UXS1_HUMAN
ID UXS1_HUMAN Reviewed; 420 AA.
AC Q8NBZ7; Q8NBX3; Q9H5C2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE EC=4.1.1.35;
DE AltName: Full=UDP-glucuronate decarboxylase 1;
DE Short=UGD;
DE Short=UXS-1;
GN Name=UXS1; ORFNames=UNQ2538/PRO6079;
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], AND ALTERNATIVE SPLICING.
RX PubMed=12391314; DOI=10.1073/pnas.172522199;
RA Hwang H.-Y., Horvitz H.R.;
RT "The SQV-1 UDP-glucuronic acid decarboxylase and the SQV-7 nucleotide-sugar
RT transporter may act in the Golgi apparatus to affect Caenorhabditis elegans
RT vulval morphogenesis and embryonic development.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14218-14223(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
RN [9]
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., Ayoub D.,
RA 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 85-402 IN COMPLEX WITH NAD AND
RP UDP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human UDP-glucoronic acid decarboxylase.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic
CC acid to UDP-xylose. Necessary for the biosynthesis of the core
CC tetrasaccharide in glycosaminoglycan biosynthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + UDP-alpha-D-glucuronate = CO2 + UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:23916, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58052; EC=4.1.1.35;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
CC biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
CC 1/1.
CC -!- SUBUNIT: Interacts with AKT1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NBZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBZ7-2; Sequence=VSP_016757;
CC Name=3;
CC IsoId=Q8NBZ7-3; Sequence=VSP_016756;
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
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DR EMBL; AY147934; AAN39844.1; -; mRNA.
DR EMBL; AY358541; AAQ88905.1; -; mRNA.
DR EMBL; AK027244; BAB15705.1; -; mRNA.
DR EMBL; AK075120; BAC11415.1; -; mRNA.
DR EMBL; AK075170; BAC11448.1; -; mRNA.
DR EMBL; AC018878; AAY15085.1; -; Genomic_DNA.
DR EMBL; BC009819; AAH09819.2; -; mRNA.
DR CCDS; CCDS46378.1; -. [Q8NBZ7-1]
DR CCDS; CCDS58720.1; -. [Q8NBZ7-3]
DR CCDS; CCDS58721.1; -. [Q8NBZ7-2]
DR RefSeq; NP_001240804.1; NM_001253875.1. [Q8NBZ7-2]
DR RefSeq; NP_001240805.1; NM_001253876.1. [Q8NBZ7-3]
DR RefSeq; NP_079352.2; NM_025076.4. [Q8NBZ7-1]
DR RefSeq; XP_016860503.1; XM_017005014.1. [Q8NBZ7-3]
DR PDB; 2B69; X-ray; 1.21 A; A=85-402.
DR PDB; 4GLL; X-ray; 2.50 A; A/B=85-420.
DR PDB; 4LK3; X-ray; 2.64 A; A/B/C/D/E/F=85-420.
DR PDB; 4M55; X-ray; 2.86 A; A/B/C/D/E/F=85-420.
DR PDBsum; 2B69; -.
DR PDBsum; 4GLL; -.
DR PDBsum; 4LK3; -.
DR PDBsum; 4M55; -.
DR AlphaFoldDB; Q8NBZ7; -.
DR SMR; Q8NBZ7; -.
DR BioGRID; 123139; 105.
DR IntAct; Q8NBZ7; 41.
DR MINT; Q8NBZ7; -.
DR STRING; 9606.ENSP00000283148; -.
DR GlyGen; Q8NBZ7; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NBZ7; -.
DR PhosphoSitePlus; Q8NBZ7; -.
DR BioMuta; UXS1; -.
DR DMDM; 74730150; -.
DR EPD; Q8NBZ7; -.
DR jPOST; Q8NBZ7; -.
DR MassIVE; Q8NBZ7; -.
DR MaxQB; Q8NBZ7; -.
DR PaxDb; Q8NBZ7; -.
DR PeptideAtlas; Q8NBZ7; -.
DR PRIDE; Q8NBZ7; -.
DR ProteomicsDB; 72836; -. [Q8NBZ7-1]
DR ProteomicsDB; 72837; -. [Q8NBZ7-2]
DR ProteomicsDB; 72838; -. [Q8NBZ7-3]
DR Antibodypedia; 1921; 125 antibodies from 19 providers.
DR DNASU; 80146; -.
DR Ensembl; ENST00000283148.12; ENSP00000283148.7; ENSG00000115652.15. [Q8NBZ7-2]
DR Ensembl; ENST00000409032.5; ENSP00000387096.1; ENSG00000115652.15. [Q8NBZ7-3]
DR Ensembl; ENST00000409501.7; ENSP00000387019.3; ENSG00000115652.15. [Q8NBZ7-1]
DR GeneID; 80146; -.
DR KEGG; hsa:80146; -.
DR MANE-Select; ENST00000283148.12; ENSP00000283148.7; NM_001253875.2; NP_001240804.1. [Q8NBZ7-2]
DR UCSC; uc002tdl.4; human. [Q8NBZ7-1]
DR CTD; 80146; -.
DR DisGeNET; 80146; -.
DR GeneCards; UXS1; -.
DR HGNC; HGNC:17729; UXS1.
DR HPA; ENSG00000115652; Low tissue specificity.
DR MIM; 609749; gene.
DR neXtProt; NX_Q8NBZ7; -.
DR OpenTargets; ENSG00000115652; -.
DR PharmGKB; PA38465; -.
DR VEuPathDB; HostDB:ENSG00000115652; -.
DR eggNOG; KOG1429; Eukaryota.
DR GeneTree; ENSGT00940000157868; -.
DR HOGENOM; CLU_007383_4_3_1; -.
DR InParanoid; Q8NBZ7; -.
DR OMA; PKVKYLN; -.
DR OrthoDB; 848823at2759; -.
DR PhylomeDB; Q8NBZ7; -.
DR TreeFam; TF105736; -.
DR PathwayCommons; Q8NBZ7; -.
DR SignaLink; Q8NBZ7; -.
DR UniPathway; UPA00796; UER00771.
DR BioGRID-ORCS; 80146; 174 hits in 1078 CRISPR screens.
DR ChiTaRS; UXS1; human.
DR EvolutionaryTrace; Q8NBZ7; -.
DR GeneWiki; UXS1; -.
DR GenomeRNAi; 80146; -.
DR Pharos; Q8NBZ7; Tbio.
DR PRO; PR:Q8NBZ7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NBZ7; protein.
DR Bgee; ENSG00000115652; Expressed in secondary oocyte and 203 other tissues.
DR ExpressionAtlas; Q8NBZ7; baseline and differential.
DR Genevisible; Q8NBZ7; HS.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044516; UXS.
DR InterPro; IPR021761; UXS1_N.
DR PANTHER; PTHR43078; PTHR43078; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR Pfam; PF11803; UXS1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Decarboxylase;
KW Glycoprotein; Golgi apparatus; Lyase; Membrane; NAD; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..420
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000183269"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 119..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 228
FT /ligand="substrate"
FT BINDING 231..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 260
FT /ligand="substrate"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 273..277
FT /ligand="substrate"
FT BINDING 290..297
FT /ligand="substrate"
FT BINDING 357..361
FT /ligand="substrate"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25732826"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..168
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016756"
FT VAR_SEQ 40
FT /note="M -> MSFLLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016757"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2B69"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4LK3"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 172..193
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:2B69"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:2B69"
FT HELIX 380..398
FT /evidence="ECO:0007829|PDB:2B69"
SQ SEQUENCE 420 AA; 47577 MW; FD7DC0E1B1D02157 CRC64;
MVSKALLRLV SAVNRRRMKL LLGIALLAYV ASVWGNFVNM RSIQENGELK IESKIEEMVE
PLREKIRDLE KSFTQKYPPV KFLSEKDRKR ILITGGAGFV GSHLTDKLMM DGHEVTVVDN
FFTGRKRNVE HWIGHENFEL INHDVVEPLY IEVDQIYHLA SPASPPNYMY NPIKTLKTNT
IGTLNMLGLA KRVGARLLLA STSEVYGDPE VHPQSEDYWG HVNPIGPRAC YDEGKRVAET
MCYAYMKQEG VEVRVARIFN TFGPRMHMND GRVVSNFILQ ALQGEPLTVY GSGSQTRAFQ
YVSDLVNGLV ALMNSNVSSP VNLGNPEEHT ILEFAQLIKN LVGSGSEIQF LSEAQDDPQK
RKPDIKKAKL MLGWEPVVPL EEGLNKAIHY FRKELEYQAN NQYIPKPKPA RIKKGRTRHS
