UEVLD_HUMAN
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 03-AUG-2022, entry version 163.
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 -!- 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}.
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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_001040697.2. [Q8IX04-1]
DR RefSeq; NP_001248311.1; NM_001261382.1. [Q8IX04-6]
DR RefSeq; NP_001248312.1; NM_001261383.1. [Q8IX04-3]
DR RefSeq; NP_001248314.1; NM_001261385.1. [Q8IX04-4]
DR RefSeq; NP_001248315.1; NM_001261386.1. [Q8IX04-7]
DR RefSeq; NP_001284700.1; NM_001297771.1. [Q8IX04-5]
DR RefSeq; NP_060784.3; NM_018314.4. [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 PDBsum; 2I6T; -.
DR PDBsum; 3DL2; -.
DR AlphaFoldDB; Q8IX04; -.
DR SMR; Q8IX04; -.
DR BioGRID; 120580; 19.
DR IntAct; Q8IX04; 17.
DR MINT; Q8IX04; -.
DR STRING; 9606.ENSP00000379500; -.
DR iPTMnet; Q8IX04; -.
DR PhosphoSitePlus; Q8IX04; -.
DR BioMuta; UEVLD; -.
DR DMDM; 126253820; -.
DR EPD; Q8IX04; -.
DR jPOST; Q8IX04; -.
DR MassIVE; Q8IX04; -.
DR MaxQB; Q8IX04; -.
DR PaxDb; Q8IX04; -.
DR PeptideAtlas; Q8IX04; -.
DR PRIDE; 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 Antibodypedia; 25122; 148 antibodies from 21 providers.
DR DNASU; 55293; -.
DR Ensembl; ENST00000300038.7; ENSP00000300038.7; ENSG00000151116.17. [Q8IX04-5]
DR Ensembl; ENST00000320750.10; ENSP00000323353.6; ENSG00000151116.17. [Q8IX04-3]
DR Ensembl; ENST00000379387.8; ENSP00000368697.4; ENSG00000151116.17. [Q8IX04-6]
DR Ensembl; ENST00000396197.8; ENSP00000379500.2; ENSG00000151116.17. [Q8IX04-1]
DR Ensembl; ENST00000535484.5; ENSP00000441092.1; ENSG00000151116.17. [Q8IX04-4]
DR Ensembl; ENST00000541984.5; ENSP00000437538.1; ENSG00000151116.17. [Q8IX04-7]
DR Ensembl; ENST00000543987.5; ENSP00000442974.1; ENSG00000151116.17. [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 CTD; 55293; -.
DR DisGeNET; 55293; -.
DR GeneCards; UEVLD; -.
DR HGNC; HGNC:30866; UEVLD.
DR HPA; ENSG00000151116; Low tissue specificity.
DR MIM; 610985; gene.
DR neXtProt; NX_Q8IX04; -.
DR OpenTargets; ENSG00000151116; -.
DR PharmGKB; PA147357188; -.
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; GIAVGKH; -.
DR OrthoDB; 1435538at2759; -.
DR PhylomeDB; Q8IX04; -.
DR TreeFam; TF314963; -.
DR PathwayCommons; Q8IX04; -.
DR SignaLink; Q8IX04; -.
DR BioGRID-ORCS; 55293; 9 hits in 1081 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 190 other tissues.
DR ExpressionAtlas; Q8IX04; baseline and differential.
DR Genevisible; Q8IX04; HS.
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:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.90.110.10; -; 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 Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR Pfam; PF05743; UEV; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS51322; UEV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; NAD; Reference proteome;
KW 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..332
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
