CAN9_HUMAN
ID CAN9_HUMAN Reviewed; 690 AA.
AC O14815; B1APS1; B1AQI0; Q9NS74;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Calpain-9;
DE EC=3.4.22.-;
DE AltName: Full=Digestive tract-specific calpain;
DE AltName: Full=New calpain 4;
DE Short=nCL-4;
DE AltName: Full=Protein CG36;
GN Name=CAPN9; Synonyms=NCL4;
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=Stomach;
RX PubMed=9524069; DOI=10.1515/bchm.1998.379.2.175;
RA Lee H.-J., Sorimachi H., Jeong S.-Y., Ishiura S., Suzuki K.;
RT "Molecular cloning and characterization of a novel tissue-specific calpain
RT predominantly expressed in the digestive tract.";
RL Biol. Chem. 379:175-183(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10835488; DOI=10.1111/j.1349-7006.2000.tb00967.x;
RA Yoshikawa Y., Mukai H., Hino F., Asada K., Kato I.;
RT "Isolation of two novel genes, down-regulated in gastric cancer.";
RL Jpn. J. Cancer Res. 91:459-463(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-102; ARG-122; ASN-164;
RP THR-234; THR-239; TRP-277; GLN-322; GLN-327; LYS-342; TRP-458; TRP-522 AND
RP ILE-611.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 28-347, ACTIVE SITE, AND
RP CALCIUM-BINDING SITES.
RX PubMed=17157313; DOI=10.1016/j.jmb.2006.11.037;
RA Davis T.L., Walker J.R., Finerty P.J. Jr., Mackenzie F., Newman E.M.,
RA Dhe-Paganon S.;
RT "The crystal structures of human calpains 1 and 9 imply diverse mechanisms
RT of action and auto-inhibition.";
RL J. Mol. Biol. 366:216-229(2007).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14815-1; Sequence=Displayed;
CC Name=2; Synonyms=CG36;
CC IsoId=O14815-2; Sequence=VSP_007553;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in stomach.
CC -!- INDUCTION: Down-regulated in gastric cancer tissue and in gastric cell
CC lines of differentiated and poorly differentiated types.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/capn9/";
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DR EMBL; AF022799; AAB80762.1; -; mRNA.
DR EMBL; AB038463; BAA92137.1; -; mRNA.
DR EMBL; AY874864; AAW49735.1; -; Genomic_DNA.
DR EMBL; AL512328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1586.1; -. [O14815-1]
DR CCDS; CCDS31053.1; -. [O14815-2]
DR RefSeq; NP_001306605.1; NM_001319676.1.
DR RefSeq; NP_006606.1; NM_006615.2. [O14815-1]
DR RefSeq; NP_057536.1; NM_016452.2. [O14815-2]
DR PDB; 1ZIV; X-ray; 2.31 A; A=28-347.
DR PDB; 2P0R; X-ray; 2.50 A; A/B=10-340.
DR PDBsum; 1ZIV; -.
DR PDBsum; 2P0R; -.
DR AlphaFoldDB; O14815; -.
DR SMR; O14815; -.
DR BioGRID; 115976; 2.
DR STRING; 9606.ENSP00000271971; -.
DR ChEMBL; CHEMBL4523126; -.
DR MEROPS; C02.006; -.
DR iPTMnet; O14815; -.
DR PhosphoSitePlus; O14815; -.
DR BioMuta; CAPN9; -.
DR jPOST; O14815; -.
DR MassIVE; O14815; -.
DR PaxDb; O14815; -.
DR PeptideAtlas; O14815; -.
DR PRIDE; O14815; -.
DR ProteomicsDB; 48253; -. [O14815-1]
DR ProteomicsDB; 48254; -. [O14815-2]
DR Antibodypedia; 20792; 247 antibodies from 31 providers.
DR DNASU; 10753; -.
DR Ensembl; ENST00000271971.7; ENSP00000271971.2; ENSG00000135773.13. [O14815-1]
DR Ensembl; ENST00000354537.1; ENSP00000346538.1; ENSG00000135773.13. [O14815-2]
DR GeneID; 10753; -.
DR KEGG; hsa:10753; -.
DR MANE-Select; ENST00000271971.7; ENSP00000271971.2; NM_006615.3; NP_006606.1.
DR UCSC; uc001htz.2; human. [O14815-1]
DR CTD; 10753; -.
DR DisGeNET; 10753; -.
DR GeneCards; CAPN9; -.
DR HGNC; HGNC:1486; CAPN9.
DR HPA; ENSG00000135773; Tissue enhanced (intestine, stomach).
DR MIM; 606401; gene.
DR neXtProt; NX_O14815; -.
DR OpenTargets; ENSG00000135773; -.
DR PharmGKB; PA26066; -.
DR VEuPathDB; HostDB:ENSG00000135773; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158966; -.
DR HOGENOM; CLU_010982_0_3_1; -.
DR InParanoid; O14815; -.
DR OMA; SADHCEF; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; O14815; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B28; 2681.
DR BRENDA; 3.4.22.B29; 2681.
DR PathwayCommons; O14815; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 10753; 20 hits in 1068 CRISPR screens.
DR ChiTaRS; CAPN9; human.
DR EvolutionaryTrace; O14815; -.
DR GeneWiki; CAPN9; -.
DR GenomeRNAi; 10753; -.
DR Pharos; O14815; Tbio.
DR PRO; PR:O14815; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14815; protein.
DR Bgee; ENSG00000135773; Expressed in C1 segment of cervical spinal cord and 100 other tissues.
DR ExpressionAtlas; O14815; baseline and differential.
DR Genevisible; O14815; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029542; CAPN9.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF385; PTHR10183:SF385; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..690
FT /note="Calpain-9"
FT /id="PRO_0000207722"
FT DOMAIN 42..337
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 518..552
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 561..589
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 591..626
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..521
FT /note="Domain III"
FT REGION 498..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..690
FT /note="Domain IV"
FT ACT_SITE 97
FT /evidence="ECO:0000269|PubMed:17157313"
FT ACT_SITE 254
FT /evidence="ECO:0000269|PubMed:17157313"
FT ACT_SITE 278
FT /evidence="ECO:0000269|PubMed:17157313"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 608
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 292..318
FT /note="SSPEWRSVGPAEQKRLCHTALDDGEFW -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10835488"
FT /id="VSP_007553"
FT VARIANT 102
FT /note="A -> V (in dbSNP:rs12562749)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022188"
FT VARIANT 122
FT /note="S -> R (in dbSNP:rs28359608)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022189"
FT VARIANT 164
FT /note="D -> N (in dbSNP:rs28359632)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022190"
FT VARIANT 234
FT /note="I -> T (in dbSNP:rs28359644)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022191"
FT VARIANT 239
FT /note="A -> T (in dbSNP:rs28359647)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022192"
FT VARIANT 277
FT /note="R -> W (in dbSNP:rs28359655)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022193"
FT VARIANT 322
FT /note="K -> Q (in dbSNP:rs1933631)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022194"
FT VARIANT 327
FT /note="H -> Q (in dbSNP:rs28359684)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022195"
FT VARIANT 342
FT /note="E -> K (in dbSNP:rs16852652)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022196"
FT VARIANT 458
FT /note="R -> W (in dbSNP:rs28359688)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022197"
FT VARIANT 522
FT /note="R -> W (in dbSNP:rs12731961)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022198"
FT VARIANT 611
FT /note="M -> I (in dbSNP:rs16852683)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022199"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2P0R"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2P0R"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2P0R"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:1ZIV"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:1ZIV"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1ZIV"
SQ SEQUENCE 690 AA; 79097 MW; 02176C04BE1E5C23 CRC64;
MPYLYRAPGP QAHPVPKDAR ITHSSGQSFE QMRQECLQRG TLFEDADFPA SNSSLFYSER
PQIPFVWKRP GEIVKNPEFI LGGATRTDIC QGELGDCWLL AAIASLTLNQ KALARVIPQD
QSFGPGYAGI FHFQFWQHSE WLDVVIDDRL PTFRDRLVFL HSADHNEFWS ALLEKAYAKL
NGSYEALKGG SAIEAMEDFT GGVAETFQTK EAPENFYEIL EKALKRGSLL GCFIDTRSAA
ESEARTPFGL IKGHAYSVTG IDQVSFRGQR IELIRIRNPW GQVEWNGSWS DSSPEWRSVG
PAEQKRLCHT ALDDGEFWMA FKDFKAHFDK VEICNLTPDA LEEDAIHKWE VTVHQGSWVR
GSTAGGCRNF LDTFWTNPQI KLSLTEKDEG QEECSFLVAL MQKDRRKLKR FGANVLTIGY
AIYECPDKDE HLNKDFFRYH ASRARSKTFI NLREVSDRFK LPPGEYILIP STFEPHQEAD
FCLRIFSEKK AITRDMDGNV DIDLPEPPKP TPPDQETEEE QRFRALFEQV AGEDMEVTAE
ELEYVLNAVL QKKKDIKFKK LSLISCKNII SLMDTSGNGK LEFDEFKVFW DKLKQWINLF
LRFDADKSGT MSTYELRTAL KAAGFQLSSH LLQLIVLRYA DEELQLDFDD FLNCLVRLEN
ASRVFQALST KNKEFIHLNI NEFIHLTMNI
