UBP46_HUMAN
ID UBP46_HUMAN Reviewed; 366 AA.
AC P62068; B7Z3Y7; B7Z675; B7Z7S3; G8ACC7; Q80V95; Q9H7U4; Q9H9T8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 46;
DE EC=3.4.19.12 {ECO:0000269|PubMed:14715245, ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:26388029};
DE AltName: Full=Deubiquitinating enzyme 46;
DE AltName: Full=Ubiquitin thioesterase 46;
DE AltName: Full=Ubiquitin-specific-processing protease 46;
GN Name=USP46;
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), CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND MUTAGENESIS OF CYS-44.
RX PubMed=22043315; DOI=10.1371/journal.pone.0026297;
RA Zhang W., Tian Q.B., Li Q.K., Wang J.M., Wang C.N., Liu T., Liu D.W.,
RA Wang M.W.;
RT "Lysine 92 amino acid residue of USP46, a gene associated with 'behavioral
RT despair' in mice, influences the deubiquitinating enzyme activity.";
RL PLoS ONE 6:E26297-E26297(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Brain, Placenta, Teratocarcinoma, Testis, and Thalamus;
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].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND ENZYME ACTIVITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, AND
RP INTERACTION WITH WDR48.
RX PubMed=19075014; DOI=10.1074/jbc.m808430200;
RA Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.;
RT "UAF1 is a subunit of multiple deubiquitinating enzyme complexes.";
RL J. Biol. Chem. 284:5343-5351(2009).
RN [7]
RP INTERACTION WITH WRD20.
RX PubMed=20147737; DOI=10.1074/jbc.m109.095141;
RA Kee Y., Yang K., Cohn M.A., Haas W., Gygi S.P., D'Andrea A.D.;
RT "WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme
RT complex.";
RL J. Biol. Chem. 285:11252-11257(2010).
RN [8] {ECO:0007744|PDB:5CVM, ECO:0007744|PDB:5CVN, ECO:0007744|PDB:5CVO}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-366 IN COMPLEXES WITH WDR48
RP AND UBIQUITIN, ZINC-BINDING, INTERACTION WITH WDR48, FUNCTION, ACTIVITY
RP REGULATION, ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-44.
RX PubMed=26388029; DOI=10.1016/j.str.2015.08.010;
RA Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A.,
RA Dueber E.C., Harris S.F.;
RT "Structural insights into WD-repeat 48 activation of ubiquitin-specific
RT protease 46.";
RL Structure 23:2043-2054(2015).
RN [9] {ECO:0007744|PDB:5L8H}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 8-366 IN COMPLEX WITH UBIQUITIN,
RP AND ZINC-BINDING.
RX PubMed=27650958; DOI=10.1016/j.jsb.2016.09.011;
RA Dharadhar S., Clerici M., van Dijk W.J., Fish A., Sixma T.K.;
RT "A conserved two-step binding for the UAF1 regulator to the USP12
RT deubiquitinating enzyme.";
RL J. Struct. Biol. 196:437-447(2016).
CC -!- FUNCTION: Deubiquitinating enzyme that plays a role in behavior,
CC possibly by regulating GABA action. May act by mediating the
CC deubiquitination of GAD1/GAD67 (By similarity). Has almost no
CC deubiquitinating activity by itself and requires the interaction with
CC WDR48 to have a high activity (PubMed:19075014, PubMed:26388029). Not
CC involved in deubiquitination of monoubiquitinated FANCD2
CC (PubMed:19075014). {ECO:0000250|UniProtKB:P62069,
CC ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:26388029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:14715245,
CC ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:26388029};
CC -!- ACTIVITY REGULATION: Activated by interaction with WDR48.
CC {ECO:0000269|PubMed:26388029}.
CC -!- SUBUNIT: Interacts with WDR48 (PubMed:19075014, PubMed:26388029).
CC Interacts with WDR20 (PubMed:20147737). {ECO:0000269|PubMed:19075014,
CC ECO:0000269|PubMed:20147737, ECO:0000269|PubMed:26388029}.
CC -!- INTERACTION:
CC P62068; P54253: ATXN1; NbExp=6; IntAct=EBI-2512753, EBI-930964;
CC P62068; Q8TBZ3: WDR20; NbExp=6; IntAct=EBI-2512753, EBI-2511486;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P62068-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62068-2; Sequence=VSP_037618, VSP_037621;
CC Name=3;
CC IsoId=P62068-3; Sequence=VSP_037619;
CC Name=4;
CC IsoId=P62068-4; Sequence=VSP_037620;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC {ECO:0000305}.
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DR EMBL; GU455414; ADV57651.1; -; mRNA.
DR EMBL; AK022614; BAB14133.1; -; mRNA.
DR EMBL; AK024318; BAB14881.1; -; mRNA.
DR EMBL; AK296493; BAH12373.1; -; mRNA.
DR EMBL; AK299883; BAH13161.1; -; mRNA.
DR EMBL; AK302438; BAH13709.1; -; mRNA.
DR EMBL; CH471057; EAX05435.1; -; Genomic_DNA.
DR EMBL; BC037574; AAH37574.1; -; mRNA.
DR CCDS; CCDS47053.1; -. [P62068-1]
DR CCDS; CCDS47054.1; -. [P62068-3]
DR RefSeq; NP_001127695.1; NM_001134223.1. [P62068-3]
DR RefSeq; NP_001273696.1; NM_001286767.1. [P62068-4]
DR RefSeq; NP_001273697.1; NM_001286768.1. [P62068-2]
DR RefSeq; NP_073743.2; NM_022832.3. [P62068-1]
DR PDB; 5CVM; X-ray; 1.90 A; A=25-366.
DR PDB; 5CVN; X-ray; 3.36 A; B=25-366.
DR PDB; 5CVO; X-ray; 3.88 A; B/E=25-366.
DR PDB; 5L8H; X-ray; 1.85 A; A=8-366.
DR PDB; 6JLQ; X-ray; 3.10 A; A=23-366.
DR PDBsum; 5CVM; -.
DR PDBsum; 5CVN; -.
DR PDBsum; 5CVO; -.
DR PDBsum; 5L8H; -.
DR PDBsum; 6JLQ; -.
DR AlphaFoldDB; P62068; -.
DR SMR; P62068; -.
DR BioGRID; 122327; 56.
DR CORUM; P62068; -.
DR DIP; DIP-53590N; -.
DR IntAct; P62068; 34.
DR MINT; P62068; -.
DR STRING; 9606.ENSP00000407818; -.
DR MEROPS; C19.052; -.
DR iPTMnet; P62068; -.
DR PhosphoSitePlus; P62068; -.
DR BioMuta; USP46; -.
DR DMDM; 49065850; -.
DR EPD; P62068; -.
DR jPOST; P62068; -.
DR MassIVE; P62068; -.
DR MaxQB; P62068; -.
DR PaxDb; P62068; -.
DR PeptideAtlas; P62068; -.
DR PRIDE; P62068; -.
DR ProteomicsDB; 57356; -. [P62068-1]
DR ProteomicsDB; 57357; -. [P62068-2]
DR ProteomicsDB; 57358; -. [P62068-3]
DR ProteomicsDB; 57359; -. [P62068-4]
DR Antibodypedia; 1722; 133 antibodies from 26 providers.
DR DNASU; 64854; -.
DR Ensembl; ENST00000441222.8; ENSP00000407818.2; ENSG00000109189.13. [P62068-1]
DR Ensembl; ENST00000508499.5; ENSP00000423244.1; ENSG00000109189.13. [P62068-3]
DR GeneID; 64854; -.
DR KEGG; hsa:64854; -.
DR MANE-Select; ENST00000441222.8; ENSP00000407818.2; NM_022832.4; NP_073743.2.
DR UCSC; uc003gzm.5; human. [P62068-1]
DR CTD; 64854; -.
DR DisGeNET; 64854; -.
DR GeneCards; USP46; -.
DR HGNC; HGNC:20075; USP46.
DR HPA; ENSG00000109189; Low tissue specificity.
DR MIM; 612849; gene.
DR neXtProt; NX_P62068; -.
DR OpenTargets; ENSG00000109189; -.
DR PharmGKB; PA134922048; -.
DR VEuPathDB; HostDB:ENSG00000109189; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000153284; -.
DR InParanoid; P62068; -.
DR OMA; NKYFCDV; -.
DR OrthoDB; 378361at2759; -.
DR PhylomeDB; P62068; -.
DR TreeFam; TF314144; -.
DR PathwayCommons; P62068; -.
DR SignaLink; P62068; -.
DR BioGRID-ORCS; 64854; 27 hits in 1124 CRISPR screens.
DR ChiTaRS; USP46; human.
DR GenomeRNAi; 64854; -.
DR Pharos; P62068; Tbio.
DR PRO; PR:P62068; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P62068; protein.
DR Bgee; ENSG00000109189; Expressed in choroid plexus epithelium and 204 other tissues.
DR ExpressionAtlas; P62068; baseline and differential.
DR Genevisible; P62068; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008343; P:adult feeding behavior; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Behavior; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..366
FT /note="Ubiquitin carboxyl-terminal hydrolase 46"
FT /id="PRO_0000080674"
FT DOMAIN 35..365
FT /note="USP"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093,
FT ECO:0000269|PubMed:26388029, ECO:0000305|PubMed:22043315"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5CVM, ECO:0007744|PDB:5CVN,
FT ECO:0007744|PDB:5CVO, ECO:0007744|PDB:5L8H"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5CVM, ECO:0007744|PDB:5CVN,
FT ECO:0007744|PDB:5CVO, ECO:0007744|PDB:5L8H"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5CVM, ECO:0007744|PDB:5CVN,
FT ECO:0007744|PDB:5CVO, ECO:0007744|PDB:5L8H"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5CVM, ECO:0007744|PDB:5CVN,
FT ECO:0007744|PDB:5CVO, ECO:0007744|PDB:5L8H"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037618"
FT VAR_SEQ 1..12
FT /note="MTVRNIASICNM -> MNCFQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037619"
FT VAR_SEQ 40..51
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037620"
FT VAR_SEQ 334..366
FT /note="KIDAQAIEEFYGLTSDISKNSESGYILFYQSRE -> VGLQIILQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037621"
FT VARIANT 81
FT /note="A -> V (in dbSNP:rs17475800)"
FT /id="VAR_051540"
FT MUTAGEN 44
FT /note="C->S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22043315,
FT ECO:0000269|PubMed:26388029"
FT CONFLICT 177
FT /note="T -> A (in Ref. 2; BAH13161)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> V (in Ref. 2; BAB14133)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="H -> R (in Ref. 2; BAB14133)"
FT /evidence="ECO:0000305"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5L8H"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5L8H"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5L8H"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6JLQ"
FT STRAND 293..311
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5L8H"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:5L8H"
FT STRAND 354..364
FT /evidence="ECO:0007829|PDB:5L8H"
SQ SEQUENCE 366 AA; 42442 MW; 67BB113FC4081C46 CRC64;
MTVRNIASIC NMGTNASALE KDIGPEQFPI NEHYFGLVNF GNTCYCNSVL QALYFCRPFR
ENVLAYKAQQ KKKENLLTCL ADLFHSIATQ KKKVGVIPPK KFISRLRKEN DLFDNYMQQD
AHEFLNYLLN TIADILQEEK KQEKQNGKLK NGNMNEPAEN NKPELTWVHE IFQGTLTNET
RCLNCETVSS KDEDFLDLSV DVEQNTSITH CLRDFSNTET LCSEQKYYCE TCCSKQEAQK
RMRVKKLPMI LALHLKRFKY MEQLHRYTKL SYRVVFPLEL RLFNTSSDAV NLDRMYDLVA
VVVHCGSGPN RGHYITIVKS HGFWLLFDDD IVEKIDAQAI EEFYGLTSDI SKNSESGYIL
FYQSRE
