UBP10_MOUSE
ID UBP10_MOUSE Reviewed; 792 AA.
AC P52479; Q3T9L4; Q3TNN5; Q3TZB8; Q3U5E0; Q6ZQG9; Q91VY7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE AltName: Full=Deubiquitinating enzyme 10;
DE AltName: Full=Ubiquitin thioesterase 10;
DE AltName: Full=Ubiquitin-specific-processing protease 10;
GN Name=Usp10; Synonyms=Kiaa0190, Ode-1, Uchrp;
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 2).
RA Ito M., Hitomi K., Tsukagoshi N.;
RT "Cloning from a mouse osteoblastic cell line of a gene, encoding a
RT ubiquitin carboxyl-terminal hydrolase related polypeptide, down regulated
RT during ascorbic acid dependent differentiation.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Spleen, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-223; SER-359;
RP THR-566 AND SER-570, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Hydrolase that can remove conjugated ubiquitin from target
CC proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential
CC regulator of p53/TP53 stability: in unstressed cells, specifically
CC deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2
CC action and stabilize p53/TP53. Following DNA damage, translocates to
CC the nucleus and deubiquitinates p53/TP53, leading to regulate the
CC p53/TP53-dependent DNA damage response. Component of a regulatory loop
CC that controls autophagy and p53/TP53 levels: mediates deubiquitination
CC of BECN1, a key regulator of autophagy, leading to stabilize the
CC PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing
CC complexes regulate USP10 stability, suggesting the existence of a
CC regulatory system by which PIK3C3/VPS34-containing complexes regulate
CC p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate
CC MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic
CC recycling. Involved in a TANK-dependent negative feedback response to
CC attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in
CC response to interleukin-1-beta (IL1B) stimulation or upon DNA damage.
CC Deubiquitinates TBX21 leading to its stabilization.
CC {ECO:0000250|UniProtKB:Q14694}.
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:0000250|UniProtKB:Q14694};
CC -!- ACTIVITY REGULATION: Specifically inhibited by spautin-1 (specific and
CC potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10
CC and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-
CC containing complexes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a deubiquitination complex with TANK, USP10 and
CC ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta
CC (IL1B)-mediated NF-kappaB activation by promoting IKBKG or TRAF6
CC deubiquitination. Interacts with IKBKG; this interaction increases in
CC response to DNA damage. Interacts with TANK; this interaction increases
CC in response to DNA damage. Interacts with TRAF6; this interaction
CC increases in response to DNA damage. Interacts with ZC3H12A; this
CC interaction increases in response to DNA damage. Interacts with G3BP1
CC (via NTF2-like domain) and G3BP2 (via NTF2-like domain). Interacts with
CC p53/TP53, SNX3 and CFTR. Interacts with TBX21.
CC {ECO:0000250|UniProtKB:Q14694}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus
CC {ECO:0000250|UniProtKB:Q14694}. Early endosome
CC {ECO:0000250|UniProtKB:Q14694}. Note=Cytoplasmic in normal conditions
CC (By similarity). After DNA damage, translocates to the nucleus
CC following phosphorylation by ATM (By similarity).
CC {ECO:0000250|UniProtKB:Q14694}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52479-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52479-2; Sequence=VSP_038870;
CC -!- PTM: Phosphorylated by ATM following DNA damage, leading to
CC stablization and translocation it to the nucleus. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by USP13 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D84096; BAA12220.1; -; mRNA.
DR EMBL; AK129083; BAC97893.1; ALT_INIT; mRNA.
DR EMBL; AK153675; BAE32139.1; -; mRNA.
DR EMBL; AK157970; BAE34291.1; -; mRNA.
DR EMBL; AK165156; BAE38053.1; -; mRNA.
DR EMBL; AK172443; BAE43006.1; -; mRNA.
DR EMBL; CH466525; EDL11620.1; -; Genomic_DNA.
DR EMBL; BC007134; AAH07134.1; -; mRNA.
DR CCDS; CCDS40495.1; -. [P52479-2]
DR CCDS; CCDS80938.1; -. [P52479-1]
DR RefSeq; NP_001297559.1; NM_001310630.1. [P52479-1]
DR RefSeq; NP_033488.1; NM_009462.2. [P52479-2]
DR AlphaFoldDB; P52479; -.
DR SMR; P52479; -.
DR BioGRID; 204424; 13.
DR IntAct; P52479; 5.
DR MINT; P52479; -.
DR STRING; 10090.ENSMUSP00000123590; -.
DR MEROPS; C19.018; -.
DR iPTMnet; P52479; -.
DR PhosphoSitePlus; P52479; -.
DR EPD; P52479; -.
DR jPOST; P52479; -.
DR MaxQB; P52479; -.
DR PaxDb; P52479; -.
DR PeptideAtlas; P52479; -.
DR PRIDE; P52479; -.
DR ProteomicsDB; 298358; -. [P52479-1]
DR ProteomicsDB; 298359; -. [P52479-2]
DR Antibodypedia; 1716; 394 antibodies from 38 providers.
DR DNASU; 22224; -.
DR Ensembl; ENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826. [P52479-1]
DR Ensembl; ENSMUST00000144458; ENSMUSP00000123590; ENSMUSG00000031826. [P52479-2]
DR GeneID; 22224; -.
DR KEGG; mmu:22224; -.
DR UCSC; uc009nqn.1; mouse. [P52479-2]
DR UCSC; uc009nqo.1; mouse. [P52479-1]
DR CTD; 9100; -.
DR MGI; MGI:894652; Usp10.
DR VEuPathDB; HostDB:ENSMUSG00000031826; -.
DR eggNOG; KOG1871; Eukaryota.
DR GeneTree; ENSGT00550000074994; -.
DR HOGENOM; CLU_008279_4_1_1; -.
DR InParanoid; P52479; -.
DR OMA; TPRTCDS; -.
DR OrthoDB; 1078977at2759; -.
DR PhylomeDB; P52479; -.
DR TreeFam; TF323203; -.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 22224; 5 hits in 107 CRISPR screens.
DR ChiTaRS; Usp10; mouse.
DR PRO; PR:P52479; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P52479; protein.
DR Bgee; ENSMUSG00000031826; Expressed in embryonic post-anal tail and 264 other tissues.
DR ExpressionAtlas; P52479; baseline and differential.
DR Genevisible; P52479; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
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:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028767; USP10.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR13328:SF5; PTHR13328:SF5; 1.
DR Pfam; PF07145; PAM2; 1.
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 Acetylation; Alternative splicing; Autophagy; Cytoplasm; DNA damage;
KW DNA repair; Endosome; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT CHAIN 2..792
FT /note="Ubiquitin carboxyl-terminal hydrolase 10"
FT /id="PRO_0000080630"
FT DOMAIN 409..789
FT /note="USP"
FT REGION 2..99
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000250"
FT REGION 126..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 743
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 330
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14694"
FT MOD_RES 566
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 49
FT /note="D -> DA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_038870"
FT CONFLICT 72
FT /note="P -> R (in Ref. 5; AAH07134)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="E -> D (in Ref. 5; AAH07134)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="N -> S (in Ref. 5; AAH07134)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> S (in Ref. 5; AAH07134)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="R -> G (in Ref. 3; BAE34291)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="P -> T (in Ref. 3; BAE32139)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="G -> R (in Ref. 3; BAE38053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 87022 MW; 02D07A8194215D09 CRC64;
MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG QEHQRIEFGV
DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP EAVEKDETYS SIDQYPASAL
ALESNSNAEA ETLENDSGAG GLGQRERKKK KKRPPGYYSY LKDGGEDSAS PATLVNGHAT
SVGTSGEAVE DAEFMDVLPP VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE
GCHEADFEQP CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD
EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP MAYVETKCSP
PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI HKPVSLQPRG LINKGNWCYI
NATLQALVAC PPMYHLMKFI PLYSKVQRPC TSTPMIDSFV RLMNEFTNMP VPPKPRQALG
DKIVRDIRPG AAFEPTYIYR LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL
SPTHEKHSVS NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF
GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV QGYTTKTKQE
VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY PVDLEISREL LSPGIKNKNF
KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ IGLNGWLRID DQTVKVINQY QVVKPPADRT
AYLLYYRRVD LL
