CRYL1_HUMAN
ID CRYL1_HUMAN Reviewed; 319 AA.
AC Q9Y2S2; A0PJ43; B3KN92; Q0VDI1; Q7Z4Z9; Q9P0G7;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Lambda-crystallin homolog;
DE EC=1.1.1.45 {ECO:0000269|PubMed:15809331};
DE AltName: Full=L-gulonate 3-dehydrogenase;
DE Short=Gul3DH;
GN Name=CRYL1; Synonyms=CRY;
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).
RC TISSUE=Pituitary;
RA Hu R., Song H., Peng Y., Fu G., Mao M., Zhang Q., Zhu H., Li G., Luo M.,
RA Hu R., Chen J.;
RT "Human lambda-crystallin mRNA.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=12527201; DOI=10.1016/s0378-1119(02)01095-8;
RA Chen J., Yu L., Li D., Gao Q., Wang J., Huang X., Bi G., Wu H., Zhao S.;
RT "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and kidney
RT and downregulated in 58% of liver cancer tissues from 60 Chinese patients,
RT and four new homologs from other mammalians.";
RL Gene 302:103-113(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hypothalamus;
RA Li Y., Shi J., Huang C., Jiang C., Ren S., Zhou J., Yu Y., Xu S., Wang Y.,
RA Fu G., Chen Z., Han Z.;
RT "A novel gene expressed in human hypothalamus.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 7-319 (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=15809331; DOI=10.1093/jb/mvi033;
RA Ishikura S., Usami N., Araki M., Hara A.;
RT "Structural and functional characterization of rabbit and human L-gulonate
RT 3-dehydrogenase.";
RL J. Biochem. 137:303-314(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-316 IN COMPLEX WITH NAD.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human lambda-crystallin, CRYL1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Has high L-gulonate 3-dehydrogenase activity. It also
CC exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA)
CC and L-threonate. {ECO:0000269|PubMed:15809331}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH;
CC Xref=Rhea:RHEA:12889, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945; EC=1.1.1.45;
CC Evidence={ECO:0000269|PubMed:15809331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12890;
CC Evidence={ECO:0000305|PubMed:15809331};
CC -!- ACTIVITY REGULATION: Inhibited by malonate.
CC {ECO:0000269|PubMed:15809331}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.01 mM for NAD {ECO:0000269|PubMed:15809331};
CC KM=0.0008 mM for NADH {ECO:0000269|PubMed:15809331};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15809331, ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2S2-2; Sequence=VSP_034641;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver and
CC kidney. {ECO:0000269|PubMed:12527201}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27782.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD27782.1; Type=Miscellaneous discrepancy; Note=Unknown reasons.; Evidence={ECO:0000305};
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DR EMBL; AF077049; AAD27782.1; ALT_SEQ; mRNA.
DR EMBL; AF087898; AAP97197.1; -; mRNA.
DR EMBL; AF160216; AAF67017.1; -; mRNA.
DR EMBL; AK024041; BAG51254.1; -; mRNA.
DR EMBL; AL161715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08259.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08260.1; -; Genomic_DNA.
DR EMBL; BC008562; AAH08562.2; -; mRNA.
DR EMBL; BC071810; AAH71810.1; -; mRNA.
DR EMBL; BC119660; AAI19661.2; -; mRNA.
DR EMBL; BC119661; AAI19662.2; -; mRNA.
DR CCDS; CCDS41871.1; -. [Q9Y2S2-1]
DR RefSeq; NP_057058.2; NM_015974.2. [Q9Y2S2-1]
DR PDB; 3F3S; X-ray; 2.00 A; A/B=6-316.
DR PDBsum; 3F3S; -.
DR AlphaFoldDB; Q9Y2S2; -.
DR SMR; Q9Y2S2; -.
DR BioGRID; 119274; 53.
DR IntAct; Q9Y2S2; 35.
DR STRING; 9606.ENSP00000298248; -.
DR iPTMnet; Q9Y2S2; -.
DR PhosphoSitePlus; Q9Y2S2; -.
DR BioMuta; CRYL1; -.
DR DMDM; 93141249; -.
DR OGP; Q9Y2S2; -.
DR REPRODUCTION-2DPAGE; IPI00645031; -.
DR EPD; Q9Y2S2; -.
DR jPOST; Q9Y2S2; -.
DR MassIVE; Q9Y2S2; -.
DR MaxQB; Q9Y2S2; -.
DR PaxDb; Q9Y2S2; -.
DR PeptideAtlas; Q9Y2S2; -.
DR PRIDE; Q9Y2S2; -.
DR ProteomicsDB; 85884; -. [Q9Y2S2-1]
DR ProteomicsDB; 85885; -. [Q9Y2S2-2]
DR Antibodypedia; 49573; 72 antibodies from 14 providers.
DR DNASU; 51084; -.
DR Ensembl; ENST00000298248.12; ENSP00000298248.7; ENSG00000165475.15. [Q9Y2S2-1]
DR Ensembl; ENST00000382812.5; ENSP00000372262.1; ENSG00000165475.15. [Q9Y2S2-2]
DR Ensembl; ENST00000643750.1; ENSP00000493818.1; ENSG00000165475.15. [Q9Y2S2-2]
DR GeneID; 51084; -.
DR KEGG; hsa:51084; -.
DR MANE-Select; ENST00000298248.12; ENSP00000298248.7; NM_015974.3; NP_057058.2.
DR UCSC; uc001ung.4; human. [Q9Y2S2-1]
DR CTD; 51084; -.
DR DisGeNET; 51084; -.
DR GeneCards; CRYL1; -.
DR HGNC; HGNC:18246; CRYL1.
DR HPA; ENSG00000165475; Tissue enhanced (kidney, liver).
DR MIM; 609877; gene.
DR neXtProt; NX_Q9Y2S2; -.
DR OpenTargets; ENSG00000165475; -.
DR PharmGKB; PA26923; -.
DR VEuPathDB; HostDB:ENSG00000165475; -.
DR eggNOG; KOG2305; Eukaryota.
DR GeneTree; ENSGT00390000007182; -.
DR HOGENOM; CLU_009834_0_0_1; -.
DR InParanoid; Q9Y2S2; -.
DR OMA; RDNCLTH; -.
DR PhylomeDB; Q9Y2S2; -.
DR TreeFam; TF313501; -.
DR PathwayCommons; Q9Y2S2; -.
DR Reactome; R-HSA-5661270; Formation of xylulose-5-phosphate.
DR SABIO-RK; Q9Y2S2; -.
DR SignaLink; Q9Y2S2; -.
DR BioGRID-ORCS; 51084; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; CRYL1; human.
DR EvolutionaryTrace; Q9Y2S2; -.
DR GenomeRNAi; 51084; -.
DR Pharos; Q9Y2S2; Tbio.
DR PRO; PR:Q9Y2S2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y2S2; protein.
DR Bgee; ENSG00000165475; Expressed in adult mammalian kidney and 184 other tissues.
DR ExpressionAtlas; Q9Y2S2; baseline and differential.
DR Genevisible; Q9Y2S2; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P14755"
FT CHAIN 2..319
FT /note="Lambda-crystallin homolog"
FT /id="PRO_0000109320"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.11"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P14755"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811X6"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_034641"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:3F3S"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3F3S"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3F3S"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3F3S"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 248..263
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:3F3S"
FT HELIX 292..315
FT /evidence="ECO:0007829|PDB:3F3S"
SQ SEQUENCE 319 AA; 35419 MW; C8DCF74DDE2FDE21 CRC64;
MASSAAGCVV IVGSGVIGRS WAMLFASGGF QVKLYDIEQQ QIRNALENIR KEMKLLEQAG
SLKGSLSVEE QLSLISGCPN IQEAVEGAMH IQECVPEDLE LKKKIFAQLD SIIDDRVILS
SSTSCLMPSK LFAGLVHVKQ CIVAHPVNPP YYIPLVELVP HPETAPTTVD RTHALMKKIG
QCPMRVQKEV AGFVLNRLQY AIISEAWRLV EEGIVSPSDL DLVMSEGLGM RYAFIGPLET
MHLNAEGMLS YCDRYSEGIK HVLQTFGPIP EFSRATAEKV NQDMCMKVPD DPEHLAARRQ
WRDECLMRLA KLKSQVQPQ
