UBP38_HUMAN
ID UBP38_HUMAN Reviewed; 1042 AA.
AC Q8NB14; B3KX93; Q3ZCV1; Q8NDF5; Q96DK6; Q96PZ6; Q9BY55;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 38;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 38;
DE AltName: Full=HP43.8KD;
DE AltName: Full=Ubiquitin thioesterase 38;
DE AltName: Full=Ubiquitin-specific-processing protease 38;
GN Name=USP38; Synonyms=KIAA1891;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Chondrocyte, and Gastric mucosa;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1042 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1042 (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [8]
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 [9]
RP FUNCTION, AND LINKAGE SPECIFICITY.
RX PubMed=22689415; DOI=10.1002/cbic.201200261;
RA Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R.,
RA van den Heuvel J., Kessler B.M., Jansch L., Franke R.;
RT "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with
RT branched ubiquitin isopeptide probes.";
RL ChemBioChem 13:1416-1420(2012).
CC -!- FUNCTION: Deubiquitinating enzyme exhibiting a preference towards 'Lys-
CC 63'-linked ubiquitin chains. {ECO:0000269|PubMed:22689415}.
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 -!- INTERACTION:
CC Q8NB14; Q92993: KAT5; NbExp=3; IntAct=EBI-2512509, EBI-399080;
CC Q8NB14; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2512509, EBI-11742507;
CC Q8NB14; P17252: PRKCA; NbExp=3; IntAct=EBI-2512509, EBI-1383528;
CC Q8NB14; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2512509, EBI-9090795;
CC Q8NB14; P61981: YWHAG; NbExp=3; IntAct=EBI-2512509, EBI-359832;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NB14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB14-2; Sequence=VSP_054486;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Expressed in
CC adrenal gland. {ECO:0000269|PubMed:11572484,
CC ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK26248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB71627.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03730.1; Type=Miscellaneous discrepancy; Note=The absence of the residues from Tyr-840 to Ser-871 is not the result of an alternative splicing.; Evidence={ECO:0000305};
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DR EMBL; AK057992; BAB71627.1; ALT_INIT; mRNA.
DR EMBL; AK091712; BAC03730.1; ALT_SEQ; mRNA.
DR EMBL; AK126943; BAG54405.1; -; mRNA.
DR EMBL; AL833976; CAD38820.1; -; mRNA.
DR EMBL; AC099549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX05075.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05076.1; -; Genomic_DNA.
DR EMBL; BC039115; AAH39115.1; -; mRNA.
DR EMBL; BC068975; AAH68975.1; -; mRNA.
DR EMBL; AB067478; BAB67784.1; -; mRNA.
DR EMBL; AF211481; AAK26248.1; ALT_INIT; mRNA.
DR CCDS; CCDS3758.1; -. [Q8NB14-1]
DR CCDS; CCDS77964.1; -. [Q8NB14-2]
DR RefSeq; NP_001277254.1; NM_001290325.1. [Q8NB14-2]
DR RefSeq; NP_001277255.1; NM_001290326.1.
DR RefSeq; NP_115946.2; NM_032557.6. [Q8NB14-1]
DR PDB; 4RXX; X-ray; 2.06 A; A=1-424.
DR PDBsum; 4RXX; -.
DR AlphaFoldDB; Q8NB14; -.
DR SMR; Q8NB14; -.
DR BioGRID; 124165; 31.
DR IntAct; Q8NB14; 15.
DR MINT; Q8NB14; -.
DR STRING; 9606.ENSP00000303434; -.
DR MEROPS; C19.056; -.
DR iPTMnet; Q8NB14; -.
DR PhosphoSitePlus; Q8NB14; -.
DR BioMuta; USP38; -.
DR EPD; Q8NB14; -.
DR jPOST; Q8NB14; -.
DR MassIVE; Q8NB14; -.
DR MaxQB; Q8NB14; -.
DR PaxDb; Q8NB14; -.
DR PeptideAtlas; Q8NB14; -.
DR PRIDE; Q8NB14; -.
DR ProteomicsDB; 61916; -.
DR ProteomicsDB; 72715; -. [Q8NB14-1]
DR Antibodypedia; 27336; 139 antibodies from 26 providers.
DR DNASU; 84640; -.
DR Ensembl; ENST00000307017.9; ENSP00000303434.4; ENSG00000170185.11. [Q8NB14-1]
DR Ensembl; ENST00000510377.5; ENSP00000427647.1; ENSG00000170185.11. [Q8NB14-2]
DR GeneID; 84640; -.
DR KEGG; hsa:84640; -.
DR MANE-Select; ENST00000307017.9; ENSP00000303434.4; NM_032557.6; NP_115946.2.
DR UCSC; uc003ija.5; human. [Q8NB14-1]
DR CTD; 84640; -.
DR DisGeNET; 84640; -.
DR GeneCards; USP38; -.
DR HGNC; HGNC:20067; USP38.
DR HPA; ENSG00000170185; Tissue enhanced (skeletal).
DR MIM; 618322; gene.
DR neXtProt; NX_Q8NB14; -.
DR OpenTargets; ENSG00000170185; -.
DR PharmGKB; PA134880611; -.
DR VEuPathDB; HostDB:ENSG00000170185; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000158403; -.
DR HOGENOM; CLU_010910_0_0_1; -.
DR InParanoid; Q8NB14; -.
DR OMA; AFVCDSV; -.
DR OrthoDB; 802596at2759; -.
DR PhylomeDB; Q8NB14; -.
DR TreeFam; TF324529; -.
DR PathwayCommons; Q8NB14; -.
DR SignaLink; Q8NB14; -.
DR BioGRID-ORCS; 84640; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; USP38; human.
DR GenomeRNAi; 84640; -.
DR Pharos; Q8NB14; Tbio.
DR PRO; PR:Q8NB14; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8NB14; protein.
DR Bgee; ENSG00000170185; Expressed in vastus lateralis and 190 other tissues.
DR ExpressionAtlas; Q8NB14; baseline and differential.
DR Genevisible; Q8NB14; 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:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02664; Peptidase_C19H; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033840; USP38.
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; Hydrolase; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1042
FT /note="Ubiquitin carboxyl-terminal hydrolase 38"
FT /id="PRO_0000080668"
FT DOMAIN 445..949
FT /note="USP"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 857
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VAR_SEQ 990..1042
FT /note="EQELNARARALQAASASCSFRPNGFDDNDPPGSCGPTGGGGGGGFNTVGRLV
FT F -> VSWKYKLYLLKILNN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054486"
FT CONFLICT 646
FT /note="M -> V (in Ref. 1; BAC03730)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="S -> G (in Ref. 1; BAB71627)"
FT /evidence="ECO:0000305"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 185..208
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 286..299
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 303..319
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4RXX"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 368..387
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:4RXX"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:4RXX"
SQ SEQUENCE 1042 AA; 116546 MW; D888D4F44C6E7251 CRC64;
MDKILEGLVS SSHPLPLKRV IVRKVVESAE HWLDEAQCEA MFDLTTRLIL EGQDPFQRQV
GHQVLEAYAR YHRPEFESFF NKTFVLGLLH QGYHSLDRKD VAILDYIHNG LKLIMSCPSV
LDLFSLLQVE VLRMVCERPE PQLCARLSDL LTDFVQCIPK GKLSITFCQQ LVRTIGHFQC
VSTQERELRE YVSQVTKVSN LLQNIWKAEP ATLLPSLQEV FASISSTDAS FEPSVALASL
VQHIPLQMIT VLIRSLTTDP NVKDASMTQA LCRMIDWLSW PLAQHVDTWV IALLKGLAAV
QKFTILIDVT LLKIELVFNR LWFPLVRPGA LAVLSHMLLS FQHSPEAFHL IVPHVVNLVH
SFKNDGLPSS TAFLVQLTEL IHCMMYHYSG FPDLYEPILE AIKDFPKPSE EKIKLILNQS
AWTSQSNSLA SCLSRLSGKS ETGKTGLINL GNTCYMNSVI QALFMATDFR RQVLSLNLNG
CNSLMKKLQH LFAFLAHTQR EAYAPRIFFE ASRPPWFTPR SQQDCSEYLR FLLDRLHEEE
KILKVQASHK PSEILECSET SLQEVASKAA VLTETPRTSD GEKTLIEKMF GGKLRTHIRC
LNCRSTSQKV EAFTDLSLAF CPSSSLENMS VQDPASSPSI QDGGLMQASV PGPSEEPVVY
NPTTAAFICD SLVNEKTIGS PPNEFYCSEN TSVPNESNKI LVNKDVPQKP GGETTPSVTD
LLNYFLAPEI LTGDNQYYCE NCASLQNAEK TMQITEEPEY LILTLLRFSY DQKYHVRRKI
LDNVSLPLVL ELPVKRITSF SSLSESWSVD VDFTDLSENL AKKLKPSGTD EASCTKLVPY
LLSSVVVHSG ISSESGHYYS YARNITSTDS SYQMYHQSEA LALASSQSHL LGRDSPSAVF
EQDLENKEMS KEWFLFNDSR VTFTSFQSVQ KITSRFPKDT AYVLLYKKQH STNGLSGNNP
TSGLWINGDP PLQKELMDAI TKDNKLYLQE QELNARARAL QAASASCSFR PNGFDDNDPP
GSCGPTGGGG GGGFNTVGRL VF
