MINY3_HUMAN
ID MINY3_HUMAN Reviewed; 445 AA.
AC Q9H8M7; Q5SZ68; Q5SZ69; Q5SZ70; Q6IA40; Q6P7P0; Q7Z2S1; Q8WUF1; Q9H3I4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-3 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:27292798};
DE AltName: Full=Dermal papilla-derived protein 5 {ECO:0000303|PubMed:12054670};
DE AltName: Full=Deubiquitinating enzyme MINDY-3 {ECO:0000312|HGNC:HGNC:23578};
DE AltName: Full=Protein CARP {ECO:0000303|PubMed:12054670};
GN Name=MINDY3 {ECO:0000312|HGNC:HGNC:23578};
GN Synonyms=C10orf97 {ECO:0000312|HGNC:HGNC:23578},
GN CARP {ECO:0000303|PubMed:12054670}, DERP5 {ECO:0000303|PubMed:12054670},
GN FAM188A {ECO:0000312|HGNC:HGNC:23578};
GN ORFNames=MSTP126 {ECO:0000303|Ref.6}, My042 {ECO:0000312|HGNC:HGNC:23578};
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12054670; DOI=10.1016/s0006-291x(02)00379-0;
RA Liu B., Liu Y., Chen J., Wei Z., Yu H., Zhen Y., Lu L., Hui R.T.;
RT "CARP is a novel caspase recruitment domain containing pro-apoptotic
RT protein.";
RL Biochem. Biophys. Res. Commun. 293:1396-1404(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ikeda A., Yamashita M., Yoshimoto M.;
RT "Molecular cloning of a dermal papilla derived gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Aorta;
RA Liu B., Qin B.M., Sheng H., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
RA Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
RT "Homo sapiens normal aorta mRNA MST126.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Testis, and 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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-445.
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP INTERACTION WITH COPS5, AND TISSUE SPECIFICITY.
RX PubMed=21499297; DOI=10.1038/onc.2011.116;
RA Shi Y., Chen J., Li Z., Zhang Z., Yu H., Sun K., Wang X., Song X., Wang Y.,
RA Zhen Y., Yang T., Lou K., Zhang Y., Zhang G., Hu Y., Ji J., Hui R.;
RT "C10ORF97 is a novel tumor-suppressor gene of non-small-cell lung cancer
RT and a functional variant of this gene increases the risk of non-small-cell
RT lung cancer.";
RL Oncogene 30:4107-4117(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND GENE FAMILY.
RX PubMed=27292798; DOI=10.1016/j.molcel.2016.05.009;
RA Abdul Rehman S.A., Kristariyanto Y.A., Choi S.Y., Nkosi P.J., Weidlich S.,
RA Labib K., Hofmann K., Kulathu Y.;
RT "MINDY-1 is a member of an evolutionarily conserved and structurally
RT distinct new family of deubiquitinating enzymes.";
RL Mol. Cell 63:146-155(2016).
CC -!- FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. {ECO:0000269|PubMed:27292798}.
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:27292798};
CC -!- SUBUNIT: Interacts with COPS5. {ECO:0000269|PubMed:21499297}.
CC -!- INTERACTION:
CC Q9H8M7; Q92905: COPS5; NbExp=3; IntAct=EBI-724928, EBI-594661;
CC Q9H8M7; Q15038: DAZAP2; NbExp=3; IntAct=EBI-724928, EBI-724310;
CC Q9H8M7; P54725: RAD23A; NbExp=7; IntAct=EBI-724928, EBI-746453;
CC Q9H8M7; O00560: SDCBP; NbExp=3; IntAct=EBI-724928, EBI-727004;
CC Q9H8M7; P0CI25: TRIM49; NbExp=6; IntAct=EBI-724928, EBI-6427421;
CC Q9H8M7; P0CI26: TRIM49C; NbExp=3; IntAct=EBI-724928, EBI-12889036;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12054670}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8M7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8M7-2; Sequence=VSP_031039;
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in heart,
CC skeletal muscle, and kidney, and low levels in liver and brain
CC (PubMed:12054670). Also expressed in lung (at protein level)
CC (PubMed:21499297). {ECO:0000269|PubMed:12054670,
CC ECO:0000269|PubMed:21499297}.
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was named CARP for 'CARD domain-containing protein' by
CC PubMed:12054670. However, no CARD domain is detected by any prediction
CC tool. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH61585.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAQ13660.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAW86233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB014761; BAB87802.1; -; mRNA.
DR EMBL; AK023459; BAB14582.1; -; mRNA.
DR EMBL; AL833873; CAD38730.1; -; mRNA.
DR EMBL; CR457315; CAG33596.1; -; mRNA.
DR EMBL; AF176916; AAQ13660.1; ALT_FRAME; mRNA.
DR EMBL; AL590439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86233.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471072; EAW86234.1; -; Genomic_DNA.
DR EMBL; BC020605; AAH20605.1; -; mRNA.
DR EMBL; BC061585; AAH61585.1; ALT_SEQ; mRNA.
DR EMBL; BC067799; AAH67799.1; -; mRNA.
DR EMBL; AF063600; AAG43159.1; ALT_INIT; mRNA.
DR CCDS; CCDS7110.1; -. [Q9H8M7-1]
DR PIR; JC7861; JC7861.
DR RefSeq; NP_001305259.1; NM_001318330.1.
DR RefSeq; NP_079224.1; NM_024948.3. [Q9H8M7-1]
DR RefSeq; XP_005252657.1; XM_005252600.2.
DR RefSeq; XP_005252659.1; XM_005252602.2.
DR RefSeq; XP_011517996.1; XM_011519694.1.
DR RefSeq; XP_016872162.1; XM_017016673.1.
DR AlphaFoldDB; Q9H8M7; -.
DR BioGRID; 123069; 41.
DR IntAct; Q9H8M7; 31.
DR STRING; 9606.ENSP00000277632; -.
DR GlyGen; Q9H8M7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H8M7; -.
DR MetOSite; Q9H8M7; -.
DR PhosphoSitePlus; Q9H8M7; -.
DR BioMuta; MINDY3; -.
DR DMDM; 74761533; -.
DR EPD; Q9H8M7; -.
DR jPOST; Q9H8M7; -.
DR MassIVE; Q9H8M7; -.
DR MaxQB; Q9H8M7; -.
DR PaxDb; Q9H8M7; -.
DR PeptideAtlas; Q9H8M7; -.
DR PRIDE; Q9H8M7; -.
DR ProteomicsDB; 81227; -. [Q9H8M7-1]
DR ProteomicsDB; 81228; -. [Q9H8M7-2]
DR Antibodypedia; 25119; 44 antibodies from 16 providers.
DR DNASU; 80013; -.
DR Ensembl; ENST00000277632.8; ENSP00000277632.3; ENSG00000148481.14. [Q9H8M7-1]
DR GeneID; 80013; -.
DR KEGG; hsa:80013; -.
DR MANE-Select; ENST00000277632.8; ENSP00000277632.3; NM_024948.4; NP_079224.1.
DR UCSC; uc001iod.2; human. [Q9H8M7-1]
DR CTD; 80013; -.
DR DisGeNET; 80013; -.
DR GeneCards; MINDY3; -.
DR HGNC; HGNC:23578; MINDY3.
DR HPA; ENSG00000148481; Low tissue specificity.
DR MIM; 611649; gene.
DR neXtProt; NX_Q9H8M7; -.
DR OpenTargets; ENSG00000148481; -.
DR PharmGKB; PA165548562; -.
DR VEuPathDB; HostDB:ENSG00000148481; -.
DR eggNOG; KOG2871; Eukaryota.
DR GeneTree; ENSGT00940000155958; -.
DR HOGENOM; CLU_033478_0_0_1; -.
DR InParanoid; Q9H8M7; -.
DR OMA; HVWDHDQ; -.
DR OrthoDB; 1276386at2759; -.
DR PhylomeDB; Q9H8M7; -.
DR TreeFam; TF323996; -.
DR PathwayCommons; Q9H8M7; -.
DR SignaLink; Q9H8M7; -.
DR BioGRID-ORCS; 80013; 8 hits in 1119 CRISPR screens.
DR ChiTaRS; FAM188A; human.
DR GenomeRNAi; 80013; -.
DR Pharos; Q9H8M7; Tbio.
DR PRO; PR:Q9H8M7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H8M7; protein.
DR Bgee; ENSG00000148481; Expressed in mucosa of stomach and 189 other tissues.
DR ExpressionAtlas; Q9H8M7; baseline and differential.
DR Genevisible; Q9H8M7; HS.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR025257; MINDY-3/4_CD.
DR InterPro; IPR039785; MINY3/4.
DR PANTHER; PTHR12473; PTHR12473; 1.
DR Pfam; PF13898; DUF4205; 1.
DR SMART; SM01174; DUF4205; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..445
FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-3"
FT /id="PRO_0000317560"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 137..445
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_031039"
FT CONFLICT 31
FT /note="Q -> R (in Ref. 5; CAG33596)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="S -> G (in Ref. 9; AAH20605)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="L -> V (in Ref. 6; AAQ13660)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> A (in Ref. 5; CAG33596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49725 MW; F30B4A5E357AF52E CRC64;
MSELTKELME LVWGTKSSPG LSDTIFCRWT QGFVFSESEG SALEQFEGGP CAVIAPVQAF
LLKKLLFSSE KSSWRDCSEE EQKELLCHTL CDILESACCD HSGSYCLVSW LRGKTTEETA
SISGSPAESS CQVEHSSALA VEELGFERFH ALIQKRSFRS LPELKDAVLD QYSMWGNKFG
VLLFLYSVLL TKGIENIKNE IEDASEPLID PVYGHGSQSL INLLLTGHAV SNVWDGDREC
SGMKLLGIHE QAAVGFLTLM EALRYCKVGS YLKSPKFPIW IVGSETHLTV FFAKDMALVA
PEAPSEQARR VFQTYDPEDN GFIPDSLLED VMKALDLVSD PEYINLMKNK LDPEGLGIIL
LGPFLQEFFP DQGSSGPESF TVYHYNGLKQ SNYNEKVMYV EGTAVVMGFE DPMLQTDDTP
IKRCLQTKWP YIELLWTTDR SPSLN
