ID UEVLD_HUMAN Reviewed; 471 AA. AC Q8IX04; B2RB69; B4DL43; F5H6L6; H7BYD6; Q6P2F0; Q96FF5; Q9NUX7; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 02-SEP-2026, entry version 181. DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 3; DE Short=UEV-3; DE AltName: Full=EV and lactate/malate dehydrogenase domain-containing protein; GN Name=UEVLD {ECO:0000312|EMBL:AAH64566.1}; GN Synonyms=UEV3 {ECO:0000312|EMBL:AAN32950.1}; 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] {ECO:0000305, ECO:0000312|EMBL:AAN32950.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Placenta {ECO:0000312|EMBL:AAN32950.1}; RX PubMed=12427560; DOI=10.1016/s0167-4781(02)00543-2; RA Kloor M., Bork P., Duwe A., Klaes R., von Knebel Doeberitz M., Ridder R.; RT "Identification and characterization of UEV3, a human cDNA with RT similarities to inactive E2 ubiquitin-conjugating enzymes."; RL Biochim. Biophys. Acta 1579:219-224(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 6). RC TISSUE=Placenta {ECO:0000312|EMBL:BAA91985.1}, Testis, and Tongue; 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 [4] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000312|EMBL:AAH64566.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 7). RC TISSUE=Brain, Placenta, and Testis {ECO:0000312|EMBL:AAH64566.1}; 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 [7] 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RA Avvakumov G.V., Walker J.R., Xue S., Newman E.M., Finerty P.J. Jr., RA Butler-Cole C., Tempel W., Weigelt J., Sundstrom M., Arrowsmith C.H., RA Edwards A.M., Bochkarev A., Dhe-Paganon S.; RT "Structural investigation into the L-lactate dehydrogenase domain of human RT ubiquitin-conjugating enzyme E2-like isoform A."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Possible negative regulator of polyubiquitination. CC {ECO:0000269|PubMed:12427560}. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC Q8IX04; Q8NDC4: MORN4; NbExp=2; IntAct=EBI-2339926, EBI-10269566; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1 {ECO:0000269|PubMed:14702039}; CC IsoId=Q8IX04-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:12427560}; CC IsoId=Q8IX04-2; Sequence=VSP_023350, VSP_023351; CC Name=3 {ECO:0000269|PubMed:15489334}; CC IsoId=Q8IX04-3; Sequence=VSP_023347, VSP_023350, VSP_023351; CC Name=4; CC IsoId=Q8IX04-4; Sequence=VSP_023346, VSP_023350, VSP_023351; CC Name=5; CC IsoId=Q8IX04-5; Sequence=VSP_023348, VSP_023349; CC Name=6; CC IsoId=Q8IX04-6; Sequence=VSP_023347; CC Name=7; CC IsoId=Q8IX04-7; Sequence=VSP_045986, VSP_045987, VSP_045988; CC -!- TISSUE SPECIFICITY: Colon, colon carcinoma cell lines, normal cervical CC epithelium, carcinomas of the uterine cervix and peripheral blood CC leukocytes. {ECO:0000269|PubMed:12427560}. CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin- CC conjugating enzyme family. UEV subfamily. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the LDH/MDH CC superfamily. {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; AF503350; AAN32950.1; -; mRNA. DR EMBL; CR616778; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK001930; BAA91985.1; -; mRNA. DR EMBL; AK296835; BAG59405.1; -; mRNA. DR EMBL; AK314521; BAG37116.1; -; mRNA. DR EMBL; AC027544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112694; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68380.1; -; Genomic_DNA. DR EMBL; BC011011; AAH11011.2; -; mRNA. DR EMBL; BC064566; AAH64566.1; -; mRNA. DR EMBL; CD109744; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS41624.1; -. [Q8IX04-1] DR CCDS; CCDS58122.1; -. [Q8IX04-4] DR CCDS; CCDS58123.1; -. [Q8IX04-3] DR CCDS; CCDS58124.1; -. [Q8IX04-6] DR CCDS; CCDS58125.1; -. [Q8IX04-7] DR CCDS; CCDS73266.1; -. [Q8IX04-5] DR CCDS; CCDS7843.1; -. [Q8IX04-2] DR RefSeq; NP_001035787.1; NM_001040697.4. [Q8IX04-1] DR RefSeq; NP_001248311.1; NM_001261382.3. [Q8IX04-6] DR RefSeq; NP_001248312.1; NM_001261383.3. [Q8IX04-3] DR RefSeq; NP_001248314.1; NM_001261385.3. [Q8IX04-4] DR RefSeq; NP_001248315.1; NM_001261386.3. [Q8IX04-7] DR RefSeq; NP_001284700.1; NM_001297771.3. [Q8IX04-5] DR RefSeq; NP_060784.3; NM_018314.6. [Q8IX04-2] DR PDB; 2I6T; X-ray; 2.10 A; A/B=171-471. DR PDB; 3DL2; X-ray; 2.10 A; A/B=171-471. DR AlphaFoldDB; Q8IX04; -. DR SMR; Q8IX04; -. DR BioGRID; 120580; 31. DR FunCoup; Q8IX04; 407. DR IntAct; Q8IX04; 21. DR MINT; Q8IX04; -. DR STRING; 9606.ENSP00000379500; -. DR iPTMnet; Q8IX04; -. DR PhosphoSitePlus; Q8IX04; -. DR BioMuta; UEVLD; -. DR DMDM; 126253820; -. DR jPOST; Q8IX04; -. DR MassIVE; Q8IX04; -. DR PaxDb; 9606-ENSP00000379500; -. DR PeptideAtlas; Q8IX04; -. DR ProteomicsDB; 27225; -. DR ProteomicsDB; 43582; -. DR ProteomicsDB; 70952; -. [Q8IX04-1] DR ProteomicsDB; 70953; -. [Q8IX04-2] DR ProteomicsDB; 70954; -. [Q8IX04-3] DR ProteomicsDB; 70955; -. [Q8IX04-4] DR ProteomicsDB; 70956; -. [Q8IX04-5] DR Pumba; Q8IX04; -. DR Antibodypedia; 25122; 149 antibodies from 22 providers. DR DNASU; 55293; -. DR Ensembl; ENST00000300038.7; ENSP00000300038.7; ENSG00000151116.18. [Q8IX04-5] DR Ensembl; ENST00000320750.10; ENSP00000323353.6; ENSG00000151116.18. [Q8IX04-3] DR Ensembl; ENST00000379387.8; ENSP00000368697.4; ENSG00000151116.18. [Q8IX04-6] DR Ensembl; ENST00000396197.8; ENSP00000379500.2; ENSG00000151116.18. [Q8IX04-1] DR Ensembl; ENST00000535484.5; ENSP00000441092.1; ENSG00000151116.18. [Q8IX04-4] DR Ensembl; ENST00000541984.5; ENSP00000437538.1; ENSG00000151116.18. [Q8IX04-7] DR Ensembl; ENST00000543987.5; ENSP00000442974.1; ENSG00000151116.18. [Q8IX04-2] DR GeneID; 55293; -. DR KEGG; hsa:55293; -. DR MANE-Select; ENST00000396197.8; ENSP00000379500.2; NM_001040697.4; NP_001035787.1. DR UCSC; uc001mot.5; human. [Q8IX04-1] DR AGR; HGNC:30866; -. DR ClinPGx; PA147357188; -. DR CTD; 55293; -. DR GeneCards; UEVLD; -. DR HGNC; HGNC:30866; UEVLD. DR HPA; ENSG00000151116; Low tissue specificity. DR MIM; 610985; gene. DR OpenTargets; ENSG00000151116; -. DR VEuPathDB; HostDB:ENSG00000151116; -. DR eggNOG; KOG1495; Eukaryota. DR eggNOG; KOG2391; Eukaryota. DR GeneTree; ENSGT00940000153903; -. DR HOGENOM; CLU_039842_0_1_1; -. DR InParanoid; Q8IX04; -. DR OMA; CIMGANG; -. DR OrthoDB; 5405561at2759; -. DR PAN-GO; Q8IX04; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q8IX04; -. DR PathwayCommons; Q8IX04; -. DR SignaLink; Q8IX04; -. DR Agora; ENSG00000151116; -. DR BioGRID-ORCS; 55293; 10 hits in 1164 CRISPR screens. DR ChiTaRS; UEVLD; human. DR EvolutionaryTrace; Q8IX04; -. DR GenomeRNAi; 55293; -. DR Pharos; Q8IX04; Tdark. DR PRO; PR:Q8IX04; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q8IX04; protein. DR Bgee; ENSG00000151116; Expressed in mucosa of sigmoid colon and 192 other cell types or tissues. DR ExpressionAtlas; Q8IX04; baseline and differential. DR GO; GO:0000813; C:ESCRT I complex; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-ARBA. DR CDD; cd05293; LDH_1; 1. DR CDD; cd11685; UEV_TSG101-like; 1. DR FunFam; 3.10.110.10:FF:000040; tumor susceptibility gene 101 protein; 1. DR FunFam; 3.90.110.10:FF:000007; ubiquitin-conjugating enzyme E2 variant 3 isoform X1; 1. DR FunFam; 3.40.50.720:FF:000270; ubiquitin-conjugating enzyme E2 variant 3 isoform X2; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR InterPro; IPR008883; UEV_N. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF33; UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 3; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR Pfam; PF05743; UEV; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS51322; UEV; 1. DR PDBsum; 2I6T; -. DR PDBsum; 3DL2; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; NAD; Proteomics identification; KW Reference proteome; Ubl conjugation pathway. FT CHAIN 1..471 FT /note="Ubiquitin-conjugating enzyme E2 variant 3" FT /id="PRO_0000278651" FT DOMAIN 2..145 FT /note="UEV" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652" FT BINDING 191..219 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT VAR_SEQ 1..38 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023346" FT VAR_SEQ 43..64 FT /note="Missing (in isoform 3 and isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_023347" FT VAR_SEQ 65..164 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045986" FT VAR_SEQ 205..215 FT /note="GIADRLVLLDL -> VESRSVTQAGV (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023348" FT VAR_SEQ 216..471 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023349" FT VAR_SEQ 239..295 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045987" FT VAR_SEQ 354..470 FT /note="VLTWSGQEEVVSHTSQVQLSNRAMELLRVKGQRSWSVGLSVADMVDSIVNNK FT KKVHSVSALAKGYYDINSEVFLSLPCILGTNGVSEVIKTTLKEDTVTEKLQSSASSIHS FT LQQQLK -> GI (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045988" FT VAR_SEQ 376..379 FT /note="AMEL -> DIMI (in isoform 2, isoform 3 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:12427560, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_023350" FT VAR_SEQ 380..471 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12427560, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_023351" FT CONFLICT 148 FT /note="D -> G (in Ref. 3; BAG59405)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="V -> A (in Ref. 3; BAG59405)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="H -> L (in Ref. 1; AAN32950 and 3; BAA91985)" FT /evidence="ECO:0000305" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 192..204 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:3DL2" FT HELIX 223..229 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 247..251 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 262..283 FT /evidence="ECO:0007829|PDB:2I6T" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 296..307 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 320..328 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 329..333 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 343..348 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 366..377 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 380..382 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 387..402 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 407..414 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 426..434 FT /evidence="ECO:0007829|PDB:2I6T" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:2I6T" FT HELIX 450..468 FT /evidence="ECO:0007829|PDB:2I6T" SQ SEQUENCE 471 AA; 52264 MW; 2502659A566E7DDD CRC64; MEFDCEGLRR LLGKYKFRDL TVEELRNVNV FFPHFKYSMD TYVFKDSSQK DLLNFTGTIP VMYQGNTYNI PIRFWILDSH PFAPPICFLK PTANMGILVG KHVDAQGRIY LPYLQNWSHP KSVIVGLIKE MIAKFQEELP MYSLSSSDEA RQVDLLAYIA KITEGVSDTN SKSWANHENK TVNKITVVGG GELGIACTLA ISAKGIADRL VLLDLSEGTK GATMDLEIFN LPNVEISKDL SASAHSKVVI FTVNSLGSSQ SYLDVVQSNV DMFRALVPAL GHYSQHSVLL VASQPVEIMT YVTWKLSTFP ANRVIGIGCN LDSQRLQYII TNVLKAQTSG KEVWVIGEQG EDKVLTWSGQ EEVVSHTSQV QLSNRAMELL RVKGQRSWSV GLSVADMVDS IVNNKKKVHS VSALAKGYYD INSEVFLSLP CILGTNGVSE VIKTTLKEDT VTEKLQSSAS SIHSLQQQLK L //