CBPC2_MOUSE
ID CBPC2_MOUSE Reviewed; 862 AA.
AC Q8CDK2; A2AH35; Q09M08; Q09M09; Q09M10; Q09M11; Q09M12; Q8C529; Q8C9X4;
AC Q8CDE6; Q8CDF6; Q8CDQ1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytosolic carboxypeptidase 2 {ECO:0000303|PubMed:25103237};
DE EC=3.4.17.- {ECO:0000269|PubMed:25103237};
DE AltName: Full=ATP/GTP-binding protein-like 2;
DE AltName: Full=Protein deglutamylase CCP2 {ECO:0000305};
GN Name=Agbl2 {ECO:0000312|MGI:MGI:2443254};
GN Synonyms=Ccp2 {ECO:0000303|PubMed:25103237};
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] (ISOFORMS 1; 2; 3; 4 AND 5), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BLKS/J;
RX PubMed=17244818; DOI=10.1096/fj.06-7329com;
RA Kalinina E., Biswas R., Berezniuk I., Hermoso A., Aviles F.X.,
RA Fricker L.D.;
RT "A novel subfamily of mouse cytosolic carboxypeptidases.";
RL FASEB J. 21:836-850(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 6 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Testis, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLU-593.
RX PubMed=25103237; DOI=10.1091/mbc.e14-06-1072;
RA Tort O., Tanco S., Rocha C., Bieche I., Seixas C., Bosc C., Andrieux A.,
RA Moutin M.J., Aviles F.X., Lorenzo J., Janke C.;
RT "The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational
RT removal of acidic amino acids.";
RL Mol. Biol. Cell 25:3017-3027(2014).
CC -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC tubulin and non-tubulin target proteins (PubMed:25103237). Catalyzes
CC the removal of polyglutamate side chains present on the gamma-carboxyl
CC group of glutamate residues within the C-terminal tail of tubulin
CC protein (PubMed:25103237). Specifically cleaves tubulin long-side-
CC chains, while it is not able to remove the branching point glutamate
CC (PubMed:25103237). Also catalyzes the removal of polyglutamate residues
CC from the carboxy-terminus of non-tubulin proteins such as MYLK
CC (PubMed:25103237). {ECO:0000269|PubMed:25103237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC Evidence={ECO:0000269|PubMed:25103237};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000305|PubMed:25103237};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by RARRES1. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RARRES1, KIF11 AND MAPRE1.
CC {ECO:0000250|UniProtKB:Q5U5Z8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:Q5U5Z8}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000250|UniProtKB:Q5U5Z8}. Note=Colocalizes with
CC gamma-tubulin in the centrioles and with glutamylated tubulin in the
CC basal bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5U5Z8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8CDK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDK2-2; Sequence=VSP_024366, VSP_024368;
CC Name=3;
CC IsoId=Q8CDK2-3; Sequence=VSP_024367, VSP_024369;
CC Name=4;
CC IsoId=Q8CDK2-4; Sequence=VSP_024365;
CC Name=5;
CC IsoId=Q8CDK2-5; Sequence=VSP_024364, VSP_024365;
CC Name=6;
CC IsoId=Q8CDK2-6; Sequence=VSP_024363, VSP_024366, VSP_024368;
CC Name=7;
CC IsoId=Q8CDK2-7; Sequence=VSP_024362, VSP_024367, VSP_024369;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in tissues with motile
CC cilia such as testis, lung and trachea. Also detected in brain, eye,
CC muscle, pancreas, intestine, stomach, pituitary, spleen, adrenal and
CC kidney. Expressed in mitral and granular cells in brain.
CC {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:25103237}.
CC -!- INDUCTION: Up-regulated during ciliogenesis.
CC {ECO:0000269|PubMed:25103237}.
CC -!- DISRUPTION PHENOTYPE: AGBL2 and AGBL3 double mutants are viable and
CC display no obvious phenotypic alterations.
CC {ECO:0000269|PubMed:25103237}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Was initially shown to catalyze the removal of carboxy-
CC terminus tyrosine from alpha-tubulin (By similarity). However, later
CC studies did not identified any detyrosinase or deglycylase activities
CC from the carboxy-terminus of tubulin (PubMed:25103237).
CC {ECO:0000250|UniProtKB:Q5U5Z8, ECO:0000269|PubMed:25103237}.
CC -!- CAUTION: Was originally thought to have detyrosinating activity from C-
CC terminal positions on tubulin. {ECO:0000250|UniProtKB:Q5U5Z8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI51945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABI51946.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABI51947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABI51948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABI51949.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC37726.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM20823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ867026; ABI51945.1; ALT_INIT; mRNA.
DR EMBL; DQ867027; ABI51946.1; ALT_INIT; mRNA.
DR EMBL; DQ867028; ABI51947.1; ALT_INIT; mRNA.
DR EMBL; DQ867029; ABI51948.1; ALT_INIT; mRNA.
DR EMBL; DQ867030; ABI51949.1; ALT_INIT; mRNA.
DR EMBL; AK029744; BAC26594.1; -; mRNA.
DR EMBL; AK029932; BAC26686.1; -; mRNA.
DR EMBL; AK030138; BAC26802.1; -; mRNA.
DR EMBL; AK030182; BAC26827.1; -; mRNA.
DR EMBL; AK040259; BAC30555.2; -; mRNA.
DR EMBL; AK079691; BAC37726.2; ALT_INIT; mRNA.
DR EMBL; AL714026; CAM20823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL714026; CAM20824.1; -; Genomic_DNA.
DR EMBL; AL714026; CAM20825.1; -; Genomic_DNA.
DR CCDS; CCDS38177.2; -. [Q8CDK2-1]
DR CCDS; CCDS89512.1; -. [Q8CDK2-6]
DR RefSeq; NP_848870.2; NM_178755.3. [Q8CDK2-1]
DR RefSeq; XP_006499695.1; XM_006499632.2. [Q8CDK2-1]
DR RefSeq; XP_006499703.1; XM_006499640.1. [Q8CDK2-4]
DR RefSeq; XP_006499704.1; XM_006499641.3.
DR RefSeq; XP_006499705.1; XM_006499642.3. [Q8CDK2-2]
DR RefSeq; XP_006499706.1; XM_006499643.1. [Q8CDK2-5]
DR RefSeq; XP_011237881.1; XM_011239579.1. [Q8CDK2-5]
DR AlphaFoldDB; Q8CDK2; -.
DR SMR; Q8CDK2; -.
DR STRING; 10090.ENSMUSP00000129216; -.
DR MEROPS; M14.029; -.
DR iPTMnet; Q8CDK2; -.
DR PhosphoSitePlus; Q8CDK2; -.
DR MaxQB; Q8CDK2; -.
DR PaxDb; Q8CDK2; -.
DR PRIDE; Q8CDK2; -.
DR ProteomicsDB; 283690; -. [Q8CDK2-1]
DR ProteomicsDB; 283691; -. [Q8CDK2-2]
DR ProteomicsDB; 283692; -. [Q8CDK2-3]
DR ProteomicsDB; 283693; -. [Q8CDK2-4]
DR ProteomicsDB; 283694; -. [Q8CDK2-5]
DR ProteomicsDB; 283695; -. [Q8CDK2-6]
DR ProteomicsDB; 283696; -. [Q8CDK2-7]
DR Antibodypedia; 1166; 123 antibodies from 22 providers.
DR DNASU; 271813; -.
DR Ensembl; ENSMUST00000037206; ENSMUSP00000047936; ENSMUSG00000040812. [Q8CDK2-6]
DR Ensembl; ENSMUST00000037219; ENSMUSP00000048647; ENSMUSG00000040812. [Q8CDK2-1]
DR Ensembl; ENSMUST00000051831; ENSMUSP00000051620; ENSMUSG00000040812. [Q8CDK2-3]
DR Ensembl; ENSMUST00000111481; ENSMUSP00000107106; ENSMUSG00000040812. [Q8CDK2-1]
DR Ensembl; ENSMUST00000170320; ENSMUSP00000129216; ENSMUSG00000040812. [Q8CDK2-1]
DR GeneID; 271813; -.
DR KEGG; mmu:271813; -.
DR UCSC; uc008ktc.2; mouse. [Q8CDK2-6]
DR UCSC; uc008ktd.2; mouse. [Q8CDK2-2]
DR UCSC; uc008kte.2; mouse. [Q8CDK2-1]
DR UCSC; uc008ktg.2; mouse. [Q8CDK2-4]
DR UCSC; uc008kth.2; mouse. [Q8CDK2-5]
DR UCSC; uc008ktk.1; mouse. [Q8CDK2-7]
DR CTD; 79841; -.
DR MGI; MGI:2443254; Agbl2.
DR VEuPathDB; HostDB:ENSMUSG00000040812; -.
DR eggNOG; KOG3641; Eukaryota.
DR GeneTree; ENSGT00940000160201; -.
DR InParanoid; Q8CDK2; -.
DR OMA; TDVVLYC; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q8CDK2; -.
DR TreeFam; TF313794; -.
DR BioGRID-ORCS; 271813; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Agbl2; mouse.
DR PRO; PR:Q8CDK2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CDK2; protein.
DR Bgee; ENSMUSG00000040812; Expressed in spermatocyte and 42 other tissues.
DR ExpressionAtlas; Q8CDK2; baseline and differential.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035610; P:protein side chain deglutamylation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Cell projection; Cytoplasm;
KW Cytoskeleton; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..862
FT /note="Cytosolic carboxypeptidase 2"
FT /id="PRO_0000283750"
FT REGION 669..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09M02"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT VAR_SEQ 1..298
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024362"
FT VAR_SEQ 2..12
FT /note="NVLLEMAFLSQ -> FPALETELKPE (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024363"
FT VAR_SEQ 79..97
FT /note="WPTCLSSTGHAHIDAVNRD -> Y (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17244818"
FT /id="VSP_024364"
FT VAR_SEQ 744..779
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17244818"
FT /id="VSP_024365"
FT VAR_SEQ 806..809
FT /note="SKKP -> GFST (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_024366"
FT VAR_SEQ 807..836
FT /note="KKPGFTASCSPKRSTNSSLGPAPDVKPNWS -> YSQPCVFSLILHEHQAQT
FT SSDTPCQNPESH (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_024367"
FT VAR_SEQ 810..862
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_024368"
FT VAR_SEQ 837..862
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17244818"
FT /id="VSP_024369"
FT MUTAGEN 593
FT /note="E->A: Abolishes deglutamylase activity."
FT /evidence="ECO:0000269|PubMed:25103237"
FT CONFLICT 134
FT /note="S -> F (in Ref. 2; BAC26827)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="I -> L (in Ref. 2; BAC26827)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> T (in Ref. 2; BAC26827)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="V -> F (in Ref. 2; BAC26827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 862 AA; 99216 MW; B532FEB80F6A8D04 CRC64;
MNVLLEMAFL SQTLPDPYED FIHHHLQYYG YFKAQKSSLP NSGTHQRVWR NSPRYMLNGS
FGERDDFISD SLEKEMLLWP TCLSSTGHAH IDAVNRDSLL LSSPLLRTRQ LIFDELDEAS
PRLREPRELF SCFSSRGPLQ APRWPIECEV IKENIHHIEW VPHQPEYFYQ PTGSEKVPEI
VGEEQGTVVY QLDSVPAEGT YFTSSRIGGK RGTIKELAVT LQGPDDNTLL FESRFESGNL
QKAVRVGIYE YELTLRTDLY TDKHTQWFYF RVQNTRKDAT YRFTIVNLLK PKSLYAVGMK
PLMYSQLDAT IYNIGWRREG REIKYYKNNV DDGQQPLYCL TWTTQFPHDQ DTCFFAHFYP
YTYTDLQCYL LSVANNPIQS QFCKLRALCR SLAGNTVYLL TITNPSRTPQ EAAAKKAVVL
SARVHPGESN SSWIMNGFLD FILSNSPDAQ LLRDIFVFKV IPMLNPDGVI VGNYRCSLAG
RDLNRHYKTV LKDSFPCIWY TKNMIKRLLE EREVLLYCDF HGHSRKNNIF LYGCHSNNRK
HWLHERVFPL MLSKNAPDKF SFDSCNFKVQ KCKEGTGRVV MWRMGIINSY TMESTFGGST
LGSKRDTHFT IEDLKSLGYH VCDTLLDFCD PDQTKYTQCL QELKELLQQE INKKLNNFGQ
DMDLEGNWSD IPLSDIESST SGSDSSLSDG PPIRLLNIVA DEPNQKTVLK NPKKKRLQTR
KQRNEQYQKS YLMRELKLTE NAPGRARFVS TLQKQPTFLK SPESPSPSVR RSENPRLNET
QLSGREKGTS LDPPLTSPKN KERIQSKKPG FTASCSPKRS TNSSLGPAPD VKPNWSKTRY
SATRKDHATM AVYPSLHIYT YP
