ID   UBP33_MOUSE             Reviewed;         909 AA.
AC   Q8R5K2; Q3UP32; Q5FWK0; Q8K0I3; Q99K22;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 33;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 33;
DE   AltName: Full=Ubiquitin thioesterase 33;
DE   AltName: Full=Ubiquitin-specific-processing protease 33;
DE   AltName: Full=VHL-interacting deubiquitinating enzyme 1;
GN   Name=Usp33; Synonyms=Vdu1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11739384; DOI=10.1074/jbc.m108269200;
RA   Li Z., Na X., Wang D., Schoen S.R., Messing E.M., Wu G.;
RT   "Ubiquitination of a novel deubiquitinating enzyme requires direct binding
RT   to von Hippel-Lindau tumor suppressor protein.";
RL   J. Biol. Chem. 277:4656-4662(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 225-909 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-880 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, INTERACTION WITH ROBO1, AND TISSUE SPECIFICITY.
RX   PubMed=19684588; DOI=10.1038/nn.2382;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.;
RT   "Midline crossing and Slit responsiveness of commissural axons require
RT   USP33.";
RL   Nat. Neurosci. 12:1087-1089(2009).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH ROBO1.
RX   PubMed=19706539; DOI=10.1073/pnas.0801262106;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.;
RT   "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in
RT   inhibiting breast cancer cell migration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Deubiquitinating enzyme involved in various processes such as
CC       centrosome duplication, cellular migration and beta-2 adrenergic
CC       receptor/ADRB2 recycling. Involved in regulation of centrosome
CC       duplication by mediating deubiquitination of CCP110 in S and G2/M
CC       phase, leading to stabilize CCP110 during the period which centrioles
CC       duplicate and elongate. Involved in cell migration via its interaction
CC       with intracellular domain of ROBO1, leading to regulate the Slit
CC       signaling. Plays a role in commissural axon guidance cross the ventral
CC       midline of the neural tube in a Slit-dependent manner, possibly by
CC       mediating the deubiquitination of ROBO1. Acts as a regulator of G-
CC       protein coupled receptor (GPCR) signaling by mediating the
CC       deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2
CC       adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling
CC       and resensitization after prolonged agonist stimulation by
CC       constitutively binding ADRB2, mediating deubiquitination of ADRB2 and
CC       inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is
CC       probably transferred to the translocated beta-arrestins, leading to
CC       beta-arrestins deubiquitination and disengagement from ADRB2. This
CC       suggests the existence of a dynamic exchange between the ADRB2 and
CC       beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid
CC       hormone regulation. Mediates deubiquitination of both 'Lys-48'- and
CC       'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:19684588,
CC       ECO:0000269|PubMed:19706539}.
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;
CC   -!- SUBUNIT: Interacts with VHL, leading to its ubiquitination and
CC       subsequent degradation (By similarity). Interacts with ARRB1 and ARRB2
CC       (By similarity). Interacts with ADRB2 (By similarity). Interacts with
CC       DIO2 (By similarity). Interacts with SELENBP1; in a selenium-dependent
CC       manner (By similarity). Interacts with CCP110 (By similarity).
CC       Interacts with ROBO1 (PubMed:19684588, PubMed:19706539).
CC       {ECO:0000250|UniProtKB:Q8TEY7, ECO:0000269|PubMed:19684588,
CC       ECO:0000269|PubMed:19706539}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}.
CC       Note=Associates with centrosomes predominantly in S and G2 phases but
CC       less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R5K2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5K2-2; Sequence=VSP_038531;
CC   -!- TISSUE SPECIFICITY: Present in 9.5 and 11.5 dpc commissural neurons (at
CC       protein level). {ECO:0000269|PubMed:19684588}.
CC   -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does
CC       not bind ubiquitin, probably because the conserved Arg in position 55
CC       is replaced by a Glu residue (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
CC       degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH89315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF383174; AAL78316.1; -; mRNA.
DR   EMBL; BC005506; AAH05506.1; ALT_INIT; mRNA.
DR   EMBL; BC031366; AAH31366.1; -; mRNA.
DR   EMBL; BC089315; AAH89315.1; ALT_INIT; mRNA.
DR   EMBL; AK143844; BAE25565.1; -; mRNA.
DR   CCDS; CCDS17918.1; -. [Q8R5K2-1]
DR   CCDS; CCDS57261.1; -. [Q8R5K2-2]
DR   RefSeq; NP_001239415.1; NM_001252486.1. [Q8R5K2-2]
DR   RefSeq; NP_573510.2; NM_133247.3. [Q8R5K2-1]
DR   AlphaFoldDB; Q8R5K2; -.
DR   BioGRID; 228458; 3.
DR   IntAct; Q8R5K2; 1.
DR   STRING; 10090.ENSMUSP00000142708; -.
DR   MEROPS; C19.037; -.
DR   iPTMnet; Q8R5K2; -.
DR   PhosphoSitePlus; Q8R5K2; -.
DR   EPD; Q8R5K2; -.
DR   MaxQB; Q8R5K2; -.
DR   PaxDb; 10090-ENSMUSP00000113265; -.
DR   ProteomicsDB; 298415; -. [Q8R5K2-1]
DR   ProteomicsDB; 298416; -. [Q8R5K2-2]
DR   Pumba; Q8R5K2; -.
DR   Antibodypedia; 33489; 314 antibodies from 32 providers.
DR   DNASU; 170822; -.
DR   Ensembl; ENSMUST00000117492.9; ENSMUSP00000113265.4; ENSMUSG00000025437.16. [Q8R5K2-2]
DR   Ensembl; ENSMUST00000197748.5; ENSMUSP00000142708.2; ENSMUSG00000025437.16. [Q8R5K2-1]
DR   GeneID; 170822; -.
DR   KEGG; mmu:170822; -.
DR   UCSC; uc008rti.2; mouse. [Q8R5K2-1]
DR   UCSC; uc008rtj.2; mouse. [Q8R5K2-2]
DR   AGR; MGI:2159711; -.
DR   CTD; 23032; -.
DR   MGI; MGI:2159711; Usp33.
DR   VEuPathDB; HostDB:ENSMUSG00000025437; -.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000157311; -.
DR   InParanoid; Q8R5K2; -.
DR   OMA; LCSVICH; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q8R5K2; -.
DR   TreeFam; TF352179; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-9010553; Regulation of expression of SLITs and ROBOs.
DR   BioGRID-ORCS; 170822; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Usp33; mouse.
DR   PRO; PR:Q8R5K2; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8R5K2; Protein.
DR   Bgee; ENSMUSG00000025437; Expressed in retinal neural layer and 265 other cell types or tissues.
DR   ExpressionAtlas; Q8R5K2; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR   GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF32; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33; 1.
DR   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51283; DUSP; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
DR   Genevisible; Q8R5K2; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase;
KW   Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat;
KW   Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..909
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 33"
FT                   /id="PRO_0000390424"
FT   DOMAIN          154..682
FT                   /note="USP"
FT   DOMAIN          684..777
FT                   /note="DUSP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          785..888
FT                   /note="DUSP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   ZN_FING         6..109
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   REGION          261..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        640
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TEY7"
FT   VAR_SEQ         519..526
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_038531"
FT   CONFLICT        309
FT                   /note="P -> S (in Ref. 1; AAL78316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        411
FT                   /note="L -> P (in Ref. 1; AAL78316 and 2; AAH05506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="I -> V (in Ref. 1; AAL78316 and 2; AAH05506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        779
FT                   /note="T -> S (in Ref. 2; AAH89315)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   909 AA;  102728 MW;  F8A2BDA9FBCD633A CRC64;
     MTTFRNHCPH LDSVGEITKE DLIQKSLGAC QDCKVRGPNL WACLENRCSY VGCGESQVDH
     STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTPP SLPHVRQPQQ TQENSVQDFK
     IPSNPALKTP MVAVSEDLDI EVEEEDELKA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ
     FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPA NLFQGIKTVN PTFRGYSQQD
     AQEFLRCLMD LLHEELKEQV MEMEEEPQTL TSEETVEEEK SQSDVDFQSC ESCSSSEKAE
     NESGSKGFPE DSNETTMLIQ DEDDLEMAKD WQKEKVCNKI NKANADVELD KDRDTVCETV
     DLNSQETVKV QIHGRASESI TDVHLNDLAT SQILPSNESV SPRLSASPPK LGSLWPGLSP
     PHKKAQSTSA KRKKQHKKYR SVISDIFDGT VISSVQCLTC DRVSITLETF QDLSLPIPGK
     EDLAKLHSSS HPTIVKAGSC GEAYAPQGWI AFFMEYVKRF VVSCVPSWFW GPVVTLQDCL
     AAFFARDELK GDNMYSCEKC KKLRNGVKFC KVQKFPEILC IHLKRFRHEL MFSTKISTHV
     SFPLEGLDLQ PFLAKDSPAQ IVTYDLLSVI CHHGTASSGH YIAYCRNNLN NLWYEFDDQS
     VTEVSESTVQ NAEAYVLFYR KSSEEAQKER RRISNLLNIM EPSLLQFYIS RQWLNKFKTF
     AEPGPISNND FLCIHGGIPP RKASYIEDLV LMLPQNIWDN LYSRYGGGPA VNHLYICHTC
     QIELEKIEKR RKTELEIFIR LNRAFQEEDS PATFYCISMQ WFREWESFVK GKDGDPPGPI
     DNTKIAVTKC GSVMLKQGAD SGQISEETWN FLQSIYGGGP EVILRPPVVH VDPDVLQAEE
     KIEVETRSL
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