefSeq; NP_919296.1; NM_194315.1. [Q8N2K1-3] DR RefSeq; NP_919440.1; NM_194458.1. DR RefSeq; XP_005244775.1; XM_005244718.3. [Q8N2K1-1] DR RefSeq; XP_005244776.1; XM_005244719.4. [Q8N2K1-1] DR RefSeq; XP_006710396.1; XM_006710333.3. [Q8N2K1-1] DR RefSeq; XP_011538915.1; XM_011540613.2. [Q8N2K1-2] DR RefSeq; XP_011538916.1; XM_011540614.2. [Q8N2K1-1] DR PDB; 2F4W; X-ray; 2.00 A; A/B=1-185. DR PDBsum; 2F4W; -. DR AlphaFoldDB; Q8N2K1; -. DR SMR; Q8N2K1; -. DR BioGRID; 125598; 40. DR IntAct; Q8N2K1; 11. DR STRING; 9606.ENSP00000383719; -. DR iPTMnet; Q8N2K1; -. DR PhosphoSitePlus; Q8N2K1; -. DR SwissPalm; Q8N2K1; -. DR BioMuta; UBE2J2; -. DR DMDM; 251757431; -. DR EPD; Q8N2K1; -. DR jPOST; Q8N2K1; -. DR MassIVE; Q8N2K1; -. DR MaxQB; Q8N2K1; -. DR PaxDb; 9606-ENSP00000383719; -. DR PeptideAtlas; Q8N2K1; -. DR ProteomicsDB; 2392; -. DR ProteomicsDB; 71714; -. [Q8N2K1-1] DR ProteomicsDB; 71715; -. [Q8N2K1-2] DR Pumba; Q8N2K1; -. DR Antibodypedia; 26182; 168 antibodies from 25 providers. DR DNASU; 118424; -. DR Ensembl; ENST00000349431.11; ENSP00000305826.7; ENSG00000160087.21. [Q8N2K1-1] DR Ensembl; ENST00000360466.6; ENSP00000353653.2; ENSG00000160087.21. [Q8N2K1-1] DR Ensembl; ENST00000400930.8; ENSP00000383719.4; ENSG00000160087.21. [Q8N2K1-3] DR GeneID; 118424; -. DR KEGG; hsa:118424; -. DR MANE-Select; ENST00000349431.11; ENSP00000305826.7; NM_058167.3; NP_477515.2. DR UCSC; uc001ado.4; human. [Q8N2K1-1] DR AGR; HGNC:19268; -. DR CTD; 118424; -. DR DisGeNET; 118424; -. DR GeneCards; UBE2J2; -. DR HGNC; HGNC:19268; UBE2J2. DR HPA; ENSG00000160087; Low tissue specificity. DR MIM; 619756; gene. DR neXtProt; NX_Q8N2K1; -. DR PharmGKB; PA134882268; -. DR VEuPathDB; HostDB:ENSG00000160087; -. DR eggNOG; KOG0894; Eukaryota. DR GeneTree; ENSGT00940000156173; -. DR HOGENOM; CLU_041481_1_2_1; -. DR InParanoid; Q8N2K1; -. DR OMA; AQSLEYN; -. DR OrthoDB; 180749at2759; -. DR PhylomeDB; Q8N2K1; -. DR TreeFam; TF101123; -. DR BRENDA; 2.3.2.23; 2681. DR PathwayCommons; Q8N2K1; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. [Q8N2K1-1] DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. [Q8N2K1-1] DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q8N2K1; -. DR SIGNOR; Q8N2K1; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 118424; 112 hits in 1164 CRISPR screens. DR ChiTaRS; UBE2J2; human. DR EvolutionaryTrace; Q8N2K1; -. DR GenomeRNAi; 118424; -. DR Pharos; Q8N2K1; Tbio. DR PRO; PR:Q8N2K1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N2K1; Protein. DR Bgee; ENSG00000160087; Expressed in left testis and 183 other cell types or tissues. DR ExpressionAtlas; Q8N2K1; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000151; C:ubiquitin ligase complex; IPI:ParkinsonsUK-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL. DR GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS50127; UBC_2; 1. DR Genevisible; Q8N2K1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Endoplasmic reticulum; KW Membrane; Nucleotide-binding; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Ubl conjugation; KW Ubl conjugation pathway; Unfolded protein response. FT CHAIN 1..259 FT /note="Ubiquitin-conjugating enzyme E2 J2" FT /id="PRO_0000082596" FT TOPO_DOM 1..226 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 227..247 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 248..259 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 12..162 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT ACT_SITE 94 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT VAR_SEQ 1..44 FT /note="MSSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEW -> MWPQ FT DIAGR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011572" FT VAR_SEQ 44 FT /note="W -> WFKRFSWLSLLSSWDYR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045219" FT CONFLICT 2 FT /note="S -> N (in Ref. 2; BAC11355)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="F -> S (in Ref. 2; BAC11355)" FT /evidence="ECO:0000305" FT CONFLICT 214..238 FT /note="PNLAGLQQANRHHGLLGGALANLFV -> QTSQGSSRPTGTTDSGWRPGELV FT C (in Ref. 1; AAK52609)" FT /evidence="ECO:0000305" FT HELIX 13..26 FT /evidence="ECO:0007829|PDB:2F4W" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:2F4W" FT STRAND 40..49 FT /evidence="ECO:0007829|PDB:2F4W" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:2F4W" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:2F4W" FT TURN 69..72 FT /evidence="ECO:0007829|PDB:2F4W" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:2F4W" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:2F4W" FT HELIX 111..123 FT /evidence="ECO:0007829|PDB:2F4W" FT HELIX 136..151 FT /evidence="ECO:0007829|PDB:2F4W" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:2F4W" FT HELIX 161..167 FT /evidence="ECO:0007829|PDB:2F4W" SQ SEQUENCE 259 AA; 28898 MW; 7DB5280D2947CE7E CRC64; MSSTSSKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS FMVEKGPTLG SIETSDFTKR QLAVQSLAFN LKDKVFCELF PEVVEEIKQK QKAQDELSSR PQTLPLPDVV PDGETHLVQN GIQLLNGHAP GAVPNLAGLQ QANRHHGLLG GALANLFVIV GFAAFAYTVK YVLRSIAQE //